Skip to main content
Erschienen in: Journal of Mammary Gland Biology and Neoplasia 3/2010

01.09.2010

Extracellular Matrix Composition Reveals Complex and Dynamic Stromal-Epithelial Interactions in the Mammary Gland

verfasst von: Ori Maller, Holly Martinson, Pepper Schedin

Erschienen in: Journal of Mammary Gland Biology and Neoplasia | Ausgabe 3/2010

Einloggen, um Zugang zu erhalten

Abstract

The mammary gland is an excellent model system to study the interplay between stroma and epithelial cells because of the gland’s unique postnatal development and its distinct functional states. This review focuses on the contribution of the extracellular matrix (ECM) to stromal-epithelial interactions in the mammary gland. We describe how ECM physical properties, protein composition, and proteolytic state impact mammary gland architecture as well as provide instructive cues that influence the function of mammary epithelial cells during pubertal gland development and throughout adulthood. Further, based on recent proteomic analyses of mammary ECM, we describe known mammary ECM proteins and their potential functions, as well as describe several ECM proteins not previously recognized in this organ. ECM proteins are discussed in the context of the morphologically-distinct stromal subcompartments: the basal lamina, the intra- and interlobular stroma, and the fibrous connective tissue. Future studies aimed at in-depth qualitative and quantitative characterization of mammary ECM within these various subcompartments is required to better elucidate the function of ECM in normal as well as in pathological breast tissue.
Literatur
1.
Zurück zum Zitat Schedin P, Mitrenga T, Kaeck M. Estrous cycle regulation of mammary epithelial cell proliferation, differentiation, and death in the Sprague-Dawley rat: a model for investigating the role of estrous cycling in mammary carcinogenesis. J Mammary Gland Biol Neoplasia. 2000;5(2):211–25.PubMedCrossRef Schedin P, Mitrenga T, Kaeck M. Estrous cycle regulation of mammary epithelial cell proliferation, differentiation, and death in the Sprague-Dawley rat: a model for investigating the role of estrous cycling in mammary carcinogenesis. J Mammary Gland Biol Neoplasia. 2000;5(2):211–25.PubMedCrossRef
2.
Zurück zum Zitat Fata JE, Chaudhary V, Khokha R. Cellular turnover in the mammary gland is correlated with systemic levels of progesterone and not 17beta-estradiol during the estrous cycle. Biol Reprod. 2001;65(3):680–8.PubMedCrossRef Fata JE, Chaudhary V, Khokha R. Cellular turnover in the mammary gland is correlated with systemic levels of progesterone and not 17beta-estradiol during the estrous cycle. Biol Reprod. 2001;65(3):680–8.PubMedCrossRef
3.
Zurück zum Zitat Ferguson DJ, Anderson TJ. Morphological evaluation of cell turnover in relation to the menstrual cycle in the “resting” human breast. Br J Cancer. 1981;44(2):177–81.PubMed Ferguson DJ, Anderson TJ. Morphological evaluation of cell turnover in relation to the menstrual cycle in the “resting” human breast. Br J Cancer. 1981;44(2):177–81.PubMed
4.
Zurück zum Zitat Ferguson JE, Schor AM, Howell A, Ferguson MW. Changes in the extracellular matrix of the normal human breast during the menstrual cycle. Cell Tissue Res. 1992;268(1):167–77.PubMedCrossRef Ferguson JE, Schor AM, Howell A, Ferguson MW. Changes in the extracellular matrix of the normal human breast during the menstrual cycle. Cell Tissue Res. 1992;268(1):167–77.PubMedCrossRef
5.
Zurück zum Zitat Robinson GW, McKnight RA, Smith GH, Hennighausen L. Mammary epithelial cells undergo secretory differentiation in cycling virgins but require pregnancy for the establishment of terminal differentiation. Development. 1995;121(7):2079–90.PubMed Robinson GW, McKnight RA, Smith GH, Hennighausen L. Mammary epithelial cells undergo secretory differentiation in cycling virgins but require pregnancy for the establishment of terminal differentiation. Development. 1995;121(7):2079–90.PubMed
6.
Zurück zum Zitat Bissell MJ, Barcellos-Hoff MH. The influence of extracellular matrix on gene expression: is structure the message? J Cell Sci Suppl. 1987;8:327–43.PubMed Bissell MJ, Barcellos-Hoff MH. The influence of extracellular matrix on gene expression: is structure the message? J Cell Sci Suppl. 1987;8:327–43.PubMed
7.
Zurück zum Zitat Butcher DT, Alliston T, Weaver VM. A tense situation: forcing tumour progression. Nat Rev Cancer. 2009;9(2):108–22.PubMedCrossRef Butcher DT, Alliston T, Weaver VM. A tense situation: forcing tumour progression. Nat Rev Cancer. 2009;9(2):108–22.PubMedCrossRef
8.
Zurück zum Zitat Vogel WF, Aszodi A, Alves F, Pawson T. Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development. Mol Cell Biol. 2001;21(8):2906–17.PubMedCrossRef Vogel WF, Aszodi A, Alves F, Pawson T. Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development. Mol Cell Biol. 2001;21(8):2906–17.PubMedCrossRef
9.
Zurück zum Zitat Scheele S, Falk M, Franzen A, Ellin F, Ferletta M, Lonai P, et al. Laminin alpha1 globular domains 4–5 induce fetal development but are not vital for embryonic basement membrane assembly. Proc Natl Acad Sci USA. 2005;102(5):1502–6.PubMedCrossRef Scheele S, Falk M, Franzen A, Ellin F, Ferletta M, Lonai P, et al. Laminin alpha1 globular domains 4–5 induce fetal development but are not vital for embryonic basement membrane assembly. Proc Natl Acad Sci USA. 2005;102(5):1502–6.PubMedCrossRef
10.
Zurück zum Zitat Midwood KS, Valenick LV, Hsia HC, Schwarzbauer JE. Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4. Mol Biol Cell. 2004;15(12):5670–7.PubMedCrossRef Midwood KS, Valenick LV, Hsia HC, Schwarzbauer JE. Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4. Mol Biol Cell. 2004;15(12):5670–7.PubMedCrossRef
11.
Zurück zum Zitat Shattil SJ, Kim C, Ginsberg MH. The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol 11(4):288–300. Shattil SJ, Kim C, Ginsberg MH. The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol 11(4):288–300.
13.
Zurück zum Zitat Desgrosellier JS, Cheresh DA. Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer 10(1):9-22. Desgrosellier JS, Cheresh DA. Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer 10(1):9-22.
14.
Zurück zum Zitat Larsen M, Artym VV, Green JA, Yamada KM. The matrix reorganized: extracellular matrix remodeling and integrin signaling. Curr Opin Cell Biol. 2006;18(5):463–71.PubMedCrossRef Larsen M, Artym VV, Green JA, Yamada KM. The matrix reorganized: extracellular matrix remodeling and integrin signaling. Curr Opin Cell Biol. 2006;18(5):463–71.PubMedCrossRef
15.
Zurück zum Zitat Ekblom P, Lonai P, Talts JF. Expression and biological role of laminin-1. Matrix Biol. 2003;22(1):35–47.PubMedCrossRef Ekblom P, Lonai P, Talts JF. Expression and biological role of laminin-1. Matrix Biol. 2003;22(1):35–47.PubMedCrossRef
16.
Zurück zum Zitat Kalluri R. Basement membranes: structure, assembly and role in tumour angiogenesis. Nat Rev Cancer. 2003;3(6):422–33.PubMedCrossRef Kalluri R. Basement membranes: structure, assembly and role in tumour angiogenesis. Nat Rev Cancer. 2003;3(6):422–33.PubMedCrossRef
17.
Zurück zum Zitat Jalkanen M, Rapraeger A, Bernfield M. Mouse mammary epithelial cells produce basement membrane and cell surface heparan sulfate proteoglycans containing distinct core proteins. J Cell Biol. 1988;106(3):953–62.PubMedCrossRef Jalkanen M, Rapraeger A, Bernfield M. Mouse mammary epithelial cells produce basement membrane and cell surface heparan sulfate proteoglycans containing distinct core proteins. J Cell Biol. 1988;106(3):953–62.PubMedCrossRef
18.
Zurück zum Zitat Bissell MJ, Hall HG, Parry G. How does the extracellular matrix direct gene expression? J Theor Biol. 1982;99(1):31–68.PubMedCrossRef Bissell MJ, Hall HG, Parry G. How does the extracellular matrix direct gene expression? J Theor Biol. 1982;99(1):31–68.PubMedCrossRef
19.
Zurück zum Zitat Masso-Welch PA, Darcy KM, Stangle-Castor NC, Ip MM. A developmental atlas of rat mammary gland histology. J Mammary Gland Biol Neoplasia. 2000;5(2):165–85.PubMedCrossRef Masso-Welch PA, Darcy KM, Stangle-Castor NC, Ip MM. A developmental atlas of rat mammary gland histology. J Mammary Gland Biol Neoplasia. 2000;5(2):165–85.PubMedCrossRef
20.
Zurück zum Zitat Silberstein GB, Daniel CW. Glycosaminoglycans in the basal lamina and extracellular matrix of the developing mouse mammary duct. Dev Biol. 1982;90(1):215–22.PubMedCrossRef Silberstein GB, Daniel CW. Glycosaminoglycans in the basal lamina and extracellular matrix of the developing mouse mammary duct. Dev Biol. 1982;90(1):215–22.PubMedCrossRef
21.
Zurück zum Zitat Nandi S, Guzman RC, Yang J. Hormones and mammary carcinogenesis in mice, rats, and humans: a unifying hypothesis. Proc Natl Acad Sci USA. 1995;92(9):3650–7.PubMedCrossRef Nandi S, Guzman RC, Yang J. Hormones and mammary carcinogenesis in mice, rats, and humans: a unifying hypothesis. Proc Natl Acad Sci USA. 1995;92(9):3650–7.PubMedCrossRef
22.
Zurück zum Zitat Hattar R, Maller O, McDaniel S, Hansen KC, Hedman KJ, Lyons TR, et al. Tamoxifen induces pleiotrophic changes in mammary stroma resulting in extracellular matrix that suppresses transformed phenotypes. Breast Cancer Res. 2009;11(1):R5.PubMedCrossRef Hattar R, Maller O, McDaniel S, Hansen KC, Hedman KJ, Lyons TR, et al. Tamoxifen induces pleiotrophic changes in mammary stroma resulting in extracellular matrix that suppresses transformed phenotypes. Breast Cancer Res. 2009;11(1):R5.PubMedCrossRef
23.
Zurück zum Zitat Schedin P, Mitrenga T, McDaniel S, Kaeck M. Mammary ECM composition and function are altered by reproductive state. Mol Carcinog. 2004;41(4):207–20.PubMedCrossRef Schedin P, Mitrenga T, McDaniel S, Kaeck M. Mammary ECM composition and function are altered by reproductive state. Mol Carcinog. 2004;41(4):207–20.PubMedCrossRef
