Skip to main content
Erschienen in: Immunologic Research 1/2021

23.01.2021 | Review

Effects of functionally diverse calpain system on immune cells

verfasst von: Yueqi Chen, Zhaoliang Su, Fang Liu

Erschienen in: Immunologic Research | Ausgabe 1/2021

Einloggen, um Zugang zu erhalten

Abstract

Calpains are a family of nonlysosomal cysteine proteases, which play important roles in numerous physiological and pathological processes. Locations of them dictates the functions so that they are classified as ubiquitously expressed calpains and tissue-specific calpains. Recent studies are mainly focused on conventional calpains (calpain-1,2) in development and diseases, and increasing people pay attention to other subtypes of calpains but may not been summarized appropriately. Growing evidence suggests that calpains are also involved in immune regulation. However, seldom articles review the regulation of calpains on immune cells. The aim of this article is to review the research progress of each calpain isozyme and the effect of calpains on immune cells, especially the promotion effect of calpains on the immune response of macrophage, neutrophils, dendritic cells, mast cells, natural killed cells, and lymphocytes. These effects would hold great promise for the clinical application of calpains as a practicable therapeutic option in the treatment of immune related diseases.
Literatur
1.
Zurück zum Zitat Araujo H, Julio A, Cardoso M. Translating genetic, biochemical and structural information to the calpain view of development. Mech Dev. 2018;154:240–50.PubMedCrossRef Araujo H, Julio A, Cardoso M. Translating genetic, biochemical and structural information to the calpain view of development. Mech Dev. 2018;154:240–50.PubMedCrossRef
2.
Zurück zum Zitat Tamtaji OR, Mirhosseini N, Reiter RJ, Azami A, Asemi Z. Melatonin, a calpain inhibitor in the central nervous system: current status and future perspectives. J Cell Physiol. 2019;234(2):1001–7.PubMedCrossRef Tamtaji OR, Mirhosseini N, Reiter RJ, Azami A, Asemi Z. Melatonin, a calpain inhibitor in the central nervous system: current status and future perspectives. J Cell Physiol. 2019;234(2):1001–7.PubMedCrossRef
3.
Zurück zum Zitat Mahaman YAR, Huang F, Kessete Afewerky H, Maibouge TMS, Ghose B, Wang X. Involvement of calpain in the neuropathogenesis of Alzheimer's disease. Med Res Rev. 2019;39(2):608–30.PubMedCrossRef Mahaman YAR, Huang F, Kessete Afewerky H, Maibouge TMS, Ghose B, Wang X. Involvement of calpain in the neuropathogenesis of Alzheimer's disease. Med Res Rev. 2019;39(2):608–30.PubMedCrossRef
4.
Zurück zum Zitat Nevzorova TA, Mordakhanova ER, Daminova AG, Ponomareva AA, Andrianova IA, Le Minh G, et al. Platelet factor 4-containing immune complexes induce platelet activation followed by calpain-dependent platelet death. Cell Death Discov. 2019;5:106.PubMedPubMedCentralCrossRef Nevzorova TA, Mordakhanova ER, Daminova AG, Ponomareva AA, Andrianova IA, Le Minh G, et al. Platelet factor 4-containing immune complexes induce platelet activation followed by calpain-dependent platelet death. Cell Death Discov. 2019;5:106.PubMedPubMedCentralCrossRef
5.
Zurück zum Zitat Miyazaki T, Akasu R, Miyazaki A. Calpain proteolytic systems counteract endothelial cell adaptation to inflammatory environments. Inflamm Regen. 2020;40:5.PubMedPubMedCentralCrossRef Miyazaki T, Akasu R, Miyazaki A. Calpain proteolytic systems counteract endothelial cell adaptation to inflammatory environments. Inflamm Regen. 2020;40:5.PubMedPubMedCentralCrossRef
6.
Zurück zum Zitat Ding ZJ, Chen X, Tang XX, Wang X, Song YL, Chen XD, et al. Apoptosis-inducing factor and calpain upregulation in glutamate-induced injury of rat spiral ganglion neurons. Mol Med Rep. 2015;12(2):1685–92.PubMedPubMedCentralCrossRef Ding ZJ, Chen X, Tang XX, Wang X, Song YL, Chen XD, et al. Apoptosis-inducing factor and calpain upregulation in glutamate-induced injury of rat spiral ganglion neurons. Mol Med Rep. 2015;12(2):1685–92.PubMedPubMedCentralCrossRef
7.
Zurück zum Zitat Dimeloe S, Burgener AV, Grahlert J, Hess C. T-cell metabolism governing activation, proliferation and differentiation; a modular view. Immunology. 2017;150(1):35–44.PubMedCrossRef Dimeloe S, Burgener AV, Grahlert J, Hess C. T-cell metabolism governing activation, proliferation and differentiation; a modular view. Immunology. 2017;150(1):35–44.PubMedCrossRef
8.
Zurück zum Zitat Liu H, Chen R, Kang F, Lai H, Wang Y. KCNQ1OT1 promotes ovarian cancer progression via modulating MIR-142-5p/CAPN10 axis. Mol Genet Genomic Med. 2020;8(2):e1077.PubMedPubMedCentralCrossRef Liu H, Chen R, Kang F, Lai H, Wang Y. KCNQ1OT1 promotes ovarian cancer progression via modulating MIR-142-5p/CAPN10 axis. Mol Genet Genomic Med. 2020;8(2):e1077.PubMedPubMedCentralCrossRef
9.
Zurück zum Zitat Wang T, Gao Y, Wang X, Shi Y, Xu J, Wu B, et al. Calpain-10 drives podocyte apoptosis and renal injury in diabetic nephropathy. Diabetes Metab Syndr Obes. 2019;12:1811–20.PubMedPubMedCentralCrossRef Wang T, Gao Y, Wang X, Shi Y, Xu J, Wu B, et al. Calpain-10 drives podocyte apoptosis and renal injury in diabetic nephropathy. Diabetes Metab Syndr Obes. 2019;12:1811–20.PubMedPubMedCentralCrossRef
10.
Zurück zum Zitat Wert KJ, Skeie JM, Bassuk AG, Olivier AK, Tsang SH, Mahajan VB. Functional validation of a human CAPN5 exome variant by lentiviral transduction into mouse retina. Hum Mol Genet. 2014;23(10):2665–77.PubMedCrossRef Wert KJ, Skeie JM, Bassuk AG, Olivier AK, Tsang SH, Mahajan VB. Functional validation of a human CAPN5 exome variant by lentiviral transduction into mouse retina. Hum Mol Genet. 2014;23(10):2665–77.PubMedCrossRef
11.
Zurück zum Zitat Richard I, Broux O, Allamand V, Fougerousse F, Chiannilkulchai N, Bourg N, et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 1995;81(1):27–40.PubMedCrossRef Richard I, Broux O, Allamand V, Fougerousse F, Chiannilkulchai N, Bourg N, et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 1995;81(1):27–40.PubMedCrossRef
12.
Zurück zum Zitat Meng Y, Sun T, Wu C, Dong C, Xiong S. Calpain regulates CVB3 induced viral myocarditis by promoting autophagic flux upon infection. Microbes Infect. 2020;22(1):46–54.PubMedCrossRef Meng Y, Sun T, Wu C, Dong C, Xiong S. Calpain regulates CVB3 induced viral myocarditis by promoting autophagic flux upon infection. Microbes Infect. 2020;22(1):46–54.PubMedCrossRef
13.
Zurück zum Zitat Ono Y, Sorimachi H. Calpains: an elaborate proteolytic system. Biochim Biophys Acta. 2012;1824(1):224–36.PubMedCrossRef Ono Y, Sorimachi H. Calpains: an elaborate proteolytic system. Biochim Biophys Acta. 2012;1824(1):224–36.PubMedCrossRef
14.
Zurück zum Zitat Kim D, Beckett J, Nagpal V, Seman-Senderos M, Gould R, Creamer T, et al. Calpain 9 as a therapeutic target in TGFβ-induced mesenchymal transition and fibrosis. Sci Transl Med. 2019;11(501):eaau2814.PubMedPubMedCentralCrossRef Kim D, Beckett J, Nagpal V, Seman-Senderos M, Gould R, Creamer T, et al. Calpain 9 as a therapeutic target in TGFβ-induced mesenchymal transition and fibrosis. Sci Transl Med. 2019;11(501):eaau2814.PubMedPubMedCentralCrossRef
