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Aesthetic Plastic Surgery

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14.12.2018 | Original Article

Recent Advances on Relationship Between Inorganic Phosphate and Pathologic Calcification: Is Calcification After Breast Augmentation with Fat Grafting Correlated with Locally Increased Concentration of Inorganic Phosphate?

verfasst von: Shangshan Li, Jie Luan

Erschienen in: Aesthetic Plastic Surgery | Ausgabe 1/2019

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Abstract

Background

Pathologic calcification has frequently occurred after breast augmentation with fat grafting as well as other conditions such as breast cancer, trauma, myocardial infarction, arteriosclerosis and even after reduction mammoplasty. Inorganic phosphate, correlated with fat metabolism, is an important factor that induces pathologic calcification such as vascular calcification.

Methods

A literature search was conducted using PubMed with the keywords: calcification, inorganic phosphate, fat. Studies related to the process of pathologic calcification, correlation between inorganic phosphate and pathologic calcification, between inorganic phosphate and fat metabolism in pathologic calcification were collected.

Results

Various mechanisms were referred to in pathologic calcification among which inorganic phosphate played an important role. Inorganic phosphate could be liberated, under the effect of various enzymes, in the process of fat metabolism. The authors hypothesized that a large-scale necrotizing zone, which could occur in fat grafting with large amounts per cannula, might provide a high-phosphate environment which might contribute to differentiation of surrounding cells such as stem cells or regenerated vessel cells into osteoblast-like cells that induce pathologic calcification.

Conclusion

Inorganic phosphate, which was correlated with fat metabolism, played a significant role in pathologic calcification. We firstly hypothesize that calcification after fat grafting may be related to locally increasing concentrations of phosphate in a necrotizing zone. Further research should be conducted to verify this hypothesis.

Level of Evidence V

This journal requires that authors assign a level of evidence to each article. For a full description of these Evidence-Based Medicine ratings, please refer to the Table of Contents or the online Instructions to Authors www.springer.com/00266.

Rubin JP, Coon D, Zuley M et al (2012) Mammographic changes after fat transfer to the breast compared with changes after breast reduction: a blinded study. Plast Reconstr Surg 129:1029–1038. https://doi.org/10.1097/PRS.0b013e31824a2a8e CrossRefPubMed

Veber M, Tourasse C, Toussoun G et al (2011) Radiographic findings after breast augmentation by autologous fat transfer. Plast Reconstr Surg 127:1289–1299. https://doi.org/10.1097/PRS.0b013e318205f38f CrossRefPubMed

Zocchi ML, Zuliani F (2008) Bicompartmental breast lipostructuring. Aesthetic Plast Surg 32:313–328. https://doi.org/10.1007/s00266-007-9089-3 CrossRefPubMed

Coleman SR, Saboeiro AP (2015) Primary breast augmentation with fat grafting. Clin Plast Surg 42(301–306):vii. https://doi.org/10.1016/j.cps.2015.03.010 CrossRef

Coleman SR (1995) Long-term survival of fat transplants: controlled demonstrations. Aesthetic Plast Surg 19:421–425CrossRefPubMed

Ling H, Liu ZB, Xu LH et al (2013) Malignant calcification is an important unfavorable prognostic factor in primary invasive breast cancer. Asia Pac J Clin Oncol 9:139–145. https://doi.org/10.1111/j.1743-7563.2012.01572.x CrossRefPubMed

O’Brien EJ, Frank CB, Shrive NG et al (2012) Heterotopic mineralization (ossification or calcification) in tendinopathy or following surgical tendon trauma. Int J Exp Pathol 93:319–331. https://doi.org/10.1111/j.1365-2613.2012.00829.x CrossRefPubMedPubMedCentral

Delo DM, Guan X, Wang Z et al (2011) Calcification after myocardial infarction is independent of amniotic fluid stem cell injection. Cardiovasc Pathol 20:e69–e78. https://doi.org/10.1016/j.carpath.2010.03.001 CrossRefPubMed

Kim H, Kang BJ, Kim SH et al (2015) What we should know in mammography after reduction mammoplasty and mastopexy? Breast Cancer 22:391–398. https://doi.org/10.1007/s12282-013-0494-y CrossRefPubMed

10.

Tolle M, Reshetnik A, Schuchardt M et al (2015) Arteriosclerosis and vascular calcification: causes, clinical assessment and therapy. Eur J Clin Investig 45:976–985. https://doi.org/10.1111/eci.12493 CrossRef

11.

