메뉴 건너뛰기




Volumn 120, Issue 2, 2012, Pages 415-423

Calpain inhibition stabilizes the platelet proteome and reactivity in diabetes

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALPAIN 1; CALPAIN 2; INTEGRIN LINKED KINASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA 2; PIOGLITAZONE; PLACEBO; RANTES; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 2; SEPTIN; SEPTIN 5; SYNTAXIN 4; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 84864066901     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2011-12-399980     Document Type: Article
Times cited : (56)

References (47)
  • 1
    • 79960104591 scopus 로고    scopus 로고
    • Impact of genetic insights into calpain biology
    • Sorimachi H, Hata S, Ono Y. Impact of genetic insights into calpain biology. J Biochem. 2011; 150(1):23-37.
    • (2011) J Biochem , vol.150 , Issue.1 , pp. 23-37
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 2
    • 36148990505 scopus 로고    scopus 로고
    • The calpains: Modular designs and functional diversity
    • Croall D, Ersfeld K. The calpains: modular designs and functional diversity. Genome Biol. 2007;8(6):218.
    • (2007) Genome Biol , vol.8 , Issue.6 , pp. 218
    • Croall, D.1    Ersfeld, K.2
  • 3
    • 0842328803 scopus 로고    scopus 로고
    • Structure, Activation, and Biology of Calpain
    • Suzuki K, Hata S, Kawabata Y, Sorimachi H. Structure, activation, and biology of calpain. Diabetes. 2004;53(90001):S12-S18. (Pubitemid 38168687)
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Suzuki, K.1    Hata, S.2    Kawabata, Y.3    Sorimachi, H.4
  • 4
    • 33748933251 scopus 로고    scopus 로고
    • Subcellular mobility of the calpain/calpastatin network: An organelle transient
    • DOI 10.1002/bies.20440
    • Hood JL, Brooks WH, Roszman TL. Subcellular mobility of the calpain/calpastatin network: an organelle transient. BioEssays. 2006;28(8):850-859. (Pubitemid 44433747)
    • (2006) BioEssays , vol.28 , Issue.8 , pp. 850-859
    • Hood, J.L.1    Brooks, W.H.2    Roszman, T.L.3
  • 5
    • 80054942841 scopus 로고    scopus 로고
    • Calpastatin is regulated by protein never in mitosis gene A interacting-1 (PIN1) in endothelial cells
    • Liu T, Schneider RA, Hoyt DG. Calpastatin is regulated by protein never in mitosis gene A interacting-1 (PIN1) in endothelial cells. Biochem Biophys Res Commun. 2011;414(3):581-586.
    • (2011) Biochem Biophys Res Commun , vol.414 , Issue.3 , pp. 581-586
    • Liu, T.1    Schneider, R.A.2    Hoyt, D.G.3
  • 6
    • 33745829449 scopus 로고    scopus 로고
    • Spatial localization of m-Calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation
    • DOI 10.1128/MCB.02243-05
    • Shao H, Chou J, Baty CJ, et al. Spatial localization of m-calpain to the plasma Membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation. Mol Cell Biol. 2006;26(14):5481-5496. (Pubitemid 44036214)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.14 , pp. 5481-5496
    • Shao, H.1    Chou, J.2    Baty, C.J.3    Burke, N.A.4    Watkins, S.C.5    Stolz, D.B.6    Wells, A.7
  • 7
    • 80053650827 scopus 로고    scopus 로고
    • Calpain interacts with class IA phosphoinositide 3-kinases regulating their stability and signaling activity
    • Beltran L, Chaussade C, Vanhaesebroeck B, Cutillas PR. Calpain interacts with class IA phosphoinositide 3-kinases regulating their stability and signaling activity. Proc Natl Acad Sci U S A. 2011;108(39):16217-16222.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.39 , pp. 16217-16222
    • Beltran, L.1    Chaussade, C.2    Vanhaesebroeck, B.3    Cutillas, P.R.4
  • 8
    • 33644558362 scopus 로고    scopus 로고
    • M-Calpain is required for preimplantation embryonic development in mice
    • Dutt P, Croall D, Arthur JS, et al. m-Calpain is required for preimplantation embryonic development in mice. BMC Dev Biol. 2006;6(1):3.