24.
Zurück zum Zitat Woodward TL, Mienaltowski AS, Modi RR, Bennett JM, Haslam SZ. Fibronectin and the alpha(5)beta(1) integrin are under developmental and ovarian steroid regulation in the normal mouse mammary gland. Endocrinology. 2001;142(7):3214–22.PubMedCrossRef Woodward TL, Mienaltowski AS, Modi RR, Bennett JM, Haslam SZ. Fibronectin and the alpha(5)beta(1) integrin are under developmental and ovarian steroid regulation in the normal mouse mammary gland. Endocrinology. 2001;142(7):3214–22.PubMedCrossRef
25.
Zurück zum Zitat DeMali KA, Wennerberg K, Burridge K. Integrin signaling to the actin cytoskeleton. Curr Opin Cell Biol. 2003;15(5):572–82.PubMedCrossRef DeMali KA, Wennerberg K, Burridge K. Integrin signaling to the actin cytoskeleton. Curr Opin Cell Biol. 2003;15(5):572–82.PubMedCrossRef
26.
Zurück zum Zitat Paszek MJ, Zahir N, Johnson KR, Lakins JN, Rozenberg GI, Gefen A, et al. Tensional homeostasis and the malignant phenotype. Cancer Cell. 2005;8(3):241–54.PubMedCrossRef Paszek MJ, Zahir N, Johnson KR, Lakins JN, Rozenberg GI, Gefen A, et al. Tensional homeostasis and the malignant phenotype. Cancer Cell. 2005;8(3):241–54.PubMedCrossRef
27.
Zurück zum Zitat Provenzano PP, Inman DR, Eliceiri KW, Keely PJ. Matrix density-induced mechanoregulation of breast cell phenotype, signaling and gene expression through a FAK-ERK linkage. Oncogene. 2009;28(49):4326–43.PubMedCrossRef Provenzano PP, Inman DR, Eliceiri KW, Keely PJ. Matrix density-induced mechanoregulation of breast cell phenotype, signaling and gene expression through a FAK-ERK linkage. Oncogene. 2009;28(49):4326–43.PubMedCrossRef
28.
Zurück zum Zitat Levental KR, Yu H, Kass L, Lakins JN, Egeblad M, Erler JT, et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell. 2009;139(5):891–906.PubMedCrossRef Levental KR, Yu H, Kass L, Lakins JN, Egeblad M, Erler JT, et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell. 2009;139(5):891–906.PubMedCrossRef
29.
Zurück zum Zitat Engler AJ, Sen S, Sweeney HL, Discher DE. Matrix elasticity directs stem cell lineage specification. Cell. 2006;126(4):677–89.PubMedCrossRef Engler AJ, Sen S, Sweeney HL, Discher DE. Matrix elasticity directs stem cell lineage specification. Cell. 2006;126(4):677–89.PubMedCrossRef
30.
Zurück zum Zitat Taddei I, Deugnier MA, Faraldo MM, Petit V, Bouvard D, Medina D, et al. Beta1 integrin deletion from the basal compartment of the mammary epithelium affects stem cells. Nat Cell Biol. 2008;10(6):716–22.PubMedCrossRef Taddei I, Deugnier MA, Faraldo MM, Petit V, Bouvard D, Medina D, et al. Beta1 integrin deletion from the basal compartment of the mammary epithelium affects stem cells. Nat Cell Biol. 2008;10(6):716–22.PubMedCrossRef
31.
Zurück zum Zitat Mecham RP, Heuser JE. The elastic fiber. In: Hay ED (ed). Cell Biology of Extracellular Matrix: Plenum 1991; p. 79–109. Mecham RP, Heuser JE. The elastic fiber. In: Hay ED (ed). Cell Biology of Extracellular Matrix: Plenum 1991; p. 79–109.
32.
Zurück zum Zitat Linsenmayer TF. Collagen. In: Hay ED, editor. Cell biology of extracellular matrix. NY: Plenum; 1991. p. 7–44. Linsenmayer TF. Collagen. In: Hay ED, editor. Cell biology of extracellular matrix. NY: Plenum; 1991. p. 7–44.
33.
Zurück zum Zitat Szauter KM, Cao T, Boyd CD, Csiszar K. Lysyl oxidase in development, aging and pathologies of the skin. Pathol Biol (Paris). 2005;53(7):448–56. Szauter KM, Cao T, Boyd CD, Csiszar K. Lysyl oxidase in development, aging and pathologies of the skin. Pathol Biol (Paris). 2005;53(7):448–56.
34.
Zurück zum Zitat Lorand L, Graham RM. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol. 2003;4(2):140–56.PubMedCrossRef Lorand L, Graham RM. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol. 2003;4(2):140–56.PubMedCrossRef
35.
Zurück zum Zitat Nunes I, Gleizes PE, Metz CN, Rifkin DB. Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta. J Cell Biol. 1997;136(5):1151–63.PubMedCrossRef Nunes I, Gleizes PE, Metz CN, Rifkin DB. Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta. J Cell Biol. 1997;136(5):1151–63.PubMedCrossRef
36.
Zurück zum Zitat Williams JM, Daniel CW. Mammary ductal elongation: differentiation of myoepithelium and basal lamina during branching morphogenesis. Dev Biol. 1983;97(2):274–90.PubMedCrossRef Williams JM, Daniel CW. Mammary ductal elongation: differentiation of myoepithelium and basal lamina during branching morphogenesis. Dev Biol. 1983;97(2):274–90.PubMedCrossRef
37.
Zurück zum Zitat Fata JE, Werb Z, Bissell MJ. Regulation of mammary gland branching morphogenesis by the extracellular matrix and its remodeling enzymes. Breast Cancer Res. 2004;6(1):1–11.PubMed Fata JE, Werb Z, Bissell MJ. Regulation of mammary gland branching morphogenesis by the extracellular matrix and its remodeling enzymes. Breast Cancer Res. 2004;6(1):1–11.PubMed
38.
Zurück zum Zitat Discher DE, Mooney DJ, Zandstra PW. Growth factors, matrices, and forces combine and control stem cells. Science. 2009;324(5935):1673–7.PubMedCrossRef Discher DE, Mooney DJ, Zandstra PW. Growth factors, matrices, and forces combine and control stem cells. Science. 2009;324(5935):1673–7.PubMedCrossRef
39.
Zurück zum Zitat Hynes RO. The extracellular matrix: not just pretty fibrils. Science. 2009;326(5957):1216–9.PubMedCrossRef Hynes RO. The extracellular matrix: not just pretty fibrils. Science. 2009;326(5957):1216–9.PubMedCrossRef
40.
Zurück zum Zitat Taipale J, Miyazono K, Heldin CH, Keski-Oja J. Latent transforming growth factor-beta 1 associates to fibroblast extracellular matrix via latent TGF-beta binding protein. J Cell Biol. 1994;124(1–2):171–81.PubMedCrossRef Taipale J, Miyazono K, Heldin CH, Keski-Oja J. Latent transforming growth factor-beta 1 associates to fibroblast extracellular matrix via latent TGF-beta binding protein. J Cell Biol. 1994;124(1–2):171–81.PubMedCrossRef
41.
Zurück zum Zitat Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000;14(2):163–76.PubMed Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000;14(2):163–76.PubMed
42.
Zurück zum Zitat Munger JS, Huang X, Kawakatsu H, Griffiths MJ, Dalton SL, Wu J, et al. The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis. Cell. 1999;96(3):319–28.PubMedCrossRef Munger JS, Huang X, Kawakatsu H, Griffiths MJ, Dalton SL, Wu J, et al. The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis. Cell. 1999;96(3):319–28.PubMedCrossRef
43.
Zurück zum Zitat Wipff PJ, Rifkin DB, Meister JJ, Hinz B. Myofibroblast contraction activates latent TGF-beta1 from the extracellular matrix. J Cell Biol. 2007;179(6):1311–23.PubMedCrossRef Wipff PJ, Rifkin DB, Meister JJ, Hinz B. Myofibroblast contraction activates latent TGF-beta1 from the extracellular matrix. J Cell Biol. 2007;179(6):1311–23.PubMedCrossRef
44.
Zurück zum Zitat Sawhney RK, Howard J. Slow local movements of collagen fibers by fibroblasts drive the rapid global self-organization of collagen gels. J Cell Biol. 2002;157(6):1083–91.PubMedCrossRef Sawhney RK, Howard J. Slow local movements of collagen fibers by fibroblasts drive the rapid global self-organization of collagen gels. J Cell Biol. 2002;157(6):1083–91.PubMedCrossRef
45.
Zurück zum Zitat Harris AK, Stopak D, Wild P. Fibroblast traction as a mechanism for collagen morphogenesis. Nature. 1981;290(5803):249–51.PubMedCrossRef Harris AK, Stopak D, Wild P. Fibroblast traction as a mechanism for collagen morphogenesis. Nature. 1981;290(5803):249–51.PubMedCrossRef
46.
Zurück zum Zitat Silberstein GB, Strickland P, Coleman S, Daniel CW. Epithelium-dependent extracellular matrix synthesis in transforming growth factor-beta 1-growth-inhibited mouse mammary gland. J Cell Biol. 1990;110(6):2209–19.PubMedCrossRef Silberstein GB, Strickland P, Coleman S, Daniel CW. Epithelium-dependent extracellular matrix synthesis in transforming growth factor-beta 1-growth-inhibited mouse mammary gland. J Cell Biol. 1990;110(6):2209–19.PubMedCrossRef
47.
Zurück zum Zitat Daniel CW, Silberstein GB, Van Horn K, Strickland P, Robinson S. TGF-beta 1-induced inhibition of mouse mammary ductal growth: developmental specificity and characterization. Dev Biol. 1989;135(1):20–30.PubMedCrossRef Daniel CW, Silberstein GB, Van Horn K, Strickland P, Robinson S. TGF-beta 1-induced inhibition of mouse mammary ductal growth: developmental specificity and characterization. Dev Biol. 1989;135(1):20–30.PubMedCrossRef
48.
Zurück zum Zitat Robinson SD, Silberstein GB, Roberts AB, Flanders KC, Daniel CW. Regulated expression and growth inhibitory effects of transforming growth factor-beta isoforms in mouse mammary gland development. Development. 1991;113(3):867–78.PubMed Robinson SD, Silberstein GB, Roberts AB, Flanders KC, Daniel CW. Regulated expression and growth inhibitory effects of transforming growth factor-beta isoforms in mouse mammary gland development. Development. 1991;113(3):867–78.PubMed
49.
Zurück zum Zitat Pierce Jr DF, Johnson MD, Matsui Y, Robinson SD, Gold LI, Purchio AF, et al. Genes Dev. 1993;7(12A):2308–17.PubMedCrossRef Pierce Jr DF, Johnson MD, Matsui Y, Robinson SD, Gold LI, Purchio AF, et al. Genes Dev. 1993;7(12A):2308–17.PubMedCrossRef
50.
Zurück zum Zitat Robinson SD, Roberts AB, Daniel CW. TGF beta suppresses casein synthesis in mouse mammary explants and may play a role in controlling milk levels during pregnancy. J Cell Biol. 1993;120(1):245–51.PubMedCrossRef Robinson SD, Roberts AB, Daniel CW. TGF beta suppresses casein synthesis in mouse mammary explants and may play a role in controlling milk levels during pregnancy. J Cell Biol. 1993;120(1):245–51.PubMedCrossRef
51.