Mineda K, Kuno S, Kato H et al (2014) Chronic inflammation and progressive calcification as a result of fat necrosis: the worst outcome in fat grafting. Plast Reconstr Surg 133:1064–1072. https://doi.org/10.1097/PRS.0000000000000097 CrossRefPubMed

12.

Pu LL (2016) Mechanisms of fat graft survival. Ann Plast Surg 77(Suppl 1):S84–S86. https://doi.org/10.1097/SAP.0000000000000730 CrossRefPubMed

13.

Redig AJ, McAllister SS (2013) Breast cancer as a systemic disease: a view of metastasis. J Intern Med 274:113–126. https://doi.org/10.1111/joim.12084 CrossRefPubMedPubMedCentral

14.

Kachgal S, Mace KA, Boudreau NJ (2012) The dual roles of homeobox genes in vascularization and wound healing. Cell Adhes Migr 6:457–470. https://doi.org/10.4161/cam.22164 CrossRef

15.

Giachelli CM (2005) Inducers and inhibitors of biomineralization: lessons from pathological calcification. Orthod Craniofac Res 8:229–231. https://doi.org/10.1111/j.1601-6343.2005.00345.x CrossRefPubMed

16.

Tabcheh L, Bianchi A, Clement A et al (2014) Phosphate-induced mineralization of tracheal smooth muscle and cartilage cells. Biomed Mater Eng 24:37–45. https://doi.org/10.3233/BME-140972 CrossRefPubMed

17.

Martin SF, DeBlanc RL, Hergenrother PJ (2000) Determination of the substrate specificity of the phospholipase D from Streptomyces chromofuscus via an inorganic phosphate quantitation assay. Anal Biochem 278:106–110. https://doi.org/10.1006/abio.1999.4420 CrossRefPubMed

18.

Demer LL (1995) A skeleton in the atherosclerosis closet. Circulation 92:2029–2032CrossRefPubMed

19.

Wexler L, Brundage B, Crouse J et al (1996) Coronary artery calcification: pathophysiology, epidemiology, imaging methods, and clinical implications. A statement for health professionals from the American Heart Association. Writing Group. Circulation 94:1175–1192CrossRefPubMed

20.

Villa-Bellosta R, Millan A, Sorribas V (2011) Role of calcium-phosphate deposition in vascular smooth muscle cell calcification. Am J Physiol Cell Physiol 300:C210–C220. https://doi.org/10.1152/ajpcell.00229.2010 CrossRefPubMed

21.

Cottignoli V, Relucenti M, Agrosi G et al (2015) Biological niches within human calcified aortic valves: towards understanding of the pathological biomineralization process. Biomed Res Int 2015:542687. https://doi.org/10.1155/2015/542687 CrossRefPubMedPubMedCentral

22.

Vattikuti R, Towler DA (2004) Osteogenic regulation of vascular calcification: an early perspective. Am J Physiol Endocrinol Metab 286:E686–E696. https://doi.org/10.1152/ajpendo.00552.2003 CrossRefPubMed

23.

Demer LL, Tintut Y (2008) Vascular calcification: pathobiology of a multifaceted disease. Circulation 117:2938–2948. https://doi.org/10.1161/CIRCULATIONAHA.107.743161 CrossRefPubMedPubMedCentral

24.

Hruska KA, Mathew S, Saab G (2005) Bone morphogenetic proteins in vascular calcification. Circ Res 97:105–114. https://doi.org/10.1161/01.RES.00000175571.53833.6c CrossRefPubMed

25.

Speer MY, Giachelli CM (2004) Regulation of cardiovascular calcification. Cardiovasc Pathol 13:63–70. https://doi.org/10.1016/S1054-8807(03)00130-3 CrossRefPubMed

26.

Jono S, Shioi A, Ikari Y et al (2006) Vascular calcification in chronic kidney disease. J Bone Miner Metab 24:176–181. https://doi.org/10.1007/s00774-005-0668-6 CrossRefPubMed

27.

Demer LL, Tintut Y (2014) Inflammatory, metabolic, and genetic mechanisms of vascular calcification. Arterioscler Thromb Vasc Biol 34:715–723. https://doi.org/10.1161/ATVBAHA.113.302070 CrossRefPubMedPubMedCentral

28.