16.
Zurück zum Zitat Hosseini M, Najmabadi H, Kahrizi K. Calpains: diverse functions but enigmatic. Arch Iran Med. 2018;21(4):170–9.PubMed Hosseini M, Najmabadi H, Kahrizi K. Calpains: diverse functions but enigmatic. Arch Iran Med. 2018;21(4):170–9.PubMed
17.
Zurück zum Zitat Sorimachi H, Mamitsuka H, Ono Y. Understanding the substrate specificity of conventional calpains. Biol Chem. 2012;393(9):853–71.PubMedCrossRef Sorimachi H, Mamitsuka H, Ono Y. Understanding the substrate specificity of conventional calpains. Biol Chem. 2012;393(9):853–71.PubMedCrossRef
18.
Zurück zum Zitat Wang Y, Bi X, Baudry M. Calpain-2 as a therapeutic target for acute neuronal injury. Expert Opin Ther Targets. 2018;22(1):19–29.PubMedCrossRef Wang Y, Bi X, Baudry M. Calpain-2 as a therapeutic target for acute neuronal injury. Expert Opin Ther Targets. 2018;22(1):19–29.PubMedCrossRef
19.
Zurück zum Zitat Nie Q, Zhu L, Zhang L, Leng B, Wang H. Astragaloside IV protects against hyperglycemia-induced vascular endothelial dysfunction by inhibiting oxidative stress and Calpain-1 activation. Life Sci. 2019;232:116662.PubMedCrossRef Nie Q, Zhu L, Zhang L, Leng B, Wang H. Astragaloside IV protects against hyperglycemia-induced vascular endothelial dysfunction by inhibiting oxidative stress and Calpain-1 activation. Life Sci. 2019;232:116662.PubMedCrossRef
20.
Zurück zum Zitat Siuda D, Randriamboavonjy V, Fleming I. Regulation of calpain 2 expression by miR-223 and miR-145. Biochim Biophys Acta Gene Regul Mech. 2019;1862(10):194438.PubMedCrossRef Siuda D, Randriamboavonjy V, Fleming I. Regulation of calpain 2 expression by miR-223 and miR-145. Biochim Biophys Acta Gene Regul Mech. 2019;1862(10):194438.PubMedCrossRef
21.
Zurück zum Zitat Bruening J, Lasswitz L, Banse P, Kahl S, Marinach C, Vondran FW, et al. Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB. PLoS Pathog. 2018;14(7):e1007111.PubMedPubMedCentralCrossRef Bruening J, Lasswitz L, Banse P, Kahl S, Marinach C, Vondran FW, et al. Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB. PLoS Pathog. 2018;14(7):e1007111.PubMedPubMedCentralCrossRef
22.
Zurück zum Zitat Schaefer KA, Toral MA, Velez G, Cox AJ, Baker SA, Borcherding NC, et al. Calpain-5 expression in the retina localizes to photoreceptor synapses. Invest Ophthalmol Vis Sci. 2016;57(6):2509–21.PubMedPubMedCentralCrossRef Schaefer KA, Toral MA, Velez G, Cox AJ, Baker SA, Borcherding NC, et al. Calpain-5 expression in the retina localizes to photoreceptor synapses. Invest Ophthalmol Vis Sci. 2016;57(6):2509–21.PubMedPubMedCentralCrossRef
23.
24.
Zurück zum Zitat Yan Q, Huang C, Jiang Y, Shan H, Jiang R, Wang J, et al. Calpain7 impairs embryo implantation by downregulating beta3-integrin expression via degradation of HOXA10. Cell Death Dis. 2018;9(3):291.PubMedPubMedCentralCrossRef Yan Q, Huang C, Jiang Y, Shan H, Jiang R, Wang J, et al. Calpain7 impairs embryo implantation by downregulating beta3-integrin expression via degradation of HOXA10. Cell Death Dis. 2018;9(3):291.PubMedPubMedCentralCrossRef
25.
Zurück zum Zitat Li Z, Wang S, Huo X, Yu H, Lu J, Zhang S, et al. Cystatin C expression is promoted by VEGFA blocking, with inhibitory effects on endothelial cell Angiogenic functions including proliferation, migration, and Chorioallantoic membrane angiogenesis. J Am Heart Assoc. 2018;7(21):e009167.PubMedPubMedCentralCrossRef Li Z, Wang S, Huo X, Yu H, Lu J, Zhang S, et al. Cystatin C expression is promoted by VEGFA blocking, with inhibitory effects on endothelial cell Angiogenic functions including proliferation, migration, and Chorioallantoic membrane angiogenesis. J Am Heart Assoc. 2018;7(21):e009167.PubMedPubMedCentralCrossRef
26.
Zurück zum Zitat Mo HY, Choi EJ, Yoo NJ, Lee SH. Inactivating mutations of tumor suppressor genes ABCA1 and CAPN13 in colorectal cancers. Pathol Res Pract. 2020;216(5):152870.PubMedCrossRef Mo HY, Choi EJ, Yoo NJ, Lee SH. Inactivating mutations of tumor suppressor genes ABCA1 and CAPN13 in colorectal cancers. Pathol Res Pract. 2020;216(5):152870.PubMedCrossRef
27.
Zurück zum Zitat Hastings MH, Qiu A, Zha C, Farah CA, Mahdid Y, Ferguson L, et al. The zinc fingers of the small optic lobes calpain bind polyubiquitin. J Neurochem. 2018;146(4):429–45.PubMedCrossRef Hastings MH, Qiu A, Zha C, Farah CA, Mahdid Y, Ferguson L, et al. The zinc fingers of the small optic lobes calpain bind polyubiquitin. J Neurochem. 2018;146(4):429–45.PubMedCrossRef
28.
Zurück zum Zitat Kramerova I, Torres JA, Eskin A, Nelson SF, Spencer MJ. Calpain 3 and CaMKIIbeta signaling are required to induce HSP70 necessary for adaptive muscle growth after atrophy. Hum Mol Genet. 2018;27(9):1642–53.PubMedPubMedCentralCrossRef Kramerova I, Torres JA, Eskin A, Nelson SF, Spencer MJ. Calpain 3 and CaMKIIbeta signaling are required to induce HSP70 necessary for adaptive muscle growth after atrophy. Hum Mol Genet. 2018;27(9):1642–53.PubMedPubMedCentralCrossRef
29.
Zurück zum Zitat Ono Y, Ojima K, Shinkai-Ouchi F, Hata S, Sorimachi H. An eccentric calpain, CAPN3/p94/calpain-3. Biochimie. 2016;122:169–87.PubMedCrossRef Ono Y, Ojima K, Shinkai-Ouchi F, Hata S, Sorimachi H. An eccentric calpain, CAPN3/p94/calpain-3. Biochimie. 2016;122:169–87.PubMedCrossRef
30.
Zurück zum Zitat Miyazaki T, Miyazaki A. Emerging roles of calpain proteolytic systems in macrophage cholesterol handling. Cell Mol Life Sci. 2017;74(16):3011–21.PubMedCrossRef Miyazaki T, Miyazaki A. Emerging roles of calpain proteolytic systems in macrophage cholesterol handling. Cell Mol Life Sci. 2017;74(16):3011–21.PubMedCrossRef
32.
Zurück zum Zitat Bochner R, Samuelov L, Sarig O, Li Q, Adase CA, Isakov O, et al. Calpain 12 function revealed through the study of an atypical case of autosomal recessive congenital Ichthyosis. J Invest Dermatol. 2017;137(2):385–93.PubMedCrossRef Bochner R, Samuelov L, Sarig O, Li Q, Adase CA, Isakov O, et al. Calpain 12 function revealed through the study of an atypical case of autosomal recessive congenital Ichthyosis. J Invest Dermatol. 2017;137(2):385–93.PubMedCrossRef
33.
Zurück zum Zitat V.A. Litosh, M. Rochman, J.K. Rymer, A. Porollo, L.C. Kottyan, M.E. Rothenberg, Calpain-14 and its association with eosinophilic esophagitis, J Allergy Clin Immunol, 139 (6) (2017) 1762–1771 e1767. V.A. Litosh, M. Rochman, J.K. Rymer, A. Porollo, L.C. Kottyan, M.E. Rothenberg, Calpain-14 and its association with eosinophilic esophagitis, J Allergy Clin Immunol, 139 (6) (2017) 1762–1771 e1767.
34.
Zurück zum Zitat Guan Y, Huang D, Chen F, Gao C, Tao T, Shi H, et al. Phosphorylation of Def regulates Nucleolar p53 turnover and cell cycle progression through Def recruitment of Calpain3. PLoS Biol. 2016;14(9):e1002555.PubMedPubMedCentralCrossRef Guan Y, Huang D, Chen F, Gao C, Tao T, Shi H, et al. Phosphorylation of Def regulates Nucleolar p53 turnover and cell cycle progression through Def recruitment of Calpain3. PLoS Biol. 2016;14(9):e1002555.PubMedPubMedCentralCrossRef