Zurück zum Zitat Wu WJ, Lee CF, Hsin CH, Du JY, Hsu TC, Lin TH, et al. TGF-beta inhibits prolactin-induced expression of beta-casein by a Smad3-dependent mechanism. J Cell Biochem. 2008;104(5):1647–59.PubMedCrossRef Wu WJ, Lee CF, Hsin CH, Du JY, Hsu TC, Lin TH, et al. TGF-beta inhibits prolactin-induced expression of beta-casein by a Smad3-dependent mechanism. J Cell Biochem. 2008;104(5):1647–59.PubMedCrossRef
52.
Zurück zum Zitat Schedin P, O’Brien J, Rudolph M, Stein T, Borges V. Microenvironment of the involuting mammary gland mediates mammary cancer progression. J Mammary Gland Biol Neoplasia. 2007;12(1):71–82.PubMedCrossRef Schedin P, O’Brien J, Rudolph M, Stein T, Borges V. Microenvironment of the involuting mammary gland mediates mammary cancer progression. J Mammary Gland Biol Neoplasia. 2007;12(1):71–82.PubMedCrossRef
53.
Zurück zum Zitat Faure E, Heisterkamp N, Groffen J, Kaartinen V. Differential expression of TGF-beta isoforms during postlactational mammary gland involution. Cell Tissue Res. 2000;300(1):89–95.PubMed Faure E, Heisterkamp N, Groffen J, Kaartinen V. Differential expression of TGF-beta isoforms during postlactational mammary gland involution. Cell Tissue Res. 2000;300(1):89–95.PubMed
54.
Zurück zum Zitat Kim ES, Sohn YW, Moon A. TGF-beta-induced transcriptional activation of MMP-2 is mediated by activating transcription factor (ATF)2 in human breast epithelial cells. Cancer Lett. 2007;252(1):147–56.PubMedCrossRef Kim ES, Sohn YW, Moon A. TGF-beta-induced transcriptional activation of MMP-2 is mediated by activating transcription factor (ATF)2 in human breast epithelial cells. Cancer Lett. 2007;252(1):147–56.PubMedCrossRef
55.
Zurück zum Zitat Bierie B, Moses HL. Transforming growth factor beta (TGF-beta) and inflammation in cancer. Cytokine Growth Factor Rev 21(1):49–59. Bierie B, Moses HL. Transforming growth factor beta (TGF-beta) and inflammation in cancer. Cytokine Growth Factor Rev 21(1):49–59.
56.
Zurück zum Zitat Adair-Kirk TL, Senior RM. Fragments of extracellular matrix as mediators of inflammation. Int J Biochem Cell Biol. 2008;40(6–7):1101–10.PubMedCrossRef Adair-Kirk TL, Senior RM. Fragments of extracellular matrix as mediators of inflammation. Int J Biochem Cell Biol. 2008;40(6–7):1101–10.PubMedCrossRef
57.
Zurück zum Zitat Schenk S, Quaranta V. Tales from the crypt[ic] sites of the extracellular matrix. Trends Cell Biol. 2003;13(7):366–75.PubMedCrossRef Schenk S, Quaranta V. Tales from the crypt[ic] sites of the extracellular matrix. Trends Cell Biol. 2003;13(7):366–75.PubMedCrossRef
58.
Zurück zum Zitat Schedin P, Strange R, Mitrenga T, Wolfe P, Kaeck M. Fibronectin fragments induce MMP activity in mouse mammary epithelial cells: evidence for a role in mammary tissue remodeling. J Cell Sci. 2000;113(Pt 5):795–806.PubMed Schedin P, Strange R, Mitrenga T, Wolfe P, Kaeck M. Fibronectin fragments induce MMP activity in mouse mammary epithelial cells: evidence for a role in mammary tissue remodeling. J Cell Sci. 2000;113(Pt 5):795–806.PubMed
59.
Zurück zum Zitat Williams CM, Engler AJ, Slone RD, Galante LL, Schwarzbauer JE. Fibronectin expression modulates mammary epithelial cell proliferation during acinar differentiation. Cancer Res. 2008;68(9):3185–92.PubMedCrossRef Williams CM, Engler AJ, Slone RD, Galante LL, Schwarzbauer JE. Fibronectin expression modulates mammary epithelial cell proliferation during acinar differentiation. Cancer Res. 2008;68(9):3185–92.PubMedCrossRef
60.
Zurück zum Zitat Friedland JC, Lee MH, Boettiger D. Mechanically activated integrin switch controls alpha5beta1 function. Science. 2009;323(5914):642–4.PubMedCrossRef Friedland JC, Lee MH, Boettiger D. Mechanically activated integrin switch controls alpha5beta1 function. Science. 2009;323(5914):642–4.PubMedCrossRef
61.
Zurück zum Zitat Liang X, Huuskonen J, Hajivandi M, Manzanedo R, Predki P, Amshey JR, et al. Identification and quantification of proteins differentially secreted by a pair of normal and malignant breast-cancer cell lines. Proteomics. 2009;9(1):182–93.PubMedCrossRef Liang X, Huuskonen J, Hajivandi M, Manzanedo R, Predki P, Amshey JR, et al. Identification and quantification of proteins differentially secreted by a pair of normal and malignant breast-cancer cell lines. Proteomics. 2009;9(1):182–93.PubMedCrossRef
62.
Zurück zum Zitat Hansen KC, Kiemele L, Maller O, O’Brien J, Shankar A, Fornetti J, et al. An in-solution ultrasonication-assisted digestion method for improved extracellular matrix proteome coverage. Mol Cell Proteomics. 2009;8(7):1648–57.PubMedCrossRef Hansen KC, Kiemele L, Maller O, O’Brien J, Shankar A, Fornetti J, et al. An in-solution ultrasonication-assisted digestion method for improved extracellular matrix proteome coverage. Mol Cell Proteomics. 2009;8(7):1648–57.PubMedCrossRef
63.
Zurück zum Zitat Farquhar MG. The glomerular basement membrane: A selective macromolecular fliter. In: Hay ED, editor. Cell biology extracellular matrix. NY: Plenum; 1991. Farquhar MG. The glomerular basement membrane: A selective macromolecular fliter. In: Hay ED, editor. Cell biology extracellular matrix. NY: Plenum; 1991.
64.
Zurück zum Zitat Li S, Edgar D, Fassler R, Wadsworth W, Yurchenco PD. The role of laminin in embryonic cell polarization and tissue organization. Dev Cell. 2003;4(5):613–24.PubMedCrossRef Li S, Edgar D, Fassler R, Wadsworth W, Yurchenco PD. The role of laminin in embryonic cell polarization and tissue organization. Dev Cell. 2003;4(5):613–24.PubMedCrossRef
65.
Zurück zum Zitat Tzu J, Marinkovich MP. Bridging structure with function: structural, regulatory, and developmental role of laminins. Int J Biochem Cell Biol. 2008;40(2):199–214.PubMedCrossRef Tzu J, Marinkovich MP. Bridging structure with function: structural, regulatory, and developmental role of laminins. Int J Biochem Cell Biol. 2008;40(2):199–214.PubMedCrossRef
66.
Zurück zum Zitat Hallmann R, Horn N, Selg M, Wendler O, Pausch F, Sorokin LM. Expression and function of laminins in the embryonic and mature vasculature. Physiol Rev. 2005;85(3):979–1000.PubMedCrossRef Hallmann R, Horn N, Selg M, Wendler O, Pausch F, Sorokin LM. Expression and function of laminins in the embryonic and mature vasculature. Physiol Rev. 2005;85(3):979–1000.PubMedCrossRef
67.
Zurück zum Zitat Francoeur C, Escaffit F, Vachon PH, Beaulieu JF. Proinflammatory cytokines TNF-alpha and IFN-gamma alter laminin expression under an apoptosis-independent mechanism in human intestinal epithelial cells. Am J Physiol Gastrointest Liver Physiol. 2004;287(3):G592–8.PubMedCrossRef Francoeur C, Escaffit F, Vachon PH, Beaulieu JF. Proinflammatory cytokines TNF-alpha and IFN-gamma alter laminin expression under an apoptosis-independent mechanism in human intestinal epithelial cells. Am J Physiol Gastrointest Liver Physiol. 2004;287(3):G592–8.PubMedCrossRef
68.
Zurück zum Zitat Kleinman HK, Martin GR. Matrigel: basement membrane matrix with biological activity. Semin Cancer Biol. 2005;15(5):378–86.PubMedCrossRef Kleinman HK, Martin GR. Matrigel: basement membrane matrix with biological activity. Semin Cancer Biol. 2005;15(5):378–86.PubMedCrossRef
69.
Zurück zum Zitat Timpl R, Rohde H, Robey PG, Rennard SI, Foidart JM, Martin GR. Laminin–a glycoprotein from basement membranes. J Biol Chem. 1979;254(19):9933–7.PubMed Timpl R, Rohde H, Robey PG, Rennard SI, Foidart JM, Martin GR. Laminin–a glycoprotein from basement membranes. J Biol Chem. 1979;254(19):9933–7.PubMed
70.
Zurück zum Zitat Miner JH, Li C, Mudd JL, Go G, Sutherland AE. Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation. Development. 2004;131(10):2247–56.PubMedCrossRef Miner JH, Li C, Mudd JL, Go G, Sutherland AE. Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation. Development. 2004;131(10):2247–56.PubMedCrossRef
71.
Zurück zum Zitat Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, et al. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol. 1999;144(1):151–60.PubMedCrossRef Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, et al. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol. 1999;144(1):151–60.PubMedCrossRef
72.
Zurück zum Zitat Hohenester E, Tisi D, Talts JF, Timpl R. The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell. 1999;4(5):783–92.PubMedCrossRef Hohenester E, Tisi D, Talts JF, Timpl R. The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell. 1999;4(5):783–92.PubMedCrossRef
73.
Zurück zum Zitat Streuli CH, Bailey N, Bissell MJ. Control of mammary epithelial differentiation: basement membrane induces tissue-specific gene expression in the absence of cell-cell interaction and morphological polarity. J Cell Biol. 1991;115(5):1383–95.PubMedCrossRef Streuli CH, Bailey N, Bissell MJ. Control of mammary epithelial differentiation: basement membrane induces tissue-specific gene expression in the absence of cell-cell interaction and morphological polarity. J Cell Biol. 1991;115(5):1383–95.PubMedCrossRef
74.
Zurück zum Zitat Li ML, Aggeler J, Farson DA, Hatier C, Hassell J, Bissell MJ. Influence of a reconstituted basement membrane and its components on casein gene expression and secretion in mouse mammary epithelial cells. Proc Natl Acad Sci USA. 1987;84(1):136–40.PubMedCrossRef Li ML, Aggeler J, Farson DA, Hatier C, Hassell J, Bissell MJ. Influence of a reconstituted basement membrane and its components on casein gene expression and secretion in mouse mammary epithelial cells. Proc Natl Acad Sci USA. 1987;84(1):136–40.PubMedCrossRef
75.
Zurück zum Zitat Bissell MJ, Kenny PA, Radisky DC. Microenvironmental regulators of tissue structure and function also regulate tumor induction and progression: the role of extracellular matrix and its degrading enzymes. Cold Spring Harb Symp Quant Biol. 2005;70:343–56.PubMedCrossRef Bissell MJ, Kenny PA, Radisky DC. Microenvironmental regulators of tissue structure and function also regulate tumor induction and progression: the role of extracellular matrix and its degrading enzymes. Cold Spring Harb Symp Quant Biol. 2005;70:343–56.PubMedCrossRef