    • (2006) BMC Dev Biol , vol.6 , Issue.1 , pp. 3
    • Dutt, P.1    Croall, D.2    Arthur, J.S.3
  • 9
    • 80053589785 scopus 로고    scopus 로고
    • Vital role of the calpain-calpastatin system for placental-integrity- dependent embryonic survival
    • Takano J, Mihira N, Fujioka R, et al. Vital role of the calpain-calpastatin system for placental-integrity-dependent embryonic survival. Mol Cell Biol. 2011;31(19):4097-4106.
    • (2011) Mol Cell Biol , vol.31 , Issue.19 , pp. 4097-4106
    • Takano, J.1    Mihira, N.2    Fujioka, R.3
  • 11
    • 34548258220 scopus 로고    scopus 로고
    • Double knockouts reveal that protein tyrosine phosphatase 1B is a physiological target of calpain-1 in platelets
    • DOI 10.1128/MCB.00522-07
    • Kuchay SM, Kim N, Grunz EA, Fay WP, Chishti AH. Double knockouts reveal that protein tyrosine phosphatase 1B is a physiological target of calpain-1 in platelets. Mol Cell Biol. 2007; 27(17):6038-6052. (Pubitemid 47326693)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.17 , pp. 6038-6052
    • Kuchay, S.M.1    Kim, N.2    Grunz, E.A.3    Fay, W.P.4    Chishti, A.H.5
  • 12
    • 37349104971 scopus 로고    scopus 로고
    • Platelet sarcoplasmic endoplasmic reticulum Ca2+-ATPase and mu-calpain activity are altered in type 2 diabetes mellitus and restored by rosiglitazone
    • DOI 10.1161/CIRCULATIONAHA.107.719807
    • Randriamboavonjy V, Pistrosch F, Bolck B, et al. Platelet sarcoplasmic endoplasmic reticulum Ca2+-ATPase and mu-calpain activity are altered in type 2 diabetes mellitus and restored by rosiglitazone. Circulation. 2008;117(1):52-60. (Pubitemid 350291181)
    • (2008) Circulation , vol.117 , Issue.1 , pp. 52-60
    • Randriamboavonjy, V.1    Pistrosch, F.2    Bolck, B.3    Schwinger, R.H.G.4    Dixit, M.5    Badenhoop, K.6    Cohen, R.A.7    Busse, R.8    Fleming, I.9
  • 13
    • 34247148528 scopus 로고    scopus 로고
    • Calpain-mediated regulation of platelet signaling pathways
    • DOI 10.1097/MOH.0b013e3280ef68f8, PII 0006275220070500000012
    • Kuchay SM, Chishti AH. Calpain-mediated regulation of platelet signaling pathways. Curr Opin Hematol. 2007;14(3):249-254. (Pubitemid 46597611)
    • (2007) Current Opinion in Hematology , vol.14 , Issue.3 , pp. 249-254
    • Kuchay, S.M.1    Chishti, A.H.2
  • 14
    • 3042760032 scopus 로고    scopus 로고
    • The effect of pioglitazone on peroxisome proliferator-activated receptor-gamma target genes related to lipid storage in vivo
    • DOI 10.2337/diacare.27.7.1660
    • Bogacka I, Xie H, Bray GA, Smith SR. The effect of pioglitazone on peroxisome proliferator-activated receptor-gamma target genes related to lipid storage in vivo. Diabetes Care. 2004;27(7): 1660-1667. (Pubitemid 38857441)
    • (2004) Diabetes Care , vol.27 , Issue.7 , pp. 1660-1667
    • Bogacka, I.1    Xie, H.2    Bray, G.A.3    Smith, S.R.4
  • 16
    • 34249074463 scopus 로고    scopus 로고
    • Chemokines in vascular remodeling
    • DOI 10.1160/TH07-02-0085
    • Schober A, Zernecke A. Chemokines in vascular remodeling. Thromb Haemost. 2007;97(5):730-737. (Pubitemid 46779958)
    • (2007) Thrombosis and Haemostasis , vol.97 , Issue.5 , pp. 730-737
    • Schober, A.1    Zernecke, A.2
  • 17
    • 78650981490 scopus 로고    scopus 로고
    • Deciphering the human platelet sheddome
    • Fong KP, Barry C, Tran AN, et al. Deciphering the human platelet sheddome. Blood. 2011;117(1): e15-e26.