35.
Zurück zum Zitat Hood JL, Logan BB, Sinai AP, Brooks WH, Roszman TL. Association of the calpain/calpastatin network with subcellular organelles. Biochem Biophys Res Commun. 2003;310(4):1200–12.PubMedCrossRef Hood JL, Logan BB, Sinai AP, Brooks WH, Roszman TL. Association of the calpain/calpastatin network with subcellular organelles. Biochem Biophys Res Commun. 2003;310(4):1200–12.PubMedCrossRef
36.
Zurück zum Zitat Ozaki T, Tomita H, Tamai M, Ishiguro S. Characteristics of mitochondrial calpains. J Biochem. 2007;142(3):365–76.PubMedCrossRef Ozaki T, Tomita H, Tamai M, Ishiguro S. Characteristics of mitochondrial calpains. J Biochem. 2007;142(3):365–76.PubMedCrossRef
37.
Zurück zum Zitat Arrington DD, Van Vleet TR, Schnellmann RG. Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction. Am J Physiol Cell Physiol. 2006;291(6):C1159–71.PubMedCrossRef Arrington DD, Van Vleet TR, Schnellmann RG. Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction. Am J Physiol Cell Physiol. 2006;291(6):C1159–71.PubMedCrossRef
38.
Zurück zum Zitat Arias A, Lucendo AJ. Molecular basis and cellular mechanisms of eosinophilic esophagitis for the clinical practice. Expert Rev Gastroenterol Hepatol. 2019;13(2):99–117.PubMedCrossRef Arias A, Lucendo AJ. Molecular basis and cellular mechanisms of eosinophilic esophagitis for the clinical practice. Expert Rev Gastroenterol Hepatol. 2019;13(2):99–117.PubMedCrossRef
40.
Zurück zum Zitat Maki M. Structures and functions of penta-EF-hand calcium-binding proteins and their interacting partners: enigmatic relationships between ALG-2 and calpain-7. Biosci Biotechnol Biochem. 2020;84(4):651–60.PubMedCrossRef Maki M. Structures and functions of penta-EF-hand calcium-binding proteins and their interacting partners: enigmatic relationships between ALG-2 and calpain-7. Biosci Biotechnol Biochem. 2020;84(4):651–60.PubMedCrossRef
41.
Zurück zum Zitat Brown AE, Yeaman SJ, Walker M. Targeted suppression of calpain-10 expression impairs insulin-stimulated glucose uptake in cultured primary human skeletal muscle cells. Mol Genet Metab. 2007;91(4):318–24.PubMedCrossRef Brown AE, Yeaman SJ, Walker M. Targeted suppression of calpain-10 expression impairs insulin-stimulated glucose uptake in cultured primary human skeletal muscle cells. Mol Genet Metab. 2007;91(4):318–24.PubMedCrossRef
42.
Zurück zum Zitat Hong JM, Teitelbaum SL, Kim TH, Ross FP, Kim SY, Kim HJ. Calpain-6, a target molecule of glucocorticoids, regulates osteoclastic bone resorption via cytoskeletal organization and microtubule acetylation. J Bone Miner Res. 2011;26(3):657–65.PubMedCrossRef Hong JM, Teitelbaum SL, Kim TH, Ross FP, Kim SY, Kim HJ. Calpain-6, a target molecule of glucocorticoids, regulates osteoclastic bone resorption via cytoskeletal organization and microtubule acetylation. J Bone Miner Res. 2011;26(3):657–65.PubMedCrossRef
43.
Zurück zum Zitat Hata S, Abe M, Suzuki H, Kitamura F, Toyama-Sorimachi N, Abe K, et al. Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense. PLoS Genet. 2010;6(7):e1001040.PubMedPubMedCentralCrossRef Hata S, Abe M, Suzuki H, Kitamura F, Toyama-Sorimachi N, Abe K, et al. Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense. PLoS Genet. 2010;6(7):e1001040.PubMedPubMedCentralCrossRef
44.
Zurück zum Zitat Davis J, Martin S, Patel P, Green A, Rakha E, Ellis I, et al. Low calpain-9 is associated with adverse disease-specific survival following endocrine therapy in breast cancer. BMC Cancer. 2014;14:995.PubMedPubMedCentralCrossRef Davis J, Martin S, Patel P, Green A, Rakha E, Ellis I, et al. Low calpain-9 is associated with adverse disease-specific survival following endocrine therapy in breast cancer. BMC Cancer. 2014;14:995.PubMedPubMedCentralCrossRef
45.
Zurück zum Zitat Chang YS, Hsu MJ, Chou RR. Postmortem role of calpain-11 in ostrich skeletal muscle. Meat Sci. 2018;143:147–52.PubMedCrossRef Chang YS, Hsu MJ, Chou RR. Postmortem role of calpain-11 in ostrich skeletal muscle. Meat Sci. 2018;143:147–52.PubMedCrossRef
46.
Zurück zum Zitat Kumar V, Ahmad A. Targeting calpains: a novel immunomodulatory approach for microbial infections. Eur J Pharmacol. 2017;814:28–44.PubMedCrossRef Kumar V, Ahmad A. Targeting calpains: a novel immunomodulatory approach for microbial infections. Eur J Pharmacol. 2017;814:28–44.PubMedCrossRef
47.
Zurück zum Zitat Schaecher K, Goust J, Banik N. The effects of calpain inhibition on IkB alpha degradation after activation of PBMCs: identification of the calpain cleavage sites. Neurochem Res. 2004;29(7):1443–51.PubMedCrossRef Schaecher K, Goust J, Banik N. The effects of calpain inhibition on IkB alpha degradation after activation of PBMCs: identification of the calpain cleavage sites. Neurochem Res. 2004;29(7):1443–51.PubMedCrossRef
48.
Zurück zum Zitat Sasahara Y. WASP-WIP complex in the molecular pathogenesis of Wiskott-Aldrich syndrome. Pediatr Int. 2016;58(1):4–7.PubMedCrossRef Sasahara Y. WASP-WIP complex in the molecular pathogenesis of Wiskott-Aldrich syndrome. Pediatr Int. 2016;58(1):4–7.PubMedCrossRef
49.
Zurück zum Zitat Penna D, Muller S, Martinon F, Demotz S, Iwashima M, Valitutti S. Degradation of ZAP-70 following antigenic stimulation in human T lymphocytes: role of calpain proteolytic pathway. J Immunol. 1999;163(1):50–6.PubMedCrossRef Penna D, Muller S, Martinon F, Demotz S, Iwashima M, Valitutti S. Degradation of ZAP-70 following antigenic stimulation in human T lymphocytes: role of calpain proteolytic pathway. J Immunol. 1999;163(1):50–6.PubMedCrossRef
50.
Zurück zum Zitat Liu CSC, Raychaudhuri D, Paul B, Chakrabarty Y, Ghosh AR, Rahaman O, et al. Cutting edge: Piezo1 Mechanosensors optimize human T cell activation. J Immunol. 2018;200(4):1255–60.PubMedCrossRef Liu CSC, Raychaudhuri D, Paul B, Chakrabarty Y, Ghosh AR, Rahaman O, et al. Cutting edge: Piezo1 Mechanosensors optimize human T cell activation. J Immunol. 2018;200(4):1255–60.PubMedCrossRef
51.
Zurück zum Zitat Rock MT, Dix AR, Brooks WH, Roszman TL. Beta1 integrin-mediated T cell adhesion and cell spreading are regulated by calpain. Exp Cell Res. 2000;261(1):260–70.PubMedCrossRef Rock MT, Dix AR, Brooks WH, Roszman TL. Beta1 integrin-mediated T cell adhesion and cell spreading are regulated by calpain. Exp Cell Res. 2000;261(1):260–70.PubMedCrossRef
52.
Zurück zum Zitat Chen J, Ganguly A, Mucsi AD, Meng J, Yan J, Detampel P, et al. Strong adhesion by regulatory T cells induces dendritic cell cytoskeletal polarization and contact-dependent lethargy. J Exp Med. 2017;214(2):327–38.PubMedPubMedCentralCrossRef Chen J, Ganguly A, Mucsi AD, Meng J, Yan J, Detampel P, et al. Strong adhesion by regulatory T cells induces dendritic cell cytoskeletal polarization and contact-dependent lethargy. J Exp Med. 2017;214(2):327–38.PubMedPubMedCentralCrossRef
53.