76.
Zurück zum Zitat Gudjonsson T, Ronnov-Jessen L, Villadsen R, Rank F, Bissell MJ, Petersen OW. Normal and tumor-derived myoepithelial cells differ in their ability to interact with luminal breast epithelial cells for polarity and basement membrane deposition. J Cell Sci. 2002;115(Pt 1):39–50.PubMed Gudjonsson T, Ronnov-Jessen L, Villadsen R, Rank F, Bissell MJ, Petersen OW. Normal and tumor-derived myoepithelial cells differ in their ability to interact with luminal breast epithelial cells for polarity and basement membrane deposition. J Cell Sci. 2002;115(Pt 1):39–50.PubMed
77.
Zurück zum Zitat Debnath J, Muthuswamy SK, Brugge JS. Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures. Methods. 2003;30(3):256–68.PubMedCrossRef Debnath J, Muthuswamy SK, Brugge JS. Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures. Methods. 2003;30(3):256–68.PubMedCrossRef
78.
Zurück zum Zitat Petersen OW, Ronnov-Jessen L, Howlett AR, Bissell MJ. Interaction with basement membrane serves to rapidly distinguish growth and differentiation pattern of normal and malignant human breast epithelial cells. Proc Natl Acad Sci USA. 1992;89(19):9064–8.PubMedCrossRef Petersen OW, Ronnov-Jessen L, Howlett AR, Bissell MJ. Interaction with basement membrane serves to rapidly distinguish growth and differentiation pattern of normal and malignant human breast epithelial cells. Proc Natl Acad Sci USA. 1992;89(19):9064–8.PubMedCrossRef
79.
Zurück zum Zitat Marinkovich MP. Tumour microenvironment: laminin 332 in squamous-cell carcinoma. Nat Rev Cancer. 2007;7(5):370–80.PubMedCrossRef Marinkovich MP. Tumour microenvironment: laminin 332 in squamous-cell carcinoma. Nat Rev Cancer. 2007;7(5):370–80.PubMedCrossRef
80.
Zurück zum Zitat Ewald AJ, Brenot A, Duong M, Chan BS, Werb Z. Collective epithelial migration and cell rearrangements drive mammary branching morphogenesis. Dev Cell. 2008;14(4):570–81.PubMedCrossRef Ewald AJ, Brenot A, Duong M, Chan BS, Werb Z. Collective epithelial migration and cell rearrangements drive mammary branching morphogenesis. Dev Cell. 2008;14(4):570–81.PubMedCrossRef
81.
Zurück zum Zitat Schenk S, Hintermann E, Bilban M, Koshikawa N, Hojilla C, Khokha R, et al. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J Cell Biol. 2003;161(1):197–209.PubMedCrossRef Schenk S, Hintermann E, Bilban M, Koshikawa N, Hojilla C, Khokha R, et al. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J Cell Biol. 2003;161(1):197–209.PubMedCrossRef
82.
Zurück zum Zitat Giannelli G, Falk-Marzillier J, Schiraldi O, Stetler-Stevenson WG, Quaranta V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science. 1997;277(5323):225–8.PubMedCrossRef Giannelli G, Falk-Marzillier J, Schiraldi O, Stetler-Stevenson WG, Quaranta V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science. 1997;277(5323):225–8.PubMedCrossRef
83.
Zurück zum Zitat Yurchenco PD, Ruben GC. Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network. J Cell Biol. 1987;105(6 Pt 1):2559–68.PubMedCrossRef Yurchenco PD, Ruben GC. Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network. J Cell Biol. 1987;105(6 Pt 1):2559–68.PubMedCrossRef
84.
Zurück zum Zitat Poschl E, Schlotzer-Schrehardt U, Brachvogel B, Saito K, Ninomiya Y, Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development. 2004;131(7):1619–28.PubMedCrossRef Poschl E, Schlotzer-Schrehardt U, Brachvogel B, Saito K, Ninomiya Y, Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development. 2004;131(7):1619–28.PubMedCrossRef
85.
Zurück zum Zitat Yurchenco PD, Schittny JC. Molecular architecture of basement membranes. Faseb J. 1990;4(6):1577–90.PubMed Yurchenco PD, Schittny JC. Molecular architecture of basement membranes. Faseb J. 1990;4(6):1577–90.PubMed
86.
Zurück zum Zitat Kalluri R, Shield CF, Todd P, Hudson BG, Neilson EG. Isoform switching of type IV collagen is developmentally arrested in X-linked Alport syndrome leading to increased susceptibility of renal basement membranes to endoproteolysis. J Clin Invest. 1997;99(10):2470–8.PubMedCrossRef Kalluri R, Shield CF, Todd P, Hudson BG, Neilson EG. Isoform switching of type IV collagen is developmentally arrested in X-linked Alport syndrome leading to increased susceptibility of renal basement membranes to endoproteolysis. J Clin Invest. 1997;99(10):2470–8.PubMedCrossRef
87.
Zurück zum Zitat Khoshnoodi J, Pedchenko V, Hudson BG. Mammalian collagen IV. Microsc Res Tech. 2008;71(5):357–70.PubMedCrossRef Khoshnoodi J, Pedchenko V, Hudson BG. Mammalian collagen IV. Microsc Res Tech. 2008;71(5):357–70.PubMedCrossRef
88.
Zurück zum Zitat Wicha MS, Liotta LA, Vonderhaar BK, Kidwell WR. Effects of inhibition of basement membrane collagen deposition on rat mammary gland development. Dev Biol. 1980;80(2):253–6.PubMedCrossRef Wicha MS, Liotta LA, Vonderhaar BK, Kidwell WR. Effects of inhibition of basement membrane collagen deposition on rat mammary gland development. Dev Biol. 1980;80(2):253–6.PubMedCrossRef
89.
Zurück zum Zitat Wicha MS, Liotta LA, Garbisa S, Kidwell WR. Basement membrane collagen requirements for attachment and growth of mammary epithelium. Exp Cell Res. 1979;124(1):181–90.PubMedCrossRef Wicha MS, Liotta LA, Garbisa S, Kidwell WR. Basement membrane collagen requirements for attachment and growth of mammary epithelium. Exp Cell Res. 1979;124(1):181–90.PubMedCrossRef
90.
Zurück zum Zitat Marneros AG, Olsen BR. The role of collagen-derived proteolytic fragments in angiogenesis. Matrix Biol. 2001;20(5–6):337–45.PubMedCrossRef Marneros AG, Olsen BR. The role of collagen-derived proteolytic fragments in angiogenesis. Matrix Biol. 2001;20(5–6):337–45.PubMedCrossRef
91.
Zurück zum Zitat Mundel TM, Kalluri R. Type IV collagen-derived angiogenesis inhibitors. Microvasc Res. 2007;74(2–3):85–9.PubMedCrossRef Mundel TM, Kalluri R. Type IV collagen-derived angiogenesis inhibitors. Microvasc Res. 2007;74(2–3):85–9.PubMedCrossRef
92.
Zurück zum Zitat Djonov V, Andres AC, Ziemiecki A. Vascular remodelling during the normal and malignant life cycle of the mammary gland. Microsc Res Tech. 2001;52(2):182–9.PubMedCrossRef Djonov V, Andres AC, Ziemiecki A. Vascular remodelling during the normal and malignant life cycle of the mammary gland. Microsc Res Tech. 2001;52(2):182–9.PubMedCrossRef
93.
Zurück zum Zitat Nischt R, Schmidt C, Mirancea N, Baranowsky A, Mokkapati S, Smyth N, et al. Lack of nidogen-1 and -2 prevents basement membrane assembly in skin-organotypic coculture. J Invest Dermatol. 2007;127(3):545–54.PubMedCrossRef Nischt R, Schmidt C, Mirancea N, Baranowsky A, Mokkapati S, Smyth N, et al. Lack of nidogen-1 and -2 prevents basement membrane assembly in skin-organotypic coculture. J Invest Dermatol. 2007;127(3):545–54.PubMedCrossRef
94.
Zurück zum Zitat Bose K, Nischt R, Page A, Bader BL, Paulsson M, Smyth N. Loss of nidogen-1 and -2 results in syndactyly and changes in limb development. J Biol Chem. 2006;281(51):39620–9.PubMedCrossRef Bose K, Nischt R, Page A, Bader BL, Paulsson M, Smyth N. Loss of nidogen-1 and -2 results in syndactyly and changes in limb development. J Biol Chem. 2006;281(51):39620–9.PubMedCrossRef
95.
Zurück zum Zitat Kohling R, Nischt R, Vasudevan A, Ho M, Weiergraber M, Schneider T, et al. Nidogen and nidogen-associated basement membrane proteins and neuronal plasticity. Neurodegener Dis. 2006;3(1–2):56–61.PubMed Kohling R, Nischt R, Vasudevan A, Ho M, Weiergraber M, Schneider T, et al. Nidogen and nidogen-associated basement membrane proteins and neuronal plasticity. Neurodegener Dis. 2006;3(1–2):56–61.PubMed
96.
Zurück zum Zitat Ekblom P, Ekblom M, Fecker L, Klein G, Zhang HY, Kadoya Y, et al. Role of mesenchymal nidogen for epithelial morphogenesis in vitro. Development. 1994;120(7):2003–14.PubMed Ekblom P, Ekblom M, Fecker L, Klein G, Zhang HY, Kadoya Y, et al. Role of mesenchymal nidogen for epithelial morphogenesis in vitro. Development. 1994;120(7):2003–14.PubMed
97.
Zurück zum Zitat Fox JW, Mayer U, Nischt R, Aumailley M, Reinhardt D, Wiedemann H, et al. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. Embo J. 1991;10(11):3137–46.PubMed Fox JW, Mayer U, Nischt R, Aumailley M, Reinhardt D, Wiedemann H, et al. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. Embo J. 1991;10(11):3137–46.PubMed
98.
Zurück zum Zitat Mayer U, Nischt R, Poschl E, Mann K, Fukuda K, Gerl M, et al. A single EGF-like motif of laminin is responsible for high affinity nidogen binding. Embo J. 1993;12(5):1879–85.PubMed Mayer U, Nischt R, Poschl E, Mann K, Fukuda K, Gerl M, et al. A single EGF-like motif of laminin is responsible for high affinity nidogen binding. Embo J. 1993;12(5):1879–85.PubMed
99.
Zurück zum Zitat Reinhardt D, Mann K, Nischt R, Fox JW, Chu ML, Krieg T, et al. Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc. J Biol Chem. 1993;268(15):10881–7.PubMed Reinhardt D, Mann K, Nischt R, Fox JW, Chu ML, Krieg T, et al. Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc. J Biol Chem. 1993;268(15):10881–7.PubMed
100.
Zurück zum Zitat Murshed M, Smyth N, Miosge N, Karolat J, Krieg T, Paulsson M, et al. The absence of nidogen 1 does not affect murine basement membrane formation. Mol Cell Biol. 2000;20(18):7007–12.PubMedCrossRef Murshed M, Smyth N, Miosge N, Karolat J, Krieg T, Paulsson M, et al. The absence of nidogen 1 does not affect murine basement membrane formation. Mol Cell Biol. 2000;20(18):7007–12.PubMedCrossRef
101.
Zurück zum Zitat Miosge N, Sasaki T, Timpl R. Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice. Matrix Biol. 2002;21(7):611–21.PubMedCrossRef Miosge N, Sasaki T, Timpl R. Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice. Matrix Biol. 2002;21(7):611–21.PubMedCrossRef
102.
