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Volumn 117, Issue 18, 2011, Pages 4978-4987

The integrin coactivator Kindlin-2 plays a critical role in angiogenesis in mice and zebrafish

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENESIS MODULATOR; BETA1 INTEGRIN; BETA3 INTEGRIN; CYTOSKELETON PROTEIN; INTEGRIN; KINDLIN 2; MORPHOLINE DERIVATIVE; UNCLASSIFIED DRUG; VASCULOTROPIN; VASCULOTROPIN RECEPTOR; VITRONECTIN RECEPTOR;

EID: 79955980408     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-11-321182     Document Type: Article
Times cited : (67)

References (51)
  • 1
    • 32944463899 scopus 로고    scopus 로고
    • Angiogenesis
    • DOI 10.1146/annurev.med.57.121304.131306
    • Folkman J. Angiogenesis. Annu Rev Med. 2006;57:1-18. (Pubitemid 43261975)
    • (2006) Annual Review of Medicine , vol.57 , pp. 1-18
    • Folkman, J.1
  • 2
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell. 2002;110(6):673-687. (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 3
    • 0036734093 scopus 로고    scopus 로고
    • Areevaluation of integrins as regulators of angiogenesis
    • Hynes RO.Areevaluation of integrins as regulators of angiogenesis. Nat Med. 2002;8(9):918-921.
    • (2002) Nat Med , vol.8 , Issue.9 , pp. 918-921
    • Hynes, R.O.1
  • 6
    • 0033636606 scopus 로고    scopus 로고
    • A mechanism for modulation of cellular responses to VEGF: Activation of the integrins
    • Byzova TV, Goldman CK, Pampori N, et al. A mechanism for modulation of cellular responses to VEGF: activation of the integrins. Mol Cell. 2000;6(4):851-860.
    • (2000) Mol Cell , vol.6 , Issue.4 , pp. 851-860
    • Byzova, T.V.1    Goldman, C.K.2    Pampori, N.3
  • 8
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M, Legate KR, Zent R, Fassler R. The tail of integrins, talin, and kindlins. Science. 2009;324(5929):895-899.
    • (2009) Science , vol.324 , Issue.5929 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 9
    • 69549114537 scopus 로고    scopus 로고
    • Kindling the flame of integrin activation and function with kindlins
    • Plow EF, Qin J, Byzova T. Kindling the flame of integrin activation and function with kindlins. Curr Opin Hematol. 2009;16(5):323-328.
    • (2009) Curr Opin Hematol , vol.16 , Issue.5 , pp. 323-328
    • Plow, E.F.1    Qin, J.2    Byzova, T.3
  • 10
    • 77953233840 scopus 로고    scopus 로고
    • Kindlins in FERM adhesion
    • Malinin NL, Plow EF, Byzova TV. Kindlins in FERM adhesion. Blood. 2010;115(20):4011-4017.
    • (2010) Blood , vol.115 , Issue.20 , pp. 4011-4017
    • Malinin, N.L.1    Plow, E.F.2    Byzova, T.V.3
  • 11
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • DOI 10.1242/jcs.01014
    • Calderwood DA. Integrin activation. J Cell Sci. 2004;117(Pt 5):657-666. (Pubitemid 38268081)
    • (2004) Journal of Cell Science , vol.117 , Issue.5 , pp. 657-666
    • Calderwood, D.A.1
  • 13
    • 43149085289 scopus 로고    scopus 로고
    • 3 integrins
    • DOI 10.1083/jcb.200710196
    • Ma YQ, Qin J, Wu C, Plow EF. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J Cell Biol. 2008;181(3):439-446. (Pubitemid 351645034)
    • (2008) Journal of Cell Biology , vol.181 , Issue.3 , pp. 439-446
    • Ma, Y.-Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 14
    • 58149154658 scopus 로고    scopus 로고
    • Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction
    • Ussar S, Moser M, Widmaier M, et al. Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction. PLoS Genet. 2008;4(12):e1000289.
    • (2008) PLoS Genet , vol.4 , Issue.12
    • Ussar, S.1    Moser, M.2    Widmaier, M.3
  • 15
    • 61949240364 scopus 로고    scopus 로고
    • A point mutation in kindlin-3 ablates activation of three integrin subfamilies in humans
    • Malinin NL, Zhang L, Choi J, et al. A point mutation in kindlin-3 ablates activation of three integrin subfamilies in humans. Nat Med. 2009;15(3):313-318.
    • (2009) Nat Med , vol.15 , Issue.3 , pp. 313-318
    • Malinin, N.L.1    Zhang, L.2    Choi, J.3
  • 16
    • 61949086409 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
    • Svensson L, Howarth K, McDowall A, et al. Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med. 2009;15(3):306-312.