Zurück zum Zitat Wan F, Letavernier E, Le Saux CJ, Houssaini A, Abid S, Czibik G, et al. Calpastatin overexpression impairs postinfarct scar healing in mice by compromising reparative immune cell recruitment and activation. Am J Physiol Heart Circ Physiol. 2015;309(11):H1883–93.PubMedCrossRef Wan F, Letavernier E, Le Saux CJ, Houssaini A, Abid S, Czibik G, et al. Calpastatin overexpression impairs postinfarct scar healing in mice by compromising reparative immune cell recruitment and activation. Am J Physiol Heart Circ Physiol. 2015;309(11):H1883–93.PubMedCrossRef
54.
Zurück zum Zitat Witkowski JM, Bryl E. Paradoxical age-related cell cycle quickening of human CD4(+) lymphocytes: a role for cyclin D1 and calpain. Exp Gerontol. 2004;39(4):577–85.PubMedCrossRef Witkowski JM, Bryl E. Paradoxical age-related cell cycle quickening of human CD4(+) lymphocytes: a role for cyclin D1 and calpain. Exp Gerontol. 2004;39(4):577–85.PubMedCrossRef
55.
Zurück zum Zitat Smith AW, Doonan BP, Tyor WR, Abou-Fayssal N, Haque A, Banik NL. Regulation of Th1/Th17 cytokines and IDO gene expression by inhibition of calpain in PBMCs from MS patients. J Neuroimmunol. 2011;232(1–2):179–85.PubMedCrossRef Smith AW, Doonan BP, Tyor WR, Abou-Fayssal N, Haque A, Banik NL. Regulation of Th1/Th17 cytokines and IDO gene expression by inhibition of calpain in PBMCs from MS patients. J Neuroimmunol. 2011;232(1–2):179–85.PubMedCrossRef
56.
Zurück zum Zitat Selliah N, Brooks WH, Roszman TL. Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody. J Immunol. 1996;156(9):3215–21.PubMedCrossRef Selliah N, Brooks WH, Roszman TL. Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody. J Immunol. 1996;156(9):3215–21.PubMedCrossRef
57.
Zurück zum Zitat Witkowski JM, Zmuda-Trzebiatowska E, Swiercz JM, Cichorek M, Ciepluch H, Lewandowski K, et al. Modulation of the activity of calcium-activated neutral proteases (calpains) in chronic lymphocytic leukemia (B-CLL) cells. Blood. 2002;100(5):1802–9.PubMedCrossRef Witkowski JM, Zmuda-Trzebiatowska E, Swiercz JM, Cichorek M, Ciepluch H, Lewandowski K, et al. Modulation of the activity of calcium-activated neutral proteases (calpains) in chronic lymphocytic leukemia (B-CLL) cells. Blood. 2002;100(5):1802–9.PubMedCrossRef
58.
Zurück zum Zitat Mikosik A, Henc I, Ruckemann-Dziurdzinska K, Frackowiak JE, Ploszynska A, Balcerska A, et al. Increased mu-Calpain activity in blasts of common B-precursor childhood acute lymphoblastic leukemia correlates with their lower susceptibility to apoptosis. PLoS One. 2015;10(8):e0136615.PubMedPubMedCentralCrossRef Mikosik A, Henc I, Ruckemann-Dziurdzinska K, Frackowiak JE, Ploszynska A, Balcerska A, et al. Increased mu-Calpain activity in blasts of common B-precursor childhood acute lymphoblastic leukemia correlates with their lower susceptibility to apoptosis. PLoS One. 2015;10(8):e0136615.PubMedPubMedCentralCrossRef
59.
Zurück zum Zitat Nassar D, Letavernier E, Baud L, Aractingi S, Khosrotehrani K. Calpain activity is essential in skin wound healing and contributes to scar formation. PLoS One. 2012;7(5):e37084.PubMedPubMedCentralCrossRef Nassar D, Letavernier E, Baud L, Aractingi S, Khosrotehrani K. Calpain activity is essential in skin wound healing and contributes to scar formation. PLoS One. 2012;7(5):e37084.PubMedPubMedCentralCrossRef
60.
Zurück zum Zitat Mikosik A, Jasiulewicz A, Daca A, Henc I, Frackowiak JE, Ruckemann-Dziurdzinska K, et al. Roles of calpain-calpastatin system (CCS) in human T cell activation. Oncotarget. 2016;7(47):76479–95.PubMedPubMedCentralCrossRef Mikosik A, Jasiulewicz A, Daca A, Henc I, Frackowiak JE, Ruckemann-Dziurdzinska K, et al. Roles of calpain-calpastatin system (CCS) in human T cell activation. Oncotarget. 2016;7(47):76479–95.PubMedPubMedCentralCrossRef
61.
Zurück zum Zitat Noma H, Kato T, Fujita H, Kitagawa M, Yamano T, Kitagawa S. Calpain inhibition induces activation of the distinct signalling pathways and cell migration in human monocytes. Immunology. 2009;128(1 Suppl):e487–96.PubMedPubMedCentralCrossRef Noma H, Kato T, Fujita H, Kitagawa M, Yamano T, Kitagawa S. Calpain inhibition induces activation of the distinct signalling pathways and cell migration in human monocytes. Immunology. 2009;128(1 Suppl):e487–96.PubMedPubMedCentralCrossRef
63.
Zurück zum Zitat Goldmann O, Sastalla I, Wos-Oxley M, Rohde M, Medina E. Streptococcus pyogenes induces oncosis in macrophages through the activation of an inflammatory programmed cell death pathway. Cell Microbiol. 2009;11(1):138–55.PubMedCrossRef Goldmann O, Sastalla I, Wos-Oxley M, Rohde M, Medina E. Streptococcus pyogenes induces oncosis in macrophages through the activation of an inflammatory programmed cell death pathway. Cell Microbiol. 2009;11(1):138–55.PubMedCrossRef
64.
Zurück zum Zitat Rana T, Misra S, Mittal MK, Farrow AL, Wilson KT, Linton MF, et al. Mechanism of down-regulation of RNA polymerase III-transcribed non-coding RNA genes in macrophages by Leishmania. J Biol Chem. 2011;286(8):6614–26.PubMedCrossRef Rana T, Misra S, Mittal MK, Farrow AL, Wilson KT, Linton MF, et al. Mechanism of down-regulation of RNA polymerase III-transcribed non-coding RNA genes in macrophages by Leishmania. J Biol Chem. 2011;286(8):6614–26.PubMedCrossRef
65.
Zurück zum Zitat P.S. de Sousa Araújo, S.S.C. de Oliveira, C.M. d’Avila-Levy, A.L.S. dos Santos, M.H. Branquinha, Susceptibility of promastigotes and intracellular amastigotes from distinct Leishmania species to the calpain inhibitor MDL28170, Parasitol Res, 117 (7) (2018) 2085–2094. P.S. de Sousa Araújo, S.S.C. de Oliveira, C.M. d’Avila-Levy, A.L.S. dos Santos, M.H. Branquinha, Susceptibility of promastigotes and intracellular amastigotes from distinct Leishmania species to the calpain inhibitor MDL28170, Parasitol Res, 117 (7) (2018) 2085–2094.
66.
Zurück zum Zitat Cirone M. EBV and KSHV infection Dysregulates autophagy to optimize viral replication, prevent immune recognition and promote tumorigenesis. Viruses. 2018;10(11). Cirone M. EBV and KSHV infection Dysregulates autophagy to optimize viral replication, prevent immune recognition and promote tumorigenesis. Viruses. 2018;10(11).
67.
Zurück zum Zitat Takano E, Park YH, Kitahara A, Yamagata Y, Kannagi R, Murachi T. Distribution of calpains and calpastatin in human blood cells. Biochem Int. 1988;16(3):391–5.PubMed Takano E, Park YH, Kitahara A, Yamagata Y, Kannagi R, Murachi T. Distribution of calpains and calpastatin in human blood cells. Biochem Int. 1988;16(3):391–5.PubMed
68.
Zurück zum Zitat Miyazaki T, Koya T, Kigawa Y, Oguchi T, Lei XF, Kim-Kaneyama JR, et al. Calpain and atherosclerosis. J Atheroscler Thromb. 2013;20(3):228–37.PubMedCrossRef Miyazaki T, Koya T, Kigawa Y, Oguchi T, Lei XF, Kim-Kaneyama JR, et al. Calpain and atherosclerosis. J Atheroscler Thromb. 2013;20(3):228–37.PubMedCrossRef
69.