    • (2011) Blood , vol.117 , Issue.1
    • Fong, K.P.1    Barry, C.2    Tran, A.N.3
  • 20
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad S, Attwell S, Gray V, et al. Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J Biol Chem. 2001;276(29):27462-27469.
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 27462-27469
    • Persad, S.1    Attwell, S.2    Gray, V.3
  • 21
    • 0037115611 scopus 로고    scopus 로고
    • Assembly fo the PINCH-IL-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • DOI 10.1242/jcs.00166
    • Zhang Y, Chen K, Tu Y, et al. Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J Cell Sci. 2002; 115(Pt 24):4777-4786. (Pubitemid 36054631)
    • (2002) Journal of Cell Science , vol.115 , Issue.24 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Velyvis, A.4    Yang, Y.5    Qin, J.6    Wu, C.7
  • 23
    • 77951242361 scopus 로고    scopus 로고
    • Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK)
    • Chan KT, Bennin DA, Huttenlocher A. Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK). J Biol Chem. 2010;285(15):11418-11426.
    • (2010) J Biol Chem , vol.285 , Issue.15 , pp. 11418-11426
    • Chan, K.T.1    Bennin, D.A.2    Huttenlocher, A.3
  • 26
    • 58149336758 scopus 로고    scopus 로고
    • Disrupting functional interactions between platelet chemokines inhibits atherosclerosis in hyperlipidemic mice
    • Koenen RR, von Hundelshausen P, Nesmelova IV, et al. Disrupting functional interactions between platelet chemokines inhibits atherosclerosis in hyperlipidemic mice. Nat Med. 2009;15(1):97-103.
    • (2009) Nat Med , vol.15 , Issue.1 , pp. 97-103
    • Koenen, R.R.1    Von Hundelshausen, P.2    Nesmelova, I.V.3
  • 27
    • 12844273556 scopus 로고    scopus 로고
    • The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex
    • DOI 10.1042/BJ20041090
    • Beites CL, Campbell KA, Trimble WS. The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex. Biochem J. 2005; 385(2):347-353. (Pubitemid 40165066)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 347-353
    • Beites, C.L.1    Campbell, K.A.2    Trimble, W.S.3
  • 29
    • 0033363646 scopus 로고    scopus 로고
    • The septin CDCrel-1 binds syntaxin and inhibits exocytosis
    • DOI 10.1038/8100
    • Beites CL, Xie H, Bowser R, Trimble WS. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat Neurosci. 1999;2(5):434-439. (Pubitemid 30491253)
    • (1999) Nature Neuroscience , vol.2 , Issue.5 , pp. 434-439
    • Beites, C.L.1    Xie, H.2    Bowser, R.3    Trimble, W.S.4
  • 30
    • 38949178835 scopus 로고    scopus 로고
    • Angiogenesis is regulated by a novel mechanism: Pro- and antiangiogenic proteins are organized into separate platelet alpha granules and differentially released
    • DOI 10.1182/blood-2007-09-113837
    • Italiano JE, Jr., Richardson JL, Patel-Hett S, et al. Angiogenesis is regulated by a novel mechanism: pro- and antiangiogenic proteins are organized into separate platelet alpha granules and differentially released. Blood. 2008;111(3):1227-1233. (Pubitemid 351213404)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1227-1233
    • Italiano Jr., J.E.1    Richardson, J.L.2    Patel-Hett, S.3    Battinelli, E.4    Zaslavsky, A.5    Short, S.6    Ryeom, S.7    Folkman, J.8    Klement, G.L.9
  • 31
    • 80051566129 scopus 로고    scopus 로고
    • Release of angiogenesis regulatory proteins from platelet alpha granules: Modulation of physiological and pathological angiogenesis
    • Battinelli EM, Markens BA, Italiano JE. Release of angiogenesis regulatory proteins from platelet alpha granules: modulation of physiological and pathological angiogenesis. Blood. 2011;118(5): 1359-1369.