Sage AP, Lu J, Tintut Y et al (2011) Hyperphosphatemia-induced nanocrystals upregulate the expression of bone morphogenetic protein-2 and osteopontin genes in mouse smooth muscle cells in vitro. Kidney Int 79:414–422. https://doi.org/10.1038/ki.2010.390 CrossRefPubMed

29.

Chen NX, O’Neill KD, Chen X et al (2008) Annexin-mediated matrix vesicle calcification in vascular smooth muscle cells. J Bone Miner Res 23:1798–1805. https://doi.org/10.1359/jbmr.080604 CrossRefPubMedPubMedCentral

30.

Kapustin AN, Davies JD, Reynolds JL et al (2011) Calcium regulates key components of vascular smooth muscle cell-derived matrix vesicles to enhance mineralization. Circ Res 109:e1–12. https://doi.org/10.1161/CIRCRESAHA.110.238808 CrossRefPubMed

31.

Anderson HC (2003) Matrix vesicles and calcification. Curr Rheumatol Rep 5:222–226CrossRefPubMed

32.

Kim KM (1976) Calcification of matrix vesicles in human aortic valve and aortic media. Fed Proc 35:156–162PubMed

33.

Tintut Y, Patel J, Territo M et al (2002) Monocyte/macrophage regulation of vascular calcification in vitro. Circulation 105:650–655CrossRefPubMed

34.

Tintut Y, Patel J, Parhami F et al (2000) Tumor necrosis factor-alpha promotes in vitro calcification of vascular cells via the cAMP pathway. Circulation 102:2636–2642CrossRefPubMed

35.

Grskovic I, Kutsch A, Frie C et al (2012) Depletion of annexin A5, annexin A6, and collagen X causes no gross changes in matrix vesicle-mediated mineralization, but lack of collagen X affects hematopoiesis and the Th1/Th2 response. J Bone Miner Res 27:2399–2412. https://doi.org/10.1002/jbmr.1682 CrossRefPubMed

36.

Mune S, Shibata M, Hatamura I et al (2009) Mechanism of phosphate-induced calcification in rat aortic tissue culture: possible involvement of Pit-1 and apoptosis. Clin Exp Nephrol 13:571–577. https://doi.org/10.1007/s10157-009-0208-0 CrossRefPubMed

37.

Duan X, Zhou Y, Teng X et al (2009) Endoplasmic reticulum stress-mediated apoptosis is activated in vascular calcification. Biochem Biophys Res Commun 387:694–699. https://doi.org/10.1016/j.bbrc.2009.07.085 CrossRefPubMed

38.

Proudfoot D, Skepper JN, Hegyi L et al (2000) Apoptosis regulates human vascular calcification in vitro: evidence for initiation of vascular calcification by apoptotic bodies. Circ Res 87:1055–1062CrossRefPubMed

39.

Kumata C, Mizobuchi M, Ogata H et al (2011) Involvement of matrix metalloproteinase-2 in the development of medial layer vascular calcification in uremic rats. Ther Apher Dial 15(Suppl 1):18–22. https://doi.org/10.1111/j.1744-9987.2011.00921.x CrossRefPubMed

40.

Rucker RB (1974) Calcium binding to elastin. Adv Exp Med Biol 48:185–209CrossRefPubMed

41.

Arsenault AL, Frankland BW, Ottensmeyer FP (1991) Vectorial sequence of mineralization in the turkey leg tendon determined by electron microscopic imaging. Calcif Tissue Int 48:46–55CrossRefPubMed

42.

Golub EE (2009) Role of matrix vesicles in biomineralization. Biochem Biophys Acta 1790:1592–1598. https://doi.org/10.1016/j.bbagen.2009.09.006 CrossRefPubMed

43.

Gufler H, Wagner S, Franke FE (2011) The interior structure of breast microcalcifications assessed with micro computed tomography. Acta Radiol 52:592–596. https://doi.org/10.1258/ar.2011.100489 CrossRefPubMed

44.

New SE, Goettsch C, Aikawa M et al (2013) Macrophage-derived matrix vesicles: an alternative novel mechanism for microcalcification in atherosclerotic plaques. Circ Res 113:72–77. https://doi.org/10.1161/CIRCRESAHA.113.301036 CrossRefPubMedPubMedCentral

45.

Anderson HC (1995) Molecular biology of matrix vesicles. Clin Orthop Relat Res 314:266–280

46.