Zurück zum Zitat T. Miyazaki, K. Tonami, S. Hata, T. Aiuchi, K. Ohnishi, X.-F. Lei, J.-r. Kim-Kaneyama, M. Takeya, H. Itabe, H. Sorimachi, H. Kurihara, A. Miyazaki, Calpain-6 confers atherogenicity to macrophages by dysregulating pre-mRNA splicing, J Clin Investig, 126 (9) (2016) 3417–3432. T. Miyazaki, K. Tonami, S. Hata, T. Aiuchi, K. Ohnishi, X.-F. Lei, J.-r. Kim-Kaneyama, M. Takeya, H. Itabe, H. Sorimachi, H. Kurihara, A. Miyazaki, Calpain-6 confers atherogenicity to macrophages by dysregulating pre-mRNA splicing, J Clin Investig, 126 (9) (2016) 3417–3432.
70.
Zurück zum Zitat Wang N, Chen W, Linsel-Nitschke P, Martinez LO, Agerholm-Larsen B, Silver DL, et al. A PEST sequence in ABCA1 regulates degradation by calpain protease and stabilization of ABCA1 by apoA-I. J Clin Invest. 2003;111(1):99–107.PubMedPubMedCentralCrossRef Wang N, Chen W, Linsel-Nitschke P, Martinez LO, Agerholm-Larsen B, Silver DL, et al. A PEST sequence in ABCA1 regulates degradation by calpain protease and stabilization of ABCA1 by apoA-I. J Clin Invest. 2003;111(1):99–107.PubMedPubMedCentralCrossRef
71.
Zurück zum Zitat Hori N, Hayashi H, Sugiyama Y. Calpain-mediated cleavage negatively regulates the expression level of ABCG1. Atherosclerosis. 2011;215(2):383–91.PubMedCrossRef Hori N, Hayashi H, Sugiyama Y. Calpain-mediated cleavage negatively regulates the expression level of ABCG1. Atherosclerosis. 2011;215(2):383–91.PubMedCrossRef
72.
Zurück zum Zitat Yang X, Yin M, Yu L, Lu M, Wang H, Tang F, et al. Simvastatin inhibited oxLDL-induced proatherogenic effects through calpain-1-PPARgamma-CD36 pathway. Can J Physiol Pharmacol. 2016;94(12):1336–43.PubMedCrossRef Yang X, Yin M, Yu L, Lu M, Wang H, Tang F, et al. Simvastatin inhibited oxLDL-induced proatherogenic effects through calpain-1-PPARgamma-CD36 pathway. Can J Physiol Pharmacol. 2016;94(12):1336–43.PubMedCrossRef
74.
Zurück zum Zitat Dewitt S, Francis RJ, Hallett MB. Ca(2)(+) and calpain control membrane expansion during the rapid cell spreading of neutrophils. J Cell Sci. 2013;126(Pt 20):4627–35.PubMedPubMedCentral Dewitt S, Francis RJ, Hallett MB. Ca(2)(+) and calpain control membrane expansion during the rapid cell spreading of neutrophils. J Cell Sci. 2013;126(Pt 20):4627–35.PubMedPubMedCentral
75.
Zurück zum Zitat Roberts RE, Hallett MB. Neutrophil cell shape change: mechanism and Signalling during cell spreading and phagocytosis. Int J Mol Sci. 2019;20(6). Roberts RE, Hallett MB. Neutrophil cell shape change: mechanism and Signalling during cell spreading and phagocytosis. Int J Mol Sci. 2019;20(6).
76.
Zurück zum Zitat Lewis KJ, Masterman B, Laffafian I, Dewitt S, Campbell JS, Hallett MB. Minimal impact electro-injection of cells undergoing dynamic shape change reveals calpain activation. Biochim Biophys Acta. 2014;1843(6):1182–7.PubMedCrossRef Lewis KJ, Masterman B, Laffafian I, Dewitt S, Campbell JS, Hallett MB. Minimal impact electro-injection of cells undergoing dynamic shape change reveals calpain activation. Biochim Biophys Acta. 2014;1843(6):1182–7.PubMedCrossRef
77.
Zurück zum Zitat Ishak R, Hallett MB. Defective rapid cell shape and transendothelial migration by calpain-1 null neutrophils. Biochem Biophys Res Commun. 2018;506(4):1065–70.PubMedCrossRef Ishak R, Hallett MB. Defective rapid cell shape and transendothelial migration by calpain-1 null neutrophils. Biochem Biophys Res Commun. 2018;506(4):1065–70.PubMedCrossRef
78.
Zurück zum Zitat Liu D, Yan Z, Minshall RD, Schwartz DE, Chen Y, Hu G. Activation of calpains mediates early lung neutrophilic inflammation in ventilator-induced lung injury. Am J Physiol Lung Cell Mol Physiol. 2012;302(4):L370–9.PubMedCrossRef Liu D, Yan Z, Minshall RD, Schwartz DE, Chen Y, Hu G. Activation of calpains mediates early lung neutrophilic inflammation in ventilator-induced lung injury. Am J Physiol Lung Cell Mol Physiol. 2012;302(4):L370–9.PubMedCrossRef
79.
Zurück zum Zitat Xu E, Chen J, Wang Y, Ke Z, Luo S, Zou Z. A phosphoproteomic study reveals shp-1 cleavage reprograms LPS signaling via a PI-3K/NF-kappaB and mTORC1 related mechanism. J Proteome. 2015;128:30–8.CrossRef Xu E, Chen J, Wang Y, Ke Z, Luo S, Zou Z. A phosphoproteomic study reveals shp-1 cleavage reprograms LPS signaling via a PI-3K/NF-kappaB and mTORC1 related mechanism. J Proteome. 2015;128:30–8.CrossRef
80.
Zurück zum Zitat White MM, Geraghty P, Hayes E, Cox S, Leitch W, Alfawaz B, et al. Neutrophil membrane cholesterol content is a key factor in cystic fibrosis lung disease. EBioMedicine. 2017;23:173–84.PubMedPubMedCentralCrossRef White MM, Geraghty P, Hayes E, Cox S, Leitch W, Alfawaz B, et al. Neutrophil membrane cholesterol content is a key factor in cystic fibrosis lung disease. EBioMedicine. 2017;23:173–84.PubMedPubMedCentralCrossRef
81.
Zurück zum Zitat Wiemer AJ, Lokuta MA, Surfus JC, Wernimont SA, Huttenlocher A. Calpain inhibition impairs TNF-alpha-mediated neutrophil adhesion, arrest and oxidative burst. Mol Immunol. 2010;47(4):894–902.PubMedCrossRef Wiemer AJ, Lokuta MA, Surfus JC, Wernimont SA, Huttenlocher A. Calpain inhibition impairs TNF-alpha-mediated neutrophil adhesion, arrest and oxidative burst. Mol Immunol. 2010;47(4):894–902.PubMedCrossRef
82.
Zurück zum Zitat Campbell JS, Hallett MB. Active calpain in phagocytically competent human neutrophils: electroinjection of fluorogenic calpain substrate. Biochem Biophys Res Commun. 2015;457(3):341–6.PubMedCrossRef Campbell JS, Hallett MB. Active calpain in phagocytically competent human neutrophils: electroinjection of fluorogenic calpain substrate. Biochem Biophys Res Commun. 2015;457(3):341–6.PubMedCrossRef
83.
Zurück zum Zitat Kumar V, Everingham S, Hall C, Greer PA, Craig AW. Calpains promote neutrophil recruitment and bacterial clearance in an acute bacterial peritonitis model. Eur J Immunol. 2014;44(3):831–41.PubMedCrossRef Kumar V, Everingham S, Hall C, Greer PA, Craig AW. Calpains promote neutrophil recruitment and bacterial clearance in an acute bacterial peritonitis model. Eur J Immunol. 2014;44(3):831–41.PubMedCrossRef
84.
Zurück zum Zitat Tanabe F, Kasai H, He L, Kin T, Fujikado T, Kumamoto T, et al. Improvement of deficient natural killer activity and delayed bactericidal activity by a thiol proteinase inhibitor, E-64-d, in leukocytes from Chediak-Higashi syndrome patients in vitro. Int Immunopharmacol. 2009;9(3):366–70.PubMedCrossRef Tanabe F, Kasai H, He L, Kin T, Fujikado T, Kumamoto T, et al. Improvement of deficient natural killer activity and delayed bactericidal activity by a thiol proteinase inhibitor, E-64-d, in leukocytes from Chediak-Higashi syndrome patients in vitro. Int Immunopharmacol. 2009;9(3):366–70.PubMedCrossRef
85.
Zurück zum Zitat Gosswein S, Lindemann A, Mahajan A, Maueroder C, Martini E, Patankar J, et al. Citrullination licenses Calpain to Decondense nuclei in neutrophil extracellular trap formation. Front Immunol. 2019;10:2481.PubMedPubMedCentralCrossRef Gosswein S, Lindemann A, Mahajan A, Maueroder C, Martini E, Patankar J, et al. Citrullination licenses Calpain to Decondense nuclei in neutrophil extracellular trap formation. Front Immunol. 2019;10:2481.PubMedPubMedCentralCrossRef