Zurück zum Zitat Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkapati S, et al. Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol Cell Biol. 2005;25(15):6846–56.PubMedCrossRef Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkapati S, et al. Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol Cell Biol. 2005;25(15):6846–56.PubMedCrossRef
103.
Zurück zum Zitat Pujuguet P, Simian M, Liaw J, Timpl R, Werb Z, Bissell MJ. Nidogen-1 regulates laminin-1-dependent mammary-specific gene expression. J Cell Sci. 2000;113(Pt 5):849–58.PubMed Pujuguet P, Simian M, Liaw J, Timpl R, Werb Z, Bissell MJ. Nidogen-1 regulates laminin-1-dependent mammary-specific gene expression. J Cell Sci. 2000;113(Pt 5):849–58.PubMed
104.
Zurück zum Zitat Friedrich MV, Gohring W, Morgelin M, Brancaccio A, David G, Timpl R. Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V. J Mol Biol. 1999;294(1):259–70.PubMedCrossRef Friedrich MV, Gohring W, Morgelin M, Brancaccio A, David G, Timpl R. Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V. J Mol Biol. 1999;294(1):259–70.PubMedCrossRef
105.
Zurück zum Zitat Handler M, Yurchenco PD, Iozzo RV. Developmental expression of perlecan during murine embryogenesis. Dev Dyn. 1997;210(2):130–45.PubMedCrossRef Handler M, Yurchenco PD, Iozzo RV. Developmental expression of perlecan during murine embryogenesis. Dev Dyn. 1997;210(2):130–45.PubMedCrossRef
106.
Zurück zum Zitat Costell M, Gustafsson E, Aszodi A, Morgelin M, Bloch W, Hunziker E, et al. Perlecan maintains the integrity of cartilage and some basement membranes. J Cell Biol. 1999;147(5):1109–22.PubMedCrossRef Costell M, Gustafsson E, Aszodi A, Morgelin M, Bloch W, Hunziker E, et al. Perlecan maintains the integrity of cartilage and some basement membranes. J Cell Biol. 1999;147(5):1109–22.PubMedCrossRef
107.
Zurück zum Zitat Arikawa-Hirasawa E, Watanabe H, Takami H, Hassell JR, Yamada Y. Perlecan is essential for cartilage and cephalic development. Nat Genet. 1999;23(3):354–8.PubMedCrossRef Arikawa-Hirasawa E, Watanabe H, Takami H, Hassell JR, Yamada Y. Perlecan is essential for cartilage and cephalic development. Nat Genet. 1999;23(3):354–8.PubMedCrossRef
108.
Zurück zum Zitat Bix G, Fu J, Gonzalez EM, Macro L, Barker A, Campbell S, et al. Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin. J Cell Biol. 2004;166(1):97–109.PubMedCrossRef Bix G, Fu J, Gonzalez EM, Macro L, Barker A, Campbell S, et al. Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin. J Cell Biol. 2004;166(1):97–109.PubMedCrossRef
109.
Zurück zum Zitat Smith SM, West LA, Govindraj P, Zhang X, Ornitz DM, Hassell JR. Heparan and chondroitin sulfate on growth plate perlecan mediate binding and delivery of FGF-2 to FGF receptors. Matrix Biol. 2007;26(3):175–84.PubMedCrossRef Smith SM, West LA, Govindraj P, Zhang X, Ornitz DM, Hassell JR. Heparan and chondroitin sulfate on growth plate perlecan mediate binding and delivery of FGF-2 to FGF receptors. Matrix Biol. 2007;26(3):175–84.PubMedCrossRef
110.
Zurück zum Zitat Datta S, Pierce M, Datta MW. Perlecan signaling: helping hedgehog stimulate prostate cancer growth. Int J Biochem Cell Biol. 2006;38(11):1855–61.PubMedCrossRef Datta S, Pierce M, Datta MW. Perlecan signaling: helping hedgehog stimulate prostate cancer growth. Int J Biochem Cell Biol. 2006;38(11):1855–61.PubMedCrossRef
111.
Zurück zum Zitat Gelse K, Poschl E, Aigner T. Collagens–structure, function, and biosynthesis. Adv Drug Deliv Rev. 2003;55(12):1531–46.PubMedCrossRef Gelse K, Poschl E, Aigner T. Collagens–structure, function, and biosynthesis. Adv Drug Deliv Rev. 2003;55(12):1531–46.PubMedCrossRef
112.
Zurück zum Zitat Church RL, Pfeiffer SE, Tanzer ML. Collagen biosynthesis: synthesis and secretion of a high molecular weight collagen precursor (procollagen). Proc Natl Acad Sci USA. 1971;68(11):2638–42.PubMedCrossRef Church RL, Pfeiffer SE, Tanzer ML. Collagen biosynthesis: synthesis and secretion of a high molecular weight collagen precursor (procollagen). Proc Natl Acad Sci USA. 1971;68(11):2638–42.PubMedCrossRef
113.
Zurück zum Zitat Berdichevsky F, Alford D, D’Souza B, Taylor-Papadimitriou J. Branching morphogenesis of human mammary epithelial cells in collagen gels. J Cell Sci. 1994;107(Pt 12):3557–68.PubMed Berdichevsky F, Alford D, D’Souza B, Taylor-Papadimitriou J. Branching morphogenesis of human mammary epithelial cells in collagen gels. J Cell Sci. 1994;107(Pt 12):3557–68.PubMed
114.
Zurück zum Zitat Krause S, Maffini MV, Soto AM, Sonnenschein C. A novel 3D in vitro culture model to study stromal-epithelial interactions in the mammary gland. Tissue Eng Part C Methods. 2008;14(3):261–71.PubMedCrossRef Krause S, Maffini MV, Soto AM, Sonnenschein C. A novel 3D in vitro culture model to study stromal-epithelial interactions in the mammary gland. Tissue Eng Part C Methods. 2008;14(3):261–71.PubMedCrossRef
115.
Zurück zum Zitat Chen J, Diacovo TG, Grenache DG, Santoro SA, Zutter MM. The alpha(2) integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis. Am J Pathol. 2002;161(1):337–44.PubMed Chen J, Diacovo TG, Grenache DG, Santoro SA, Zutter MM. The alpha(2) integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis. Am J Pathol. 2002;161(1):337–44.PubMed
116.
117.
Zurück zum Zitat McDaniel SM, Rumer KK, Biroc SL, Metz RP, Singh M, Porter W, et al. Remodeling of the Mammary Microenvironment after Lactation Promotes Breast Tumor Cell Metastasis. Am J Pathol 2006;168(2). McDaniel SM, Rumer KK, Biroc SL, Metz RP, Singh M, Porter W, et al. Remodeling of the Mammary Microenvironment after Lactation Promotes Breast Tumor Cell Metastasis. Am J Pathol 2006;168(2).
118.
Zurück zum Zitat O’Brien J, Lyons T, Monks J, Lucia MS, Wilson RS, Hines L, et al. Alternatively activated macrophages and collagen remodeling characterize the postpartum involuting mammary gland across species. Am J Pathol. 2010;176(3):1241–55.PubMedCrossRef O’Brien J, Lyons T, Monks J, Lucia MS, Wilson RS, Hines L, et al. Alternatively activated macrophages and collagen remodeling characterize the postpartum involuting mammary gland across species. Am J Pathol. 2010;176(3):1241–55.PubMedCrossRef
119.
Zurück zum Zitat Ferreira AM, Takagawa S, Fresco R, Zhu X, Varga J, DiPietro LA. Diminished induction of skin fibrosis in mice with MCP-1 deficiency. J Invest Dermatol. 2006;126(8):1900–8.PubMedCrossRef Ferreira AM, Takagawa S, Fresco R, Zhu X, Varga J, DiPietro LA. Diminished induction of skin fibrosis in mice with MCP-1 deficiency. J Invest Dermatol. 2006;126(8):1900–8.PubMedCrossRef
120.
Zurück zum Zitat George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 1993;119(4):1079–91.PubMed George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 1993;119(4):1079–91.PubMed
121.
Zurück zum Zitat Yamada KM. Fibronectin and other cell interactive glycoproteins. In: Hay ED, editor. Cell biology of extracellular matrix. NY: Plenum; 1991. p. 111–46. Yamada KM. Fibronectin and other cell interactive glycoproteins. In: Hay ED, editor. Cell biology of extracellular matrix. NY: Plenum; 1991. p. 111–46.
122.
Zurück zum Zitat Blaustein M, Pelisch F, Coso OA, Bissell MJ, Kornblihtt AR, Srebrow A. Mammary epithelial-mesenchymal interaction regulates fibronectin alternative splicing via phosphatidylinositol 3-kinase. J Biol Chem. 2004;279(20):21029–37.PubMedCrossRef Blaustein M, Pelisch F, Coso OA, Bissell MJ, Kornblihtt AR, Srebrow A. Mammary epithelial-mesenchymal interaction regulates fibronectin alternative splicing via phosphatidylinositol 3-kinase. J Biol Chem. 2004;279(20):21029–37.PubMedCrossRef
123.
Zurück zum Zitat George J, Wang SS, Sevcsik AM, Sanicola M, Cate RL, Koteliansky VE, et al. Transforming growth factor-beta initiates wound repair in rat liver through induction of the EIIIA-fibronectin splice isoform. Am J Pathol. 2000;156(1):115–24.PubMed George J, Wang SS, Sevcsik AM, Sanicola M, Cate RL, Koteliansky VE, et al. Transforming growth factor-beta initiates wound repair in rat liver through induction of the EIIIA-fibronectin splice isoform. Am J Pathol. 2000;156(1):115–24.PubMed
124.
Zurück zum Zitat Sakai T, Larsen M, Yamada KM. Fibronectin requirement in branching morphogenesis. Nature. 2003;423(6942):876–81.PubMedCrossRef Sakai T, Larsen M, Yamada KM. Fibronectin requirement in branching morphogenesis. Nature. 2003;423(6942):876–81.PubMedCrossRef
125.
Zurück zum Zitat Jones PL, Jones FS. Tenascin-C in development and disease: gene regulation and cell function. Matrix Biol. 2000;19(7):581–96.PubMedCrossRef Jones PL, Jones FS. Tenascin-C in development and disease: gene regulation and cell function. Matrix Biol. 2000;19(7):581–96.PubMedCrossRef
126.
Zurück zum Zitat Pas J, Wyszko E, Rolle K, Rychlewski L, Nowak S, Zukiel R, et al. Analysis of structure and function of tenascin-C. Int J Biochem Cell Biol. 2006;38(9):1594–602.PubMedCrossRef Pas J, Wyszko E, Rolle K, Rychlewski L, Nowak S, Zukiel R, et al. Analysis of structure and function of tenascin-C. Int J Biochem Cell Biol. 2006;38(9):1594–602.PubMedCrossRef
127.
Zurück zum Zitat Chiquet-Ehrismann R, Kalla P, Pearson CA, Beck K, Chiquet M. Tenascin interferes with fibronectin action. Cell. 1988;53(3):383–90.PubMedCrossRef Chiquet-Ehrismann R, Kalla P, Pearson CA, Beck K, Chiquet M. Tenascin interferes with fibronectin action. Cell. 1988;53(3):383–90.PubMedCrossRef
128.
Zurück zum Zitat Huang W, Chiquet-Ehrismann R, Moyano JV, Garcia-Pardo A, Orend G. Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation. Cancer Res. 2001;61(23):8586–94.PubMed Huang W, Chiquet-Ehrismann R, Moyano JV, Garcia-Pardo A, Orend G. Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation. Cancer Res. 2001;61(23):8586–94.PubMed
129.