Golub EE (2011) Biomineralization and matrix vesicles in biology and pathology. Semin Immunopathol 33:409–417. https://doi.org/10.1007/s00281-010-0230-z CrossRefPubMed

47.

Xiao Z, Blonder J, Zhou M et al (2009) Proteomic analysis of extracellular matrix and vesicles. J Proteomics 72:34–45. https://doi.org/10.1016/j.jprot.2008.11.011 CrossRefPubMed

48.

Manolagas SC (2000) Birth and death of bone cells: basic regulatory mechanisms and implications for the pathogenesis and treatment of osteoporosis. Endocr Rev 21:115–137. https://doi.org/10.1210/edrv.21.2.0395 CrossRefPubMed

49.

Kirsch T (2006) Determinants of pathological mineralization. Curr Opin Rheumatol 18:174–180. https://doi.org/10.1097/01.bor.0000209431.59226.46 CrossRefPubMed

50.

Blair B, Fabrizio M (2000) Pharmacology for renal calculi. Expert Opin Pharmacother 1:435–441. https://doi.org/10.1517/14656566.1.3.435 CrossRefPubMed

51.

Sohshang HL, Singh MA, Singh NG et al (2000) Biochemical and bacteriological study of urinary calculi. J Commun Dis 32:216–221PubMed

52.

Mathew G, McKay DS, Ciftcioglu N (2008) Do blood-borne calcifying nanoparticles self-propagate? Int J Nanomed 3:265–275

53.

Ewence AE, Bootman M, Roderick HL et al (2008) Calcium phosphate crystals induce cell death in human vascular smooth muscle cells: a potential mechanism in atherosclerotic plaque destabilization. Circ Res 103:e28–e34. https://doi.org/10.1161/CIRCRESAHA.108.181305 CrossRefPubMed

54.

Nadra I, Boccaccini AR, Philippidis P et al (2008) Effect of particle size on hydroxyapatite crystal-induced tumor necrosis factor alpha secretion by macrophages. Atherosclerosis 196:98–105. https://doi.org/10.1016/j.atherosclerosis.2007.02.005 CrossRefPubMed

55.

Vervaet BA, Verhulst A, Dauwe SE et al (2009) An active renal crystal clearance mechanism in rat and man. Kidney Int 75:41–51. https://doi.org/10.1038/ki.2008.450 CrossRefPubMed

56.

Huang MS, Sage AP, Lu J et al (2008) Phosphate and pyrophosphate mediate PKA-induced vascular cell calcification. Biochem Biophys Res Commun 374:553–558. https://doi.org/10.1016/j.bbrc.2008.07.062 CrossRefPubMedPubMedCentral

57.

Shanahan CM, Crouthamel MH, Kapustin A et al (2011) Arterial calcification in chronic kidney disease: key roles for calcium and phosphate. Circ Res 109:697–711. https://doi.org/10.1161/CIRCRESAHA.110.234914 CrossRefPubMedPubMedCentral

58.

Kirsch T (2008) Determinants of pathologic mineralization. Crit Rev Eukaryot Gene Expr 18:1–9CrossRefPubMed

59.

Greenawalt JW, Rossi CS, Lehninger AL (1964) Effect of active accumulation of calcium and phosphate ions on the structure of rat liver mitochondria. J Cell Biol 23:21–38CrossRefPubMedPubMedCentral

60.

Weinbach EC, Von Brand T (1967) Formation, isolation and composition of dense granules from mitochondria. Biochem Biophys Acta 148:256–266CrossRefPubMed

61.

Villa-Bellosta R, Hamczyk MR, Andres V (2017) Novel phosphate-activated macrophages prevent ectopic calcification by increasing extracellular ATP and pyrophosphate. PLoS ONE 12:e0174998. https://doi.org/10.1371/journal.pone.0174998 CrossRefPubMedPubMedCentral

62.

Sonou T, Ohya M, Yashiro M et al (2015) Mineral composition of phosphate-induced calcification in a rat aortic tissue culture model. J Atheroscler Thromb 22:1197–1206. https://doi.org/10.5551/jat.28647 CrossRefPubMed

63.

Jono S, McKee MD, Murry CE et al (2000) Phosphate regulation of vascular smooth muscle cell calcification. Circ Res 87:E10–E17CrossRefPubMed

64.