86.
Zurück zum Zitat Wang GJ, Wang Y, Teng YS, Sun FL, Xiang H, Liu JJ, et al. Protective effects of Emodin-induced neutrophil apoptosis via the Ca(2+)-Caspase 12 pathway against SIRS in rats with severe acute pancreatitis. Biomed Res Int. 2016;2016:1736024.PubMedPubMedCentralCrossRef Wang GJ, Wang Y, Teng YS, Sun FL, Xiang H, Liu JJ, et al. Protective effects of Emodin-induced neutrophil apoptosis via the Ca(2+)-Caspase 12 pathway against SIRS in rats with severe acute pancreatitis. Biomed Res Int. 2016;2016:1736024.PubMedPubMedCentralCrossRef
87.
Zurück zum Zitat van Raam BJ, Drewniak A, Groenewold V, van den Berg TK, Kuijpers TW. Granulocyte colony-stimulating factor delays neutrophil apoptosis by inhibition of calpains upstream of caspase-3. Blood. 2008;112(5):2046–54.PubMedPubMedCentralCrossRef van Raam BJ, Drewniak A, Groenewold V, van den Berg TK, Kuijpers TW. Granulocyte colony-stimulating factor delays neutrophil apoptosis by inhibition of calpains upstream of caspase-3. Blood. 2008;112(5):2046–54.PubMedPubMedCentralCrossRef
88.
Zurück zum Zitat McCracken J, Kinkead L, McCaffrey R, Allen L. Francisella tularensis modulates a distinct subset of regulatory factors and sustains mitochondrial integrity to impair human neutrophil apoptosis. Journal of innate immunity. 2016;8(3):299–313.PubMedPubMedCentralCrossRef McCracken J, Kinkead L, McCaffrey R, Allen L. Francisella tularensis modulates a distinct subset of regulatory factors and sustains mitochondrial integrity to impair human neutrophil apoptosis. Journal of innate immunity. 2016;8(3):299–313.PubMedPubMedCentralCrossRef
89.
Zurück zum Zitat Francis RJ, Kotecha S, Hallett MB. Ca2+ activation of cytosolic calpain induces the transition from apoptosis to necrosis in neutrophils with externalized phosphatidylserine. J Leukoc Biol. 2013;93(1):95–100.PubMedCrossRef Francis RJ, Kotecha S, Hallett MB. Ca2+ activation of cytosolic calpain induces the transition from apoptosis to necrosis in neutrophils with externalized phosphatidylserine. J Leukoc Biol. 2013;93(1):95–100.PubMedCrossRef
90.
Zurück zum Zitat Francis RJ, Butler RE, Stewart GR. Mycobacterium tuberculosis ESAT-6 is a leukocidin causing Ca2+ influx, necrosis and neutrophil extracellular trap formation. Cell Death Dis. 2014;5:e1474.PubMedPubMedCentralCrossRef Francis RJ, Butler RE, Stewart GR. Mycobacterium tuberculosis ESAT-6 is a leukocidin causing Ca2+ influx, necrosis and neutrophil extracellular trap formation. Cell Death Dis. 2014;5:e1474.PubMedPubMedCentralCrossRef
92.
Zurück zum Zitat Calle Y, Carragher NO, Thrasher AJ, Jones GE. Inhibition of calpain stabilises podosomes and impairs dendritic cell motility. J Cell Sci. 2006;119(Pt 11):2375–85.PubMedCrossRef Calle Y, Carragher NO, Thrasher AJ, Jones GE. Inhibition of calpain stabilises podosomes and impairs dendritic cell motility. J Cell Sci. 2006;119(Pt 11):2375–85.PubMedCrossRef
93.
Zurück zum Zitat Chou HC, Anton IM, Holt MR, Curcio C, Lanzardo S, Worth A, et al. WIP regulates the stability and localization of WASP to podosomes in migrating dendritic cells. Curr Biol. 2006;16(23):2337–44.PubMedPubMedCentralCrossRef Chou HC, Anton IM, Holt MR, Curcio C, Lanzardo S, Worth A, et al. WIP regulates the stability and localization of WASP to podosomes in migrating dendritic cells. Curr Biol. 2006;16(23):2337–44.PubMedPubMedCentralCrossRef
94.
Zurück zum Zitat Sorrentino R, Terlizzi M, Di Crescenzo VG, Popolo A, Pecoraro M, Perillo G, et al. Human lung cancer-derived immunosuppressive plasmacytoid dendritic cells release IL-1alpha in an AIM2 inflammasome-dependent manner. Am J Pathol. 2015;185(11):3115–24.PubMedCrossRef Sorrentino R, Terlizzi M, Di Crescenzo VG, Popolo A, Pecoraro M, Perillo G, et al. Human lung cancer-derived immunosuppressive plasmacytoid dendritic cells release IL-1alpha in an AIM2 inflammasome-dependent manner. Am J Pathol. 2015;185(11):3115–24.PubMedCrossRef
95.
Zurück zum Zitat Hamel-Cote G, Gendron D, Rola-Pleszczynski M, Stankova J. Regulation of platelet-activating factor-mediated protein tyrosine phosphatase 1B activation by a Janus kinase 2/calpain pathway. PLoS One. 2017;12(7):e0180336.PubMedPubMedCentralCrossRef Hamel-Cote G, Gendron D, Rola-Pleszczynski M, Stankova J. Regulation of platelet-activating factor-mediated protein tyrosine phosphatase 1B activation by a Janus kinase 2/calpain pathway. PLoS One. 2017;12(7):e0180336.PubMedPubMedCentralCrossRef
96.
Zurück zum Zitat Meephansan J, Tsuda H, Komine M, Tominaga S, Ohtsuki M. Regulation of IL-33 expression by IFN-gamma and tumor necrosis factor-alpha in normal human epidermal keratinocytes. J Invest Dermatol. 2012;132(11):2593–600.PubMedCrossRef Meephansan J, Tsuda H, Komine M, Tominaga S, Ohtsuki M. Regulation of IL-33 expression by IFN-gamma and tumor necrosis factor-alpha in normal human epidermal keratinocytes. J Invest Dermatol. 2012;132(11):2593–600.PubMedCrossRef
97.
Zurück zum Zitat Wu Z, Chen X, Liu F, Chen W, Wu P, Wieschhaus AJ, et al. Calpain-1 contributes to IgE-mediated mast cell activation. J Immunol. 2014;192(11):5130–9.PubMedCrossRef Wu Z, Chen X, Liu F, Chen W, Wu P, Wieschhaus AJ, et al. Calpain-1 contributes to IgE-mediated mast cell activation. J Immunol. 2014;192(11):5130–9.PubMedCrossRef
98.
Zurück zum Zitat Selvakumar GP, Ahmed ME, Thangavel R, Kempuraj D, Dubova I, Raikwar SP, et al. A role for glia maturation factor dependent activation of mast cells and microglia in MPTP induced dopamine loss and behavioural deficits in mice. Brain Behav Immun. 2020;87:429–43.PubMedPubMedCentralCrossRef Selvakumar GP, Ahmed ME, Thangavel R, Kempuraj D, Dubova I, Raikwar SP, et al. A role for glia maturation factor dependent activation of mast cells and microglia in MPTP induced dopamine loss and behavioural deficits in mice. Brain Behav Immun. 2020;87:429–43.PubMedPubMedCentralCrossRef
99.
Zurück zum Zitat Forsythe P, Befus AD. Inhibition of calpain is a component of nitric oxide-induced down-regulation of human mast cell adhesion. J Immunol. 2003;170(1):287–93.PubMedCrossRef Forsythe P, Befus AD. Inhibition of calpain is a component of nitric oxide-induced down-regulation of human mast cell adhesion. J Immunol. 2003;170(1):287–93.PubMedCrossRef
100.
Zurück zum Zitat Hendry L, John S. Regulation of STAT signalling by proteolytic processing. Eur J Biochem. 2004;271(23–24):4613–20.PubMedCrossRef Hendry L, John S. Regulation of STAT signalling by proteolytic processing. Eur J Biochem. 2004;271(23–24):4613–20.PubMedCrossRef
101.
Zurück zum Zitat Blom W, de Bont H, Mulder G, Nagelkerke J. The role of calpains in apoptotic changes in isolated hepatocytes after attack by natural killer cells. Environ Toxicol Pharmacol. 2002;11:159–65.PubMedCrossRef Blom W, de Bont H, Mulder G, Nagelkerke J. The role of calpains in apoptotic changes in isolated hepatocytes after attack by natural killer cells. Environ Toxicol Pharmacol. 2002;11:159–65.PubMedCrossRef
102.