    • (2011) Blood , vol.118 , Issue.5 , pp. 1359-1369
    • Battinelli, E.M.1    Markens, B.A.2    Italiano, J.E.3
  • 32
    • 77956354082 scopus 로고    scopus 로고
    • Intrapersonal and populational heterogeneity of the chemokine RANTES
    • Oran PE, Sherma ND, Borges CR, Jarvis JW, Nelson RW. Intrapersonal and populational heterogeneity of the chemokine RANTES. Clin Chem. 2010;56(9):1432-1441.
    • (2010) Clin Chem , vol.56 , Issue.9 , pp. 1432-1441
    • Oran, P.E.1    Sherma, N.D.2    Borges, C.R.3    Jarvis, J.W.4    Nelson, R.W.5
  • 33
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • DOI 10.1084/jem.186.11.1865
    • Oravecz T, Pall M, Roderiquez G, et al. Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J Exp Med. 1997;186(11):1865-1872. (Pubitemid 27524596)
    • (1997) Journal of Experimental Medicine , vol.186 , Issue.11 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3    Gorrell, M.D.4    Ditto, M.5    Nguyen, N.Y.6    Boykins, R.7    Unsworth, E.8    Norcross, M.A.9
  • 34
    • 33845418941 scopus 로고    scopus 로고
    • N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
    • DOI 10.1189/jlb.0406290
    • Lim JK, Lu W, Hartley O, DeVico AL. N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant. J Leukoc Biol. 2006;80(6): 1395-1404. (Pubitemid 44904978)
    • (2006) Journal of Leukocyte Biology , vol.80 , Issue.6 , pp. 1395-1404
    • Lim, J.K.1    Lu, W.2    Hartley, O.3    DeVico, A.L.4
  • 36
    • 75049085759 scopus 로고    scopus 로고
    • The ILK/PINCH/Parvin complex: The kinase is dead, long live the pseudokinase!
    • Wickström SA, Lange A, Montanez E, Fassler R. The ILK/PINCH/Parvin complex: the kinase is dead, long live the pseudokinase! EMBO J. 2010; 29(2):281-291.
    • (2010) EMBO J , vol.29 , Issue.2 , pp. 281-291
    • Wickström, S.A.1    Lange, A.2    Montanez, E.3    Fassler, R.4
  • 37
    • 79957552048 scopus 로고    scopus 로고
    • Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK)
    • Fukuda K, Knight JDR, Piszczek G, Kothary R, Qin J. Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK). J Biol Chem. 2011;286(24): 21886-21895.
    • (2011) J Biol Chem , vol.286 , Issue.24 , pp. 21886-21895
    • Fukuda, K.1    Knight, J.D.R.2    Piszczek, G.3    Kothary, R.4    Qin, J.5
  • 39
    • 58149388333 scopus 로고    scopus 로고
    • A dual role for integrin-linked kinase in platelets: Regulating integrin function and alpha-granule secretion
    • Tucker KL, Sage T, Stevens JM, et al. A dual role for integrin-linked kinase in platelets: regulating integrin function and alpha-granule secretion. Blood. 2008;112(12):4523-4531.
    • (2008) Blood , vol.112 , Issue.12 , pp. 4523-4531
    • Tucker, K.L.1    Sage, T.2    Stevens, J.M.3
  • 40
    • 79961131888 scopus 로고    scopus 로고
    • PINCH proteins regulate cardiac contractility by modulating integrin linked kinase-protein kinase B signaling
    • Meder B, Huttner IG, Sedaghat-Hamedani F, et al. PINCH proteins regulate cardiac contractility by modulating integrin linked kinase-protein kinase B signaling. Mol Cell Biol. 2011;31:3424-3435.
    • (2011) Mol Cell Biol , vol.31 , pp. 3424-3435
    • Meder, B.1    Huttner, I.G.2    Sedaghat-Hamedani, F.3
  • 41
    • 78149420565 scopus 로고    scopus 로고
    • Proteins involved in platelet signaling are differentially regulated in acute coronary syndrome: A proteomic study
    • Parguiña AF, Grigorian-Shamajian L, Agra RM, et al. Proteins involved in platelet signaling are differentially regulated in acute coronary syndrome: a proteomic study. PLoS One. 2010; 5(10):e13404.