    • (2009) Nat Med , vol.15 , Issue.3 , pp. 306-312
    • Svensson, L.1    Howarth, K.2    McDowall, A.3
  • 17
    • 77953317401 scopus 로고    scopus 로고
    • The integrin coactivator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell
    • Bialkowska K, Ma YQ, Bledzka K, et al. The integrin coactivator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell. J Biol Chem. 2010;285(24):18640-18649.
    • (2010) J Biol Chem , vol.285 , Issue.24 , pp. 18640-18649
    • Bialkowska, K.1    Ma, Y.Q.2    Bledzka, K.3
  • 18
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: New members to the club of focal adhesion proteins
    • Meves A, Stremmel C, Gottschalk K, Fassler R. The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol. 2009;19(10):504-513.
    • (2009) Trends Cell Biol , vol.19 , Issue.10 , pp. 504-513
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fassler, R.4
  • 19
    • 84980115073 scopus 로고
    • Congenital poikiloderma with traumatic bulla formation and progressive cutaneous atrophy
    • Kindler T. Congenital poikiloderma with traumatic bulla formation and progressive cutaneous atrophy. Br J Dermatol. 1954;66(3):104-111.
    • (1954) Br J Dermatol , vol.66 , Issue.3 , pp. 104-111
    • Kindler, T.1
  • 20
    • 58149154658 scopus 로고    scopus 로고
    • Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction
    • Ussar S, Moser M, Widmaier M, et al. Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction. PLoS Genet. 2008;4(12):e1000289.
    • (2008) PLoS Genet , vol.4 , Issue.12
    • Ussar, S.1    Moser, M.2    Widmaier, M.3
  • 21
    • 41949127144 scopus 로고    scopus 로고
    • Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function
    • DOI 10.1161/CIRCRESAHA.107.161489
    • Dowling JJ, Gibbs E, Russell M, et al. Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function. Circ Res. 2008;102(4):423-431. (Pubitemid 351651103)
    • (2008) Circulation Research , vol.102 , Issue.4 , pp. 423-431
    • Dowling, J.J.1    Gibbs, E.2    Russell, M.3    Goldman, D.4    Minarcik, J.5    Golden, J.A.6    Feldman, E.L.7
  • 22
    • 48249112975 scopus 로고    scopus 로고
    • Kindlin-2 is required for myocyte elongation and is essential for myogenesis
    • Dowling JJ, Vreede AP, Kim S, Golden J, Feldman EL. Kindlin-2 is required for myocyte elongation and is essential for myogenesis. BMC Cell Biol. 2008;9:36.
    • (2008) BMC Cell Biol , vol.9 , pp. 36
    • Dowling, J.J.1    Vreede, A.P.2    Kim, S.3    Golden, J.4    Feldman, E.L.5
  • 23
    • 39049192701 scopus 로고    scopus 로고
    • Methods for isolation of endothelial and smooth muscle cells and in vitro proliferation assays
    • Mahabeleshwar GH, Somanath PR, Byzova TV. Methods for isolation of endothelial and smooth muscle cells and in vitro proliferation assays. Methods Mol Med. 2006;129:197-208.
    • (2006) Methods Mol Med , vol.129 , pp. 197-208
    • Mahabeleshwar, G.H.1    Somanath, P.R.2    Byzova, T.V.3
  • 26
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells
    • Moser M, Bauer M, Schmid S, et al. Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells. Nat Med. 2009;15(3):300-305.
    • (2009) Nat Med , vol.15 , Issue.3 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3
  • 28
    • 70349254038 scopus 로고    scopus 로고
    • A key role for the integrin alpha2beta1 in experimental and developmental angiogenesis
    • San Antonio JD, Zoeller JJ, Habursky K, et al. A key role for the integrin alpha2beta1 in experimental and developmental angiogenesis. Am J Pathol. 2009;175(3):1338-1347.
    • (2009) Am J Pathol , vol.175 , Issue.3 , pp. 1338-1347
    • San Antonio, J.D.1    Zoeller, J.J.2    Habursky, K.3
  • 29
    • 0029929716 scopus 로고    scopus 로고
    • The vascular endothelial growth factor receptor Flt-1 mediates biological activities. Implications for a functional role of placenta growth factor in monocyte activation and chemotaxis
    • DOI 10.1074/jbc.271.30.17629
    • Clauss M, Weich H, Breier G, et al. The vascular endothelial growth factor receptor Flt-1 mediates biological activities. Implications for a functional role of placenta growth factor in monocyte activation and chemotaxis. J Biol Chem. 1996;271(30):17629-17634. (Pubitemid 26250731)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 17629-17634
    • Clauss, M.1    Weich, H.2    Breier, G.3    Knies, U.4    Rockl, W.5    Waltenberger, J.6    Risaut, W.7
  • 31
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger DS, Bouaouina M, Calderwood DA. Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J Biol Chem. 2009;284(17):11485-11497.