Lee K, Kim H, Jeong D (2014) Microtubule stabilization attenuates vascular calcification through the inhibition of osteogenic signaling and matrix vesicle release. Biochem Biophys Res Commun 451:436–441. https://doi.org/10.1016/j.bbrc.2014.08.007 CrossRefPubMed

65.

Bellows CG, Heersche JN, Aubin JE (1992) Inorganic phosphate added exogenously or released from beta-glycerophosphate initiates mineralization of osteoid nodules in vitro. Bone Miner 17:15–29CrossRefPubMed

66.

Tenenbaum HC (1981) Role of organic phosphate in mineralization of bone in vitro. J Dent Res. https://doi.org/10.1177/0022034581060003S0801 CrossRefPubMed

67.

Chung CH, Golub EE, Forbes E et al (1992) Mechanism of action of beta-glycerophosphate on bone cell mineralization. Calcif Tissue Int 51:305–311CrossRefPubMed

68.

Leboy PS, Vaias L, Uschmann B et al (1989) Ascorbic acid induces alkaline phosphatase, type X collagen, and calcium deposition in cultured chick chondrocytes. J Biol Chem 264:17281–17286PubMed

69.

Wan XC, Liu CP, Li M et al (2008) Staphylococcal enterotoxin C injection in combination with ascorbic acid promotes the differentiation of bone marrow-derived mesenchymal stem cells into osteoblasts in vitro. Biochem Biophys Res Commun 373:488–492. https://doi.org/10.1016/j.bbrc.2008.06.037 CrossRefPubMed

70.

Maniatopoulos C, Sodek J, Melcher AH (1988) Bone formation in vitro by stromal cells obtained from bone marrow of young adult rats. Cell Tissue Res 254:317–330CrossRefPubMed

71.

Coelho MJ, Fernandes MH (2000) Human bone cell cultures in biocompatibility testing. Part II: effect of ascorbic acid, beta-glycerophosphate and dexamethasone on osteoblastic differentiation. Biomaterials 21:1095–1102CrossRefPubMed

72.

Mori K, Shioi A, Jono S et al (1999) Dexamethasone enhances In vitro vascular calcification by promoting osteoblastic differentiation of vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 19:2112–2118CrossRefPubMed

73.

Steitz SA, Speer MY, Curinga G et al (2001) Smooth muscle cell phenotypic transition associated with calcification: upregulation of Cbfa1 and downregulation of smooth muscle lineage markers. Circ Res 89:1147–1154CrossRefPubMed

74.

Moe SM, Duan D, Doehle BP et al (2003) Uremia induces the osteoblast differentiation factor Cbfa1 in human blood vessels. Kidney Int 63:1003–1011. https://doi.org/10.1046/j.1523-1755.2003.00820.x CrossRefPubMed

75.

Biber J, Custer M, Magagnin S et al (1996) Renal Na/Pi-cotransporters. Kidney Int 49:981–985CrossRefPubMed

76.

Tenenhouse HS (2007) Phosphate transport: molecular basis, regulation and pathophysiology. J Steroid Biochem Mol Biol 103:572–577. https://doi.org/10.1016/j.jsbmb.2006.12.090 CrossRefPubMed

77.

Virkki LV, Biber J, Murer H et al (2007) Phosphate transporters: a tale of two solute carrier families. Am J Physiol Renal Physiol 293:F643–F654. https://doi.org/10.1152/ajprenal.00228.2007 CrossRefPubMed

78.

Chavkin NW, Chia JJ, Crouthamel MH et al (2015) Phosphate uptake-independent signaling functions of the type III sodium-dependent phosphate transporter, PiT-1, in vascular smooth muscle cells. Exp Cell Res 333:39–48. https://doi.org/10.1016/j.yexcr.2015.02.002 CrossRefPubMedPubMedCentral

79.

Cote N, El Husseini D, Pepin A et al (2012) ATP acts as a survival signal and prevents the mineralization of aortic valve. J Mol Cell Cardiol 52:1191–1202. https://doi.org/10.1016/j.yjmcc.2012.02.003 CrossRefPubMed

80.

Mathieu P, Boulanger MC (2014) Basic mechanisms of calcific aortic valve disease. Can J Cardiol 30:982–993. https://doi.org/10.1016/j.cjca.2014.03.029 CrossRefPubMed

81.

El Husseini D, Boulanger MC, Fournier D et al (2013) High expression of the Pi-transporter SLC20A1/Pit1 in calcific aortic valve disease promotes mineralization through regulation of Akt-1. PLoS ONE 8:e53393. https://doi.org/10.1371/journal.pone.0053393 CrossRefPubMedPubMedCentral

82.