    • (2010) PLoS One , vol.5 , Issue.10
    • Parguiña, A.F.1    Grigorian-Shamajian, L.2    Agra, R.M.3
  • 42
    • 81755184133 scopus 로고    scopus 로고
    • Variations in platelet proteins associated with ST-elevation myocardial infarction: Novel clues on pathways underlying platelet activation in acute coronary syndromes
    • Parguiña AF, Grigorian-Shamagian L, Agra RM, et al. Variations in platelet proteins associated with ST-elevation myocardial infarction: novel clues on pathways underlying platelet activation in acute coronary syndromes. Arterioscler Thromb Vasc Biol. 2011;31(12):2957-2964.
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , Issue.12 , pp. 2957-2964
    • Parguiña, A.F.1    Grigorian-Shamagian, L.2    Agra, R.M.3
  • 43
    • 76749124869 scopus 로고    scopus 로고
    • A novel calpain inhibitor, ((1S)-1-((((1S)-1-Benzyl-3-cyclopropylamino-2, 3-di-oxopropyl) mino)carbony l)-3-methylbutyl)carbamic acid 5-methoxy-3- oxapentyl ester (SNJ-1945), reduces murine retinal cell death in vitro and in vivo
    • Shimazawa M, Suemori S, Inokuchi Y, et al. A novel calpain inhibitor, ((1S)-1-((((1S)-1-Benzyl-3-cyclopropylamino-2,3-di-oxopropyl) mino)carbony l)-3-methylbutyl)carbamic acid 5-methoxy-3-oxapentyl ester (SNJ-1945), reduces murine retinal cell death in vitro and in vivo. J Pharmacol Exp Ther. 2010;332(2):380-387.
    • (2010) J Pharmacol Exp Ther , vol.332 , Issue.2 , pp. 380-387
    • Shimazawa, M.1    Suemori, S.2    Inokuchi, Y.3
  • 44
    • 33646524709 scopus 로고    scopus 로고
    • The calpain inhibitor, A-705253, corrects penile nitrergic nerve dysfunction in diabetic mice
    • Nangle MR, Cotter MA, Cameron NE. The calpain inhibitor, A-705253, corrects penile nitrergic nerve dysfunction in diabetic mice. Eur J Pharmacol. 2006;538(1-3):148-153.
    • (2006) Eur J Pharmacol , vol.538 , Issue.1-3 , pp. 148-153
    • Nangle, M.R.1    Cotter, M.A.2    Cameron, N.E.3
  • 45
    • 84855342980 scopus 로고    scopus 로고
    • Calpain inhibition attenuates angiotensin II-induced abdominal aortic aneurysms and atherosclerosis in LDL receptor deficient mice
    • Subramanian V, Uchida HA, Ijaz T, et al. Calpain inhibition attenuates angiotensin II-induced abdominal aortic aneurysms and atherosclerosis in LDL receptor deficient mice. J Cardiovasc Pharmacol. 2012;59(1):66-76.
    • (2012) J Cardiovasc Pharmacol , vol.59 , Issue.1 , pp. 66-76
    • Subramanian, V.1    Uchida, H.A.2    Ijaz, T.3
  • 46
    • 79955612468 scopus 로고    scopus 로고
    • A novel role for calpain in the endothelial dysfunction induced by activation of angiotensin II type 1 receptor signaling / novelty and significance
    • Scalia R, Gong Y, Berzins B, et al. A novel role for calpain in the endothelial dysfunction induced by activation of angiotensin II type 1 receptor signaling / novelty and significance. Circ Res. 2011; 108(9):1102-1111.
    • (2011) Circ Res , vol.108 , Issue.9 , pp. 1102-1111
    • Scalia, R.1    Gong, Y.2    Berzins, B.3
  • 47
    • 79955106083 scopus 로고    scopus 로고
    • Calpain inhibitors: A survey of compounds reported in the patent and scientific literature
    • Donkor IO. Calpain inhibitors: a survey of compounds reported in the patent and scientific literature. Expert Opin Ther Pat. 2011;21(5):601-636.
    • (2011) Expert Opin Ther Pat , vol.21 , Issue.5 , pp. 601-636
    • Donkor, I.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.