Zurück zum Zitat Shenoy AM, Brahmi Z. Inhibition of the calpain-mediated proteolysis of protein kinase C enhances lytic activity in human NK cells. Cell Immunol. 1991;138(1):24–34.PubMedCrossRef Shenoy AM, Brahmi Z. Inhibition of the calpain-mediated proteolysis of protein kinase C enhances lytic activity in human NK cells. Cell Immunol. 1991;138(1):24–34.PubMedCrossRef
103.
Zurück zum Zitat Tanabe F, Cui S, Ito M. Abnormal down-regulation of PKC is responsible for giant granule formation in fibroblasts from CHS (beige) mice--a thiol proteinase inhibitor, E-64-d, prevents giant granule formation in beige fibroblasts. J Leukoc Biol. 2000;67(5):749–55.PubMedCrossRef Tanabe F, Cui S, Ito M. Abnormal down-regulation of PKC is responsible for giant granule formation in fibroblasts from CHS (beige) mice--a thiol proteinase inhibitor, E-64-d, prevents giant granule formation in beige fibroblasts. J Leukoc Biol. 2000;67(5):749–55.PubMedCrossRef
104.
Zurück zum Zitat Cui S, Tanabe F, Terunuma H, Iwatani Y, Nunoi H, Agematsu K, et al. A thiol proteinase inhibitor, E-64-d, corrects the abnormalities in concanavalin a cap formation and the lysosomal enzyme activity in leucocytes from patients with Chediak-Higashi syndrome by reversing the down-regulated protein kinase C activity. Clin Exp Immunol. 2001;125(2):283–90.PubMedPubMedCentralCrossRef Cui S, Tanabe F, Terunuma H, Iwatani Y, Nunoi H, Agematsu K, et al. A thiol proteinase inhibitor, E-64-d, corrects the abnormalities in concanavalin a cap formation and the lysosomal enzyme activity in leucocytes from patients with Chediak-Higashi syndrome by reversing the down-regulated protein kinase C activity. Clin Exp Immunol. 2001;125(2):283–90.PubMedPubMedCentralCrossRef
105.
Zurück zum Zitat Mikosik A, Zaremba A, Puchalska Z, Daca A, Smolenska Z, Lopatniuk P, et al. Ex vivo measurement of calpain activation in human peripheral blood lymphocytes by detection of immunoreactive products of calpastatin degradation. Folia Histochem Cytobiol. 2007;45(4):343–7.PubMed Mikosik A, Zaremba A, Puchalska Z, Daca A, Smolenska Z, Lopatniuk P, et al. Ex vivo measurement of calpain activation in human peripheral blood lymphocytes by detection of immunoreactive products of calpastatin degradation. Folia Histochem Cytobiol. 2007;45(4):343–7.PubMed
106.
Zurück zum Zitat Mikosik A, Foerster J, Jasiulewicz A, Frackowiak J, Colonna-Romano G, Bulati M, et al. Expression of calpain-calpastatin system (CCS) member proteins in human lymphocytes of young and elderly individuals; pilot baseline data for the CALPACENT project. Immun Ageing. 2013;10(1):27.PubMedPubMedCentralCrossRef Mikosik A, Foerster J, Jasiulewicz A, Frackowiak J, Colonna-Romano G, Bulati M, et al. Expression of calpain-calpastatin system (CCS) member proteins in human lymphocytes of young and elderly individuals; pilot baseline data for the CALPACENT project. Immun Ageing. 2013;10(1):27.PubMedPubMedCentralCrossRef
107.
Zurück zum Zitat Salazar AM, Panico P, Burns AL, Diaz-Villasenor A, Torres-Arellano JM, Juarez-Najera A, et al. Calpain activity in leukocytes is associated with diabetes biochemical markers. Arch Med Res. 2019;50(7):451–60.PubMedCrossRef Salazar AM, Panico P, Burns AL, Diaz-Villasenor A, Torres-Arellano JM, Juarez-Najera A, et al. Calpain activity in leukocytes is associated with diabetes biochemical markers. Arch Med Res. 2019;50(7):451–60.PubMedCrossRef
108.
Zurück zum Zitat Svensson L, McDowall A, Giles KM, Stanley P, Feske S, Hogg N. Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes. PLoS One. 2010;5(11):e15090.PubMedPubMedCentralCrossRef Svensson L, McDowall A, Giles KM, Stanley P, Feske S, Hogg N. Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes. PLoS One. 2010;5(11):e15090.PubMedPubMedCentralCrossRef
109.
Zurück zum Zitat Babich A, Burkhardt JK. Coordinate control of cytoskeletal remodeling and calcium mobilization during T-cell activation. Immunol Rev. 2013;256(1):80–94.PubMedCrossRef Babich A, Burkhardt JK. Coordinate control of cytoskeletal remodeling and calcium mobilization during T-cell activation. Immunol Rev. 2013;256(1):80–94.PubMedCrossRef
110.
Zurück zum Zitat Lim D, Lu Y, Rudd CE. Non-cleavable Talin rescues defect in the T-cell conjugation of T-cells deficient in the immune adaptor SKAP1. Immunol Lett. 2016;172:40–6.PubMedPubMedCentralCrossRef Lim D, Lu Y, Rudd CE. Non-cleavable Talin rescues defect in the T-cell conjugation of T-cells deficient in the immune adaptor SKAP1. Immunol Lett. 2016;172:40–6.PubMedPubMedCentralCrossRef
111.
Zurück zum Zitat Iguchi-Hashimoto M, Usui T, Yoshifuji H, Shimizu M, Kobayashi S, Ito Y, et al. Overexpression of a minimal domain of calpastatin suppresses IL-6 production and Th17 development via reduced NF-kappaB and increased STAT5 signals. PLoS One. 2011;6(10):e27020.PubMedPubMedCentralCrossRef Iguchi-Hashimoto M, Usui T, Yoshifuji H, Shimizu M, Kobayashi S, Ito Y, et al. Overexpression of a minimal domain of calpastatin suppresses IL-6 production and Th17 development via reduced NF-kappaB and increased STAT5 signals. PLoS One. 2011;6(10):e27020.PubMedPubMedCentralCrossRef
112.
Zurück zum Zitat Gasperi V, Rapino C, Battista N, Bari M, Mastrangelo N, Angeletti S, et al. A functional interplay between 5-lipoxygenase and mu-calpain affects survival and cytokine profile of human Jurkat T lymphocyte exposed to simulated microgravity. Biomed Res Int. 2014;2014:782390.PubMedPubMedCentralCrossRef Gasperi V, Rapino C, Battista N, Bari M, Mastrangelo N, Angeletti S, et al. A functional interplay between 5-lipoxygenase and mu-calpain affects survival and cytokine profile of human Jurkat T lymphocyte exposed to simulated microgravity. Biomed Res Int. 2014;2014:782390.PubMedPubMedCentralCrossRef
113.
Zurück zum Zitat Paul DS, Harmon AW, Winston CP, Patel YM. Calpain facilitates GLUT4 vesicle translocation during insulin-stimulated glucose uptake in adipocytes. Biochem J. 2003;376(Pt 3):625–32.PubMedPubMedCentralCrossRef Paul DS, Harmon AW, Winston CP, Patel YM. Calpain facilitates GLUT4 vesicle translocation during insulin-stimulated glucose uptake in adipocytes. Biochem J. 2003;376(Pt 3):625–32.PubMedPubMedCentralCrossRef
114.
Zurück zum Zitat Panico P, Juarez-Najera A, Iturriaga-Goyon E, Ostrosky-Wegman P, Salazar AM. Arsenic impairs GLUT1 trafficking through the inhibition of the calpain system in lymphocytes. Toxicol Appl Pharmacol. 2019;380:114700.PubMedCrossRef Panico P, Juarez-Najera A, Iturriaga-Goyon E, Ostrosky-Wegman P, Salazar AM. Arsenic impairs GLUT1 trafficking through the inhibition of the calpain system in lymphocytes. Toxicol Appl Pharmacol. 2019;380:114700.PubMedCrossRef
Metadaten
Titel
Effects of functionally diverse calpain system on immune cells
verfasst von
Yueqi Chen
Zhaoliang Su
Fang Liu
Publikationsdatum
23.01.2021
Verlag
Springer US
Erschienen in
Immunologic Research / Ausgabe 1/2021
Print ISSN: 0257-277X
Elektronische ISSN: 1559-0755
DOI
https://doi.org/10.1007/s12026-021-09177-5