Zhang W, Zhang X, Wang S et al (2013) Comparison of the use of adipose tissue-derived and bone marrow-derived stem cells for rapid bone regeneration. J Dent Res 92:1136–1141. https://doi.org/10.1177/0022034513507581 CrossRefPubMed

83.

Nomura A, Seya K, Yu Z et al (2013) CD34-negative mesenchymal stem-like cells may act as the cellular origin of human aortic valve calcification. Biochem Biophys Res Commun 440:780–785. https://doi.org/10.1016/j.bbrc.2013.10.003 CrossRefPubMed

84.

Consortium, A (2000) Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23. Nat Genet 26:345–348. https://doi.org/10.1038/81664 CrossRef

85.

Shimada T, Mizutani S, Muto T et al (2001) Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc Natl Acad Sci USA 98:6500–6505. https://doi.org/10.1073/pnas.101545198 CrossRefPubMedPubMedCentral

86.

Bai X, Miao D, Li J et al (2004) Transgenic mice overexpressing human fibroblast growth factor 23 (R176Q) delineate a putative role for parathyroid hormone in renal phosphate wasting disorders. Endocrinology 145:5269–5279. https://doi.org/10.1210/en.2004-0233 CrossRefPubMed

87.

Stubbs J, Liu S, Quarles LD (2007) Role of fibroblast growth factor 23 in phosphate homeostasis and pathogenesis of disordered mineral metabolism in chronic kidney disease. Semin Dial 20:302–308. https://doi.org/10.1111/j.1525-139X.2007.00308.x CrossRefPubMed

88.

Kurosu H, Ogawa Y, Miyoshi M et al (2006) Regulation of fibroblast growth factor-23 signaling by klotho. J Biol Chem 281:6120–6123. https://doi.org/10.1074/jbc.C500457200 CrossRefPubMed

89.

Goetz R, Beenken A, Ibrahimi OA et al (2007) Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members. Mol Cell Biol 27:3417–3428. https://doi.org/10.1128/MCB.02249-06 CrossRefPubMedPubMedCentral

90.

Goetz R, Nakada Y, Hu MC et al (2010) Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation. Proc Natl Acad Sci USA 107:407–412. https://doi.org/10.1073/pnas.0902006107 CrossRefPubMed

91.

Urakawa I, Yamazaki Y, Shimada T et al (2006) Klotho converts canonical FGF receptor into a specific receptor for FGF23. Nature 444:770–774. https://doi.org/10.1038/nature05315 CrossRefPubMed

92.

Nakatani T, Sarraj B, Ohnishi M et al (2009) In vivo genetic evidence for klotho-dependent, fibroblast growth factor 23 (Fgf23) -mediated regulation of systemic phosphate homeostasis. FASEB J 23:433–441. https://doi.org/10.1096/fj.08-114397 CrossRefPubMedPubMedCentral

93.

Razzaque MS (2011) Phosphate toxicity: new insights into an old problem. Clin Sci 120:91–97. https://doi.org/10.1042/CS20100377 CrossRef

94.

Razzaque MS (2011) Osteo-renal regulation of systemic phosphate metabolism. IUBMB Life 63:240–247. https://doi.org/10.1002/iub.437 CrossRefPubMedPubMedCentral

95.

Razzaque MS (2009) The FGF23-Klotho axis: endocrine regulation of phosphate homeostasis. Nat Rev Endocrinol 5:611–619. https://doi.org/10.1038/nrendo.2009.196 CrossRefPubMedPubMedCentral

96.

Memon F, El-Abbadi M, Nakatani T et al (2008) Does Fgf23-klotho activity influence vascular and soft tissue calcification through regulating mineral ion metabolism? Kidney Int 74:566–570. https://doi.org/10.1038/ki.2008.218 CrossRefPubMedPubMedCentral

97.

Ichikawa S, Austin AM, Gray AK et al (2011) Dietary phosphate restriction normalizes biochemical and skeletal abnormalities in a murine model of tumoral calcinosis. Endocrinology 152:4504–4513. https://doi.org/10.1210/en.2011-1137 CrossRefPubMedPubMedCentral

98.