Zurück zum Zitat Wehrle-Haller B, Chiquet M. Dual function of tenascin: simultaneous promotion of neurite growth and inhibition of glial migration. J Cell Sci. 1993;106(Pt 2):597–610.PubMed Wehrle-Haller B, Chiquet M. Dual function of tenascin: simultaneous promotion of neurite growth and inhibition of glial migration. J Cell Sci. 1993;106(Pt 2):597–610.PubMed
130.
Zurück zum Zitat Saga Y, Yagi T, Ikawa Y, Sakakura T, Aizawa S. Mice develop normally without tenascin. Genes Dev. 1992;6(10):1821–31.PubMedCrossRef Saga Y, Yagi T, Ikawa Y, Sakakura T, Aizawa S. Mice develop normally without tenascin. Genes Dev. 1992;6(10):1821–31.PubMedCrossRef
131.
Zurück zum Zitat Fukamauchi F, Mataga N, Wang YJ, Sato S, Yoshiki A, Kusakabe M. Tyrosine hydroxylase activity and its mRNA level in dopaminergic neurons of tenascin gene knockout mouse. Biochem Biophys Res Commun. 1997;231(2):356–9.PubMedCrossRef Fukamauchi F, Mataga N, Wang YJ, Sato S, Yoshiki A, Kusakabe M. Tyrosine hydroxylase activity and its mRNA level in dopaminergic neurons of tenascin gene knockout mouse. Biochem Biophys Res Commun. 1997;231(2):356–9.PubMedCrossRef
132.
Zurück zum Zitat Fukamauchi F, Mataga N, Wang YJ, Sato S, Youshiki A, Kusakabe M. Abnormal behavior and neurotransmissions of tenascin gene knockout mouse. Biochem Biophys Res Commun. 1996;221(1):151–6.PubMedCrossRef Fukamauchi F, Mataga N, Wang YJ, Sato S, Youshiki A, Kusakabe M. Abnormal behavior and neurotransmissions of tenascin gene knockout mouse. Biochem Biophys Res Commun. 1996;221(1):151–6.PubMedCrossRef
133.
Zurück zum Zitat Chiquet-Ehrismann R, Chiquet M. Tenascins: regulation and putative functions during pathological stress. J Pathol. 2003;200(4):488–99.PubMedCrossRef Chiquet-Ehrismann R, Chiquet M. Tenascins: regulation and putative functions during pathological stress. J Pathol. 2003;200(4):488–99.PubMedCrossRef
134.
Zurück zum Zitat Latijnhouwers M, Bergers M, Ponec M, Dijkman H, Andriessen M, Schalkwijk J. Human epidermal keratinocytes are a source of tenascin-C during wound healing. J Invest Dermatol. 1997;108(5):776–83.PubMedCrossRef Latijnhouwers M, Bergers M, Ponec M, Dijkman H, Andriessen M, Schalkwijk J. Human epidermal keratinocytes are a source of tenascin-C during wound healing. J Invest Dermatol. 1997;108(5):776–83.PubMedCrossRef
135.
Zurück zum Zitat Chiquet-Ehrismann R, Mackie EJ, Pearson CA, Sakakura T. Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell. 1986;47(1):131–9.PubMedCrossRef Chiquet-Ehrismann R, Mackie EJ, Pearson CA, Sakakura T. Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell. 1986;47(1):131–9.PubMedCrossRef
136.
Zurück zum Zitat Jones PL, Boudreau N, Myers CA, Erickson HP, Bissell MJ. Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments. J Cell Sci. 1995;108(Pt 2):519–27.PubMed Jones PL, Boudreau N, Myers CA, Erickson HP, Bissell MJ. Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments. J Cell Sci. 1995;108(Pt 2):519–27.PubMed
137.
Zurück zum Zitat Kalembey I, Yoshida T, Iriyama K, Sakakura T. Analysis of tenascin mRNA expression in the murine mammary gland from embryogenesis to carcinogenesis: an in situ hybridization study. Int J Dev Biol. 1997;41(4):569–73.PubMed Kalembey I, Yoshida T, Iriyama K, Sakakura T. Analysis of tenascin mRNA expression in the murine mammary gland from embryogenesis to carcinogenesis: an in situ hybridization study. Int J Dev Biol. 1997;41(4):569–73.PubMed
138.
Zurück zum Zitat Koukoulis GK, Gould VE, Bhattacharyya A, Gould JE, Howeedy AA, Virtanen I. Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: biologic and pathologic implications. Hum Pathol. 1991;22(7):636–43.PubMedCrossRef Koukoulis GK, Gould VE, Bhattacharyya A, Gould JE, Howeedy AA, Virtanen I. Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: biologic and pathologic implications. Hum Pathol. 1991;22(7):636–43.PubMedCrossRef
139.
Zurück zum Zitat Bristow J, Tee MK, Gitelman SE, Mellon SH, Miller WL. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J Cell Biol. 1993;122(1):265–78.PubMedCrossRef Bristow J, Tee MK, Gitelman SE, Mellon SH, Miller WL. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J Cell Biol. 1993;122(1):265–78.PubMedCrossRef
140.
Zurück zum Zitat Burch GH, Gong Y, Liu W, Dettman RW, Curry CJ, Smith L, et al. Tenascin-X deficiency is associated with Ehlers-Danlos syndrome. Nat Genet. 1997;17(1):104–8.PubMedCrossRef Burch GH, Gong Y, Liu W, Dettman RW, Curry CJ, Smith L, et al. Tenascin-X deficiency is associated with Ehlers-Danlos syndrome. Nat Genet. 1997;17(1):104–8.PubMedCrossRef
141.
Zurück zum Zitat Wong SY, Crowley D, Bronson RT, Hynes RO. Analyses of the role of endogenous SPARC in mouse models of prostate and breast cancer. Clin Exp Metastasis. 2008;25(2):109–18.PubMedCrossRef Wong SY, Crowley D, Bronson RT, Hynes RO. Analyses of the role of endogenous SPARC in mouse models of prostate and breast cancer. Clin Exp Metastasis. 2008;25(2):109–18.PubMedCrossRef
142.
Zurück zum Zitat Brekken RA, Sage EH. SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol. 2001;19(8):816–27.PubMedCrossRef Brekken RA, Sage EH. SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol. 2001;19(8):816–27.PubMedCrossRef
143.
Zurück zum Zitat Hohenester E, Engel J. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 2002;21(2):115–28.PubMedCrossRef Hohenester E, Engel J. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 2002;21(2):115–28.PubMedCrossRef
144.
Zurück zum Zitat Bradshaw AD, Puolakkainen P, Dasgupta J, Davidson JM, Wight TN. Helene Sage E. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength J Invest Dermatol. 2003;120(6):949–55. Bradshaw AD, Puolakkainen P, Dasgupta J, Davidson JM, Wight TN. Helene Sage E. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength J Invest Dermatol. 2003;120(6):949–55.
145.
Zurück zum Zitat Sweetwyne MT, Brekken RA, Workman G, Bradshaw AD, Carbon J, Siadak AW, et al. Functional analysis of the matricellular protein SPARC with novel monoclonal antibodies. J Histochem Cytochem. 2004;52(6):723–33.PubMedCrossRef Sweetwyne MT, Brekken RA, Workman G, Bradshaw AD, Carbon J, Siadak AW, et al. Functional analysis of the matricellular protein SPARC with novel monoclonal antibodies. J Histochem Cytochem. 2004;52(6):723–33.PubMedCrossRef
146.
Zurück zum Zitat Barker TH, Baneyx G, Cardo-Vila M, Workman GA, Weaver M, Menon PM, et al. SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity. J Biol Chem. 2005;280(43):36483–93.PubMedCrossRef Barker TH, Baneyx G, Cardo-Vila M, Workman GA, Weaver M, Menon PM, et al. SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity. J Biol Chem. 2005;280(43):36483–93.PubMedCrossRef
147.
Zurück zum Zitat Schaefer L, Iozzo RV. Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction. J Biol Chem. 2008;283(31):21305–9.PubMedCrossRef Schaefer L, Iozzo RV. Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction. J Biol Chem. 2008;283(31):21305–9.PubMedCrossRef
148.
Zurück zum Zitat Wight TN, Heinegard DK, Hascall VC. Proteoglycans Structure and Function. In: Hay ED (ed). Cell Biology of Extracellular Matrix, 1991, p. 45–78. Wight TN, Heinegard DK, Hascall VC. Proteoglycans Structure and Function. In: Hay ED (ed). Cell Biology of Extracellular Matrix, 1991, p. 45–78.
149.
Zurück zum Zitat Coppock DL, Kopman C, Scandalis S, Gilleran S. Preferential gene expression in quiescent human lung fibroblasts. Cell Growth Differ. 1993;4(6):483–93.PubMed Coppock DL, Kopman C, Scandalis S, Gilleran S. Preferential gene expression in quiescent human lung fibroblasts. Cell Growth Differ. 1993;4(6):483–93.PubMed
150.
Zurück zum Zitat Minor K, Tang X, Kahrilas G, Archibald SJ, Davies JE, Davies SJ. Decorin promotes robust axon growth on inhibitory CSPGs and myelin via a direct effect on neurons. Neurobiol Dis. 2008;32(1):88–95.PubMedCrossRef Minor K, Tang X, Kahrilas G, Archibald SJ, Davies JE, Davies SJ. Decorin promotes robust axon growth on inhibitory CSPGs and myelin via a direct effect on neurons. Neurobiol Dis. 2008;32(1):88–95.PubMedCrossRef
151.
Zurück zum Zitat Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol. 1997;136(3):729–43.PubMedCrossRef Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol. 1997;136(3):729–43.PubMedCrossRef
152.
Zurück zum Zitat Reed CC, Waterhouse A, Kirby S, Kay P, Owens RT, McQuillan DJ, et al. Decorin prevents metastatic spreading of breast cancer. Oncogene. 2005;24(6):1104–10.PubMedCrossRef Reed CC, Waterhouse A, Kirby S, Kay P, Owens RT, McQuillan DJ, et al. Decorin prevents metastatic spreading of breast cancer. Oncogene. 2005;24(6):1104–10.PubMedCrossRef
153.
Zurück zum Zitat Zhu JX, Goldoni S, Bix G, Owens RT, McQuillan DJ, Reed CC, et al. Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis. J Biol Chem. 2005;280(37):32468–79.PubMedCrossRef Zhu JX, Goldoni S, Bix G, Owens RT, McQuillan DJ, Reed CC, et al. Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis. J Biol Chem. 2005;280(37):32468–79.PubMedCrossRef
154.
Zurück zum Zitat Grant DS, Yenisey C, Rose RW, Tootell M, Santra M, Iozzo RV. Decorin suppresses tumor cell-mediated angiogenesis. Oncogene. 2002;21(31):4765–77.PubMedCrossRef Grant DS, Yenisey C, Rose RW, Tootell M, Santra M, Iozzo RV. Decorin suppresses tumor cell-mediated angiogenesis. Oncogene. 2002;21(31):4765–77.PubMedCrossRef
155.
Zurück zum Zitat Yamaguchi Y, Mann DM, Ruoslahti E. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature. 1990;346(6281):281–4.PubMedCrossRef Yamaguchi Y, Mann DM, Ruoslahti E. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature. 1990;346(6281):281–4.PubMedCrossRef
156.
Zurück zum Zitat Xu T, Bianco P, Fisher LW, Longenecker G, Smith E, Goldstein S, et al. Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice. Nat Genet. 1998;20(1):78–82.PubMedCrossRef Xu T, Bianco P, Fisher LW, Longenecker G, Smith E, Goldstein S, et al. Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice. Nat Genet. 1998;20(1):78–82.PubMedCrossRef
157.