Weitere Artikel der Ausgabe 1/2021

Immunologic Research 1/2021 Zur Ausgabe

Erhebliches Risiko für Kehlkopfkrebs bei mäßiger Dysplasie

29.05.2024 Larynxkarzinom Nachrichten

Fast ein Viertel der Personen mit mäßig dysplastischen Stimmlippenläsionen entwickelt einen Kehlkopftumor. Solche Personen benötigen daher eine besonders enge ärztliche Überwachung.

Hörschwäche erhöht Demenzrisiko unabhängig von Beta-Amyloid

29.05.2024 Hörstörungen Nachrichten

Hört jemand im Alter schlecht, nimmt das Hirn- und Hippocampusvolumen besonders schnell ab, was auch mit einem beschleunigten kognitiven Abbau einhergeht. Und diese Prozesse scheinen sich unabhängig von der Amyloidablagerung zu ereignen.

„Übersichtlicher Wegweiser“: Lauterbachs umstrittener Klinik-Atlas ist online

17.05.2024 Klinik aktuell Nachrichten

Sie sei „ethisch geboten“, meint Gesundheitsminister Karl Lauterbach: mehr Transparenz über die Qualität von Klinikbehandlungen. Um sie abzubilden, lässt er gegen den Widerstand vieler Länder einen virtuellen Klinik-Atlas freischalten.

Betalaktam-Allergie: praxisnahes Vorgehen beim Delabeling

16.05.2024 Pädiatrische Allergologie Nachrichten

Die große Mehrheit der vermeintlichen Penicillinallergien sind keine. Da das „Etikett“ Betalaktam-Allergie oft schon in der Kindheit erworben wird, kann ein frühzeitiges Delabeling lebenslange Vorteile bringen. Ein Team von Pädiaterinnen und Pädiatern aus Kanada stellt vor, wie sie dabei vorgehen.

Update HNO

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert – ganz bequem per eMail.