Ichikawa S, Gray AK, Padgett LR et al (2014) High dietary phosphate intake induces development of ectopic calcifications in a murine model of familial tumoral calcinosis. J Bone Miner Res 29:2017–2023. https://doi.org/10.1002/jbmr.2242 CrossRefPubMed

99.

El-Abbadi MM, Pai AS, Leaf EM et al (2009) Phosphate feeding induces arterial medial calcification in uremic mice: role of serum phosphorus, fibroblast growth factor-23, and osteopontin. Kidney Int 75:1297–1307. https://doi.org/10.1038/ki.2009.83 CrossRefPubMedPubMedCentral

100.

Zhang R, Li G, Yang L et al (2016) Multiple ectopic calcifications in subcutaneous tissues with chronic renal failure: a case report. Int J Surg Case Rep 29:113–119. https://doi.org/10.1016/j.ijscr.2016.09.041 CrossRefPubMedPubMedCentral

101.

Lau WL, Festing MH, Giachelli CM (2010) Phosphate and vascular calcification: emerging role of the sodium-dependent phosphate co-transporter PiT-1. Thromb Haemost 104:464–470. https://doi.org/10.1160/TH09-12-0814 CrossRefPubMedPubMedCentral

102.

O’Brien KD, Kuusisto J, Reichenbach DD et al (1995) Osteopontin is expressed in human aortic valvular lesions. Circulation 92:2163–2168CrossRefPubMed

103.

Li X, Yang HY, Giachelli CM (2006) Role of the sodium-dependent phosphate cotransporter, Pit-1, in vascular smooth muscle cell calcification. Circ Res 98:905–912. https://doi.org/10.1161/01.RES.0000216409.20863.e7 CrossRefPubMed

104.

Mathew S, Tustison KS, Sugatani T et al (2008) The mechanism of phosphorus as a cardiovascular risk factor in CKD. J Am Soc Nephrol 19:1092–1105. https://doi.org/10.1681/ASN.2007070760 CrossRefPubMedPubMedCentral

105.

Cox RF, Morgan MP (2013) Microcalcifications in breast cancer: lessons from physiological mineralization. Bone 53:437–450. https://doi.org/10.1016/j.bone.2013.01.013 CrossRefPubMed

106.

Rajamannan NM (2011) Serum phosphate concentrations: a novel pre-clinical biomarker for cardiovascular calcification. J Am Coll Cardiol 58:298–299. https://doi.org/10.1016/j.jacc.2011.01.047 CrossRefPubMedPubMedCentral

107.

Mahmut A, Boulanger MC, El Husseini D et al (2014) Elevated expression of lipoprotein-associated phospholipase A2 in calcific aortic valve disease: implications for valve mineralization. J Am Coll Cardiol 63:460–469. https://doi.org/10.1016/j.jacc.2013.05.105 CrossRefPubMed

108.

Thanassoulis G, Campbell CY, Owens DS et al (2013) Genetic associations with valvular calcification and aortic stenosis. N Engl J Med 368:503–512. https://doi.org/10.1056/NEJMoa1109034 CrossRefPubMedPubMedCentral

109.

Kamstrup PR, Tybjaerg-Hansen A, Nordestgaard BG (2014) Elevated lipoprotein(a) and risk of aortic valve stenosis in the general population. J Am Coll Cardiol 63:470–477. https://doi.org/10.1016/j.jacc.2013.09.038 CrossRefPubMed

110.

Abedin M, Lim J, Tang TB et al (2006) N-3 fatty acids inhibit vascular calcification via the p38-mitogen-activated protein kinase and peroxisome proliferator-activated receptor-gamma pathways. Circ Res 98:727–729. https://doi.org/10.1161/01.RES.0000216009.68958.e6 CrossRefPubMed

111.

Kageyama A, Matsui H, Ohta M et al (2013) Palmitic acid induces osteoblastic differentiation in vascular smooth muscle cells through ACSL3 and NF-kappaB, novel targets of eicosapentaenoic acid. PLoS ONE 8:e68197. https://doi.org/10.1371/journal.pone.0068197 CrossRefPubMedPubMedCentral

112.

Bailey MT, Pillarisetti S, Xiao H et al (2003) Role of elastin in pathologic calcification of xenograft heart valves. J Biomed Mater Res, Part A 66:93–102. https://doi.org/10.1002/jbm.a.10543 CrossRef

113.