Zurück zum Zitat Fust A, LeBellego F, Iozzo RV, Roughley PJ, Ludwig MS. Alterations in lung mechanics in decorin-deficient mice. Am J Physiol Lung Cell Mol Physiol. 2005;288(1):L159–66.PubMedCrossRef Fust A, LeBellego F, Iozzo RV, Roughley PJ, Ludwig MS. Alterations in lung mechanics in decorin-deficient mice. Am J Physiol Lung Cell Mol Physiol. 2005;288(1):L159–66.PubMedCrossRef
158.
Zurück zum Zitat Schaefer L, Mihalik D, Babelova A, Krzyzankova M, Grone HJ, Iozzo RV, et al. Regulation of fibrillin-1 by biglycan and decorin is important for tissue preservation in the kidney during pressure-induced injury. Am J Pathol. 2004;165(2):383–96.PubMed Schaefer L, Mihalik D, Babelova A, Krzyzankova M, Grone HJ, Iozzo RV, et al. Regulation of fibrillin-1 by biglycan and decorin is important for tissue preservation in the kidney during pressure-induced injury. Am J Pathol. 2004;165(2):383–96.PubMed
159.
Zurück zum Zitat Salgado RM, Favaro RR, Martin SS, Zorn TM. The estrous cycle modulates small leucine-rich proteoglycans expression in mouse uterine tissues. Anat Rec (Hoboken). 2009;292(1):138–53. Salgado RM, Favaro RR, Martin SS, Zorn TM. The estrous cycle modulates small leucine-rich proteoglycans expression in mouse uterine tissues. Anat Rec (Hoboken). 2009;292(1):138–53.
160.
Zurück zum Zitat San Martin S, Soto-Suazo M, De Oliveira SF, Aplin JD, Abrahamsohn P, Zorn TM. Small leucine-rich proteoglycans (SLRPs) in uterine tissues during pregnancy in mice. Reproduction. 2003;125(4):585–95.PubMedCrossRef San Martin S, Soto-Suazo M, De Oliveira SF, Aplin JD, Abrahamsohn P, Zorn TM. Small leucine-rich proteoglycans (SLRPs) in uterine tissues during pregnancy in mice. Reproduction. 2003;125(4):585–95.PubMedCrossRef
161.
Zurück zum Zitat Fleming WW, Sullivan CE, Torchia DA. Characterization of molecular motions in 13C-labeled aortic elastin by 13C-1H magnetic double resonance. Biopolymers. 1980;19(3):597–617.PubMedCrossRef Fleming WW, Sullivan CE, Torchia DA. Characterization of molecular motions in 13C-labeled aortic elastin by 13C-1H magnetic double resonance. Biopolymers. 1980;19(3):597–617.PubMedCrossRef
162.
Zurück zum Zitat Yanagisawa H, Davis EC, Starcher BC, Ouchi T, Yanagisawa M, Richardson JA, et al. Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo. Nature. 2002;415(6868):168–71.PubMedCrossRef Yanagisawa H, Davis EC, Starcher BC, Ouchi T, Yanagisawa M, Richardson JA, et al. Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo. Nature. 2002;415(6868):168–71.PubMedCrossRef
163.
Zurück zum Zitat Choi J, Bergdahl A, Zheng Q, Starcher B, Yanagisawa H, Davis EC. Analysis of dermal elastic fibers in the absence of fibulin-5 reveals potential roles for fibulin-5 in elastic fiber assembly. Matrix Biol. 2009;28(4):211–20.PubMedCrossRef Choi J, Bergdahl A, Zheng Q, Starcher B, Yanagisawa H, Davis EC. Analysis of dermal elastic fibers in the absence of fibulin-5 reveals potential roles for fibulin-5 in elastic fiber assembly. Matrix Biol. 2009;28(4):211–20.PubMedCrossRef
164.
Zurück zum Zitat Reinboth B, Hanssen E, Cleary EG, Gibson MA. Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1. J Biol Chem. 2002;277(6):3950–7.PubMedCrossRef Reinboth B, Hanssen E, Cleary EG, Gibson MA. Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1. J Biol Chem. 2002;277(6):3950–7.PubMedCrossRef
165.
Zurück zum Zitat Trask BC, Trask TM, Broekelmann T, Mecham RP. The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin. Mol Biol Cell. 2000;11(5):1499–507.PubMed Trask BC, Trask TM, Broekelmann T, Mecham RP. The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin. Mol Biol Cell. 2000;11(5):1499–507.PubMed
166.
Zurück zum Zitat Boyd NF, Lockwood GA, Byng JW, Tritchler DL, Yaffe MJ. Mammographic densities and breast cancer risk. Cancer Epidemiol Biomarkers Prev. 1998;7(12):1133–44.PubMed Boyd NF, Lockwood GA, Byng JW, Tritchler DL, Yaffe MJ. Mammographic densities and breast cancer risk. Cancer Epidemiol Biomarkers Prev. 1998;7(12):1133–44.PubMed
167.
Zurück zum Zitat Provenzano PP, Inman DR, Eliceiri KW, Knittel JG, Yan L, Rueden CT, et al. Collagen density promotes mammary tumor initiation and progression. BMC Med. 2008;6:11.PubMedCrossRef Provenzano PP, Inman DR, Eliceiri KW, Knittel JG, Yan L, Rueden CT, et al. Collagen density promotes mammary tumor initiation and progression. BMC Med. 2008;6:11.PubMedCrossRef
168.
Zurück zum Zitat Mydel P, Shipley JM, Adair-Kirk TL, Kelley DG, Broekelmann TJ, Mecham RP, et al. Neutrophil elastase cleaves laminin-332 (laminin-5) generating peptides that are chemotactic for neutrophils. J Biol Chem. 2008;283(15):9513–22.PubMedCrossRef Mydel P, Shipley JM, Adair-Kirk TL, Kelley DG, Broekelmann TJ, Mecham RP, et al. Neutrophil elastase cleaves laminin-332 (laminin-5) generating peptides that are chemotactic for neutrophils. J Biol Chem. 2008;283(15):9513–22.PubMedCrossRef
169.
Zurück zum Zitat Senior RM, Gresham HD, Griffin GL, Brown EJ, Chung AE. Entactin stimulates neutrophil adhesion and chemotaxis through interactions between its Arg-Gly-Asp (RGD) domain and the leukocyte response integrin. J Clin Invest. 1992;90(6):2251–7.PubMedCrossRef Senior RM, Gresham HD, Griffin GL, Brown EJ, Chung AE. Entactin stimulates neutrophil adhesion and chemotaxis through interactions between its Arg-Gly-Asp (RGD) domain and the leukocyte response integrin. J Clin Invest. 1992;90(6):2251–7.PubMedCrossRef
170.
Zurück zum Zitat Senior RM, Hinek A, Griffin GL, Pipoly DJ, Crouch EC, Mecham RP. Neutrophils show chemotaxis to type IV collagen and its 7 S domain and contain a 67 kD type IV collagen binding protein with lectin properties. Am J Respir Cell Mol Biol. 1989;1(6):479–87.PubMed Senior RM, Hinek A, Griffin GL, Pipoly DJ, Crouch EC, Mecham RP. Neutrophils show chemotaxis to type IV collagen and its 7 S domain and contain a 67 kD type IV collagen binding protein with lectin properties. Am J Respir Cell Mol Biol. 1989;1(6):479–87.PubMed
171.
Zurück zum Zitat Adair-Kirk TL, Atkinson JJ, Broekelmann TJ, Doi M, Tryggvason K, Miner JH, et al. A site on laminin alpha 5, AQARSAASKVKVSMKF, induces inflammatory cell production of matrix metalloproteinase-9 and chemotaxis. J Immunol. 2003;171(1):398–406.PubMed Adair-Kirk TL, Atkinson JJ, Broekelmann TJ, Doi M, Tryggvason K, Miner JH, et al. A site on laminin alpha 5, AQARSAASKVKVSMKF, induces inflammatory cell production of matrix metalloproteinase-9 and chemotaxis. J Immunol. 2003;171(1):398–406.PubMed
172.
Zurück zum Zitat Stein T, Morris JS, Davies CR, Weber-Hall SJ, Duffy MA, Heath VJ, et al. Involution of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3. Breast Cancer Res. 2004;6(2):R75–91.PubMedCrossRef Stein T, Morris JS, Davies CR, Weber-Hall SJ, Duffy MA, Heath VJ, et al. Involution of the mouse mammary gland is associated with an immune cascade and an acute-phase response, involving LBP, CD14 and STAT3. Breast Cancer Res. 2004;6(2):R75–91.PubMedCrossRef
173.
Zurück zum Zitat Vaday GG, Lider O. Extracellular matrix moieties, cytokines, and enzymes: dynamic effects on immune cell behavior and inflammation. J Leukoc Biol. 2000;67(2):149–59.PubMed Vaday GG, Lider O. Extracellular matrix moieties, cytokines, and enzymes: dynamic effects on immune cell behavior and inflammation. J Leukoc Biol. 2000;67(2):149–59.PubMed
174.
Zurück zum Zitat Lilla JN, Joshi RV, Craik CS, Werb Z. Active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation, and stromal remodeling during mammary gland involution. J Biol Chem. 2009;284(20):13792–803.PubMedCrossRef Lilla JN, Joshi RV, Craik CS, Werb Z. Active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation, and stromal remodeling during mammary gland involution. J Biol Chem. 2009;284(20):13792–803.PubMedCrossRef
175.
Zurück zum Zitat Babelova A, Moreth K, Tsalastra-Greul W, Zeng-Brouwers J, Eickelberg O, Young MF, et al. Biglycan, a danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors. J Biol Chem. 2009;284(36):24035–48.PubMedCrossRef Babelova A, Moreth K, Tsalastra-Greul W, Zeng-Brouwers J, Eickelberg O, Young MF, et al. Biglycan, a danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors. J Biol Chem. 2009;284(36):24035–48.PubMedCrossRef
176.
Zurück zum Zitat Johnson GB, Brunn GJ, Kodaira Y, Platt JL. Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4. J Immunol. 2002;168(10):5233–9.PubMed Johnson GB, Brunn GJ, Kodaira Y, Platt JL. Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4. J Immunol. 2002;168(10):5233–9.PubMed
177.
Zurück zum Zitat Termeer C, Benedix F, Sleeman J, Fieber C, Voith U, Ahrens T, et al. Oligosaccharides of Hyaluronan activate dendritic cells via toll-like receptor 4. J Exp Med. 2002;195(1):99–111.PubMedCrossRef Termeer C, Benedix F, Sleeman J, Fieber C, Voith U, Ahrens T, et al. Oligosaccharides of Hyaluronan activate dendritic cells via toll-like receptor 4. J Exp Med. 2002;195(1):99–111.PubMedCrossRef
178.
Zurück zum Zitat Elenstrom-Magnusson C, Chen W, Clinchy B, Obrink B, Severison E. IL-4-induced B cell migration involves transient interactions between beta 1 integrins and extracellular matrix components. Int Immunol. 1995;7(4):567–73.PubMedCrossRef Elenstrom-Magnusson C, Chen W, Clinchy B, Obrink B, Severison E. IL-4-induced B cell migration involves transient interactions between beta 1 integrins and extracellular matrix components. Int Immunol. 1995;7(4):567–73.PubMedCrossRef
Metadaten
Titel
Extracellular Matrix Composition Reveals Complex and Dynamic Stromal-Epithelial Interactions in the Mammary Gland
verfasst von
Ori Maller
Holly Martinson
Pepper Schedin
Publikationsdatum
01.09.2010
Verlag
Springer US
Erschienen in
Journal of Mammary Gland Biology and Neoplasia / Ausgabe 3/2010
Print ISSN: 1083-3021
Elektronische ISSN: 1573-7039
DOI
https://doi.org/10.1007/s10911-010-9189-6