Dewanjee MK, Solis E, Lanker J et al (1986) Effect of diphosphonate binding to collagen upon inhibition of calcification and promotion of spontaneous endothelial cell coverage on tissue valve prostheses. ASAIO Trans 32:24–29CrossRefPubMed

114.

Shen M, Kara-Mostefa A, Chen L et al (2001) Effect of ethanol and ether in the prevention of calcification of bioprostheses. Ann Thorac Surg 71:S413–S416CrossRefPubMed

115.

Houston B, Seawright E, Jefferies D et al (1999) Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes. Biochem Biophys Acta 1448:500–506CrossRefPubMed

116.

Stewart AJ, Schmid R, Blindauer CA et al (2003) Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily. Protein Eng 16:889–895. https://doi.org/10.1093/protein/gzg126 CrossRefPubMed

117.

Roberts SJ, Stewart AJ, Sadler PJ et al (2004) Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities. Biochem J 382:59–65. https://doi.org/10.1042/BJ20040511 CrossRefPubMedPubMedCentral

118.

Roberts S, Narisawa S, Harmey D et al (2007) Functional involvement of PHOSPHO1 in matrix vesicle-mediated skeletal mineralization. J Bone Miner Res 22:617–627. https://doi.org/10.1359/jbmr.070108 CrossRefPubMed

119.

Stewart AJ, Roberts SJ, Seawright E et al (2006) The presence of PHOSPHO1 in matrix vesicles and its developmental expression prior to skeletal mineralization. Bone 39:1000–1007. https://doi.org/10.1016/j.bone.2006.05.014 CrossRefPubMed

120.

Kvam BJ, Pollesello P, Vittur F et al (1992) 31P NMR studies of resting zone cartilage from growth plate. Magn Reson Med 25:355–361CrossRefPubMed

121.

Yadav MC, Simao AM, Narisawa S et al (2011) Loss of skeletal mineralization by the simultaneous ablation of PHOSPHO1 and alkaline phosphatase function: a unified model of the mechanisms of initiation of skeletal calcification. J Bone Miner Res 26:286–297. https://doi.org/10.1002/jbmr.195 CrossRefPubMed

122.

Huesa C, Yadav MC, Finnila MA et al (2011) PHOSPHO1 is essential for mechanically competent mineralization and the avoidance of spontaneous fractures. Bone 48:1066–1074. https://doi.org/10.1016/j.bone.2011.01.010 CrossRefPubMedPubMedCentral

123.

Kiffer-Moreira T, Yadav MC, Zhu D et al (2013) Pharmacological inhibition of PHOSPHO1 suppresses vascular smooth muscle cell calcification. J Bone Miner Res 28:81–91. https://doi.org/10.1002/jbmr.1733 CrossRefPubMed

124.

Gremse DA (2001) Lansoprazole: pharmacokinetics, pharmacodynamics and clinical uses. Expert Opin Pharmacother 2:1663–1670. https://doi.org/10.1517/14656566.2.10.1663 CrossRefPubMed

125.

Delomenede M, Buchet R, Mebarek S (2009) Lansoprazole is an uncompetitive inhibitor of tissue-nonspecific alkaline phosphatase. Acta Biochim Pol 56:301–305CrossRefPubMed

126.

Cox RF, Hernandez-Santana A, Ramdass S et al (2012) Microcalcifications in breast cancer: novel insights into the molecular mechanism and functional consequence of mammary mineralisation. Br J Cancer 106:525–537. https://doi.org/10.1038/bjc.2011.583 CrossRefPubMedPubMedCentral

127.

Kato H, Mineda K, Eto H et al (2014) Degeneration, regeneration, and cicatrization after fat grafting: dynamic total tissue remodeling during the first 3 months. Plast Reconstr Surg 133:303e–313e. https://doi.org/10.1097/PRS.0000000000000066 CrossRefPubMed

Titel: Recent Advances on Relationship Between Inorganic Phosphate and Pathologic Calcification: Is Calcification After Breast Augmentation with Fat Grafting Correlated with Locally Increased Concentration of Inorganic Phosphate?
verfasst von: Shangshan Li
Jie Luan
Publikationsdatum: 14.12.2018
Verlag: Springer US
Erschienen in: Aesthetic Plastic Surgery / Ausgabe 1/2019
Print ISSN: 0364-216X
Elektronische ISSN: 1432-5241
DOI: https://doi.org/10.1007/s00266-018-1285-9

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Abstract

Background

Methods

Results

Conclusion

Level of Evidence V

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