Weitere Artikel der Ausgabe 3/2010

Journal of Mammary Gland Biology and Neoplasia 3/2010 Zur Ausgabe

„Überwältigende“ Evidenz für Tripeltherapie beim metastasierten Prostata-Ca.

22.05.2024 Prostatakarzinom Nachrichten

Patienten mit metastasiertem hormonsensitivem Prostatakarzinom sollten nicht mehr mit einer alleinigen Androgendeprivationstherapie (ADT) behandelt werden, mahnt ein US-Team nach Sichtung der aktuellen Datenlage. Mit einer Tripeltherapie haben die Betroffenen offenbar die besten Überlebenschancen.

So sicher sind Tattoos: Neue Daten zur Risikobewertung

22.05.2024 Melanom Nachrichten

Das größte medizinische Problem bei Tattoos bleiben allergische Reaktionen. Melanome werden dadurch offensichtlich nicht gefördert, die Farbpigmente könnten aber andere Tumoren begünstigen.

CAR-M-Zellen: Warten auf das große Fressen

22.05.2024 Onkologische Immuntherapie Nachrichten

Auch myeloide Immunzellen lassen sich mit chimären Antigenrezeptoren gegen Tumoren ausstatten. Solche CAR-Fresszell-Therapien werden jetzt für solide Tumoren entwickelt. Künftig soll dieser Prozess nicht mehr ex vivo, sondern per mRNA im Körper der Betroffenen erfolgen.

Blutdrucksenkung könnte Uterusmyome verhindern

Frauen mit unbehandelter oder neu auftretender Hypertonie haben ein deutlich erhöhtes Risiko für Uterusmyome. Eine Therapie mit Antihypertensiva geht hingegen mit einer verringerten Inzidenz der gutartigen Tumoren einher.

Update Onkologie

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.