    • (2009) J Biol Chem , vol.284 , Issue.17 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 33
    • 0030038229 scopus 로고    scopus 로고
    • Suppression of p53 activity and p21(WAF1/CIP1) expression by vascular cell integrin αvβ3 during angiogenesis
    • Stromblad S, Becker JC, Yebra M, Brooks PC, Cheresh DA. Suppression of p53 activity and p21WAFI/CIPI expression by vascular cell integrin alphaVbeta3 during angiogenesis. J Clin Invest. 1996;98(2):426-433. (Pubitemid 26255742)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.2 , pp. 426-433
    • Stromblad, S.1    Becker, J.C.2    Yebra, M.3    Brooks, P.C.4    Cheresh, D.A.5
  • 34
    • 0027513593 scopus 로고
    • Integrin β1- and β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms
    • Leavesley DI, Schwartz MA, Rosenfeld M, Cheresh DA. Integrin beta1- and beta3-mediated endothelial cell migration is triggered through distinct signaling mechanisms. J Cell Biol. 1993;121(1):163-170. (Pubitemid 23097372)
    • (1993) Journal of Cell Biology , vol.121 , Issue.1 , pp. 163-170
    • Leavesley, D.I.1    Schwartz, M.A.2    Rosenfeld, M.3    Cheresh, D.A.4
  • 35
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alphavbeta3 for angiogenesis
    • Brooks PC, Clark RA, Cheresh DA. Requirement of vascular integrin alphavbeta3 for angiogenesis. Science. 1994;264(5158):569-571.
    • (1994) Science , vol.264 , Issue.5158 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 40
    • 33644839612 scopus 로고    scopus 로고
    • Signaling mechanisms regulating endothelial permeability
    • Mehta D, Malik AB. Signaling mechanisms regulating endothelial permeability. Physiol Rev. 2006;86(1):279-367.
    • (2006) Physiol Rev , vol.86 , Issue.1 , pp. 279-367
    • Mehta, D.1    Malik, A.B.2
  • 41
    • 29244442618 scopus 로고    scopus 로고
    • Endothelial focal adhesions and barrier function
    • DOI 10.1113/jphysiol.2005.096537
    • Wu MH. Endothelial focal adhesions and barrier function. J Physiol. 2005;569(Pt 2):359-366. (Pubitemid 41830107)
    • (2005) Journal of Physiology , vol.569 , Issue.2 , pp. 359-366
    • Wu, M.H.1
  • 42
    • 33645282289 scopus 로고    scopus 로고
    • Focal adhesions: Paradigm for a signaling nexus
    • Romer LH, Birukov KG, Garcia JG. Focal adhesions: paradigm for a signaling nexus. Circ Res. 2006;98(5):606-616.
    • (2006) Circ Res , vol.98 , Issue.5 , pp. 606-616
    • Romer, L.H.1    Birukov, K.G.2    Garcia, J.G.3
  • 43
    • 0035338471 scopus 로고    scopus 로고
    • Integrin binding to fibronectin and vitronectin maintains the barrier function of isolated porcine coronary venules
    • DOI 10.1111/j.1469-7793.2001.0785e.x
    • Wu MH, Ustinova E, Granger HJ. Integrin binding to fibronectin and vitronectin maintains the barrier function of isolated porcine coronary venules. J Physiol. 2001;532(Pt 3):785-791. (Pubitemid 32427891)
    • (2001) Journal of Physiology , vol.532 , Issue.3 , pp. 785-791
    • Wu, M.H.1    Ustinova, E.2    Granger, H.J.3
  • 44
    • 67649379003 scopus 로고    scopus 로고
    • Impaired integrin-mediated adhesion contributes to reduced barrier properties in VASP-deficient microvascular endothelium
    • Schlegel N, Waschke J. Impaired integrin-mediated adhesion contributes to reduced barrier properties in VASP-deficient microvascular endothelium. J Cell Physiol. 2009;220(2):357-366.
    • (2009) J Cell Physiol , vol.220 , Issue.2 , pp. 357-366
    • Schlegel, N.1    Waschke, J.2
  • 45
    • 0026013429 scopus 로고
    • The role of integrins in the maintenance of endothelial monolayer integrity
    • Lampugnani MG, Resnati M, Dejana E, Marchisio PC. The role of integrins in the maintenance of endothelial monolayer integrity. J Cell Biol. 1991;112(3):479-490. (Pubitemid 21926002)
    • (1991) Journal of Cell Biology , vol.112 , Issue.3 , pp. 479-490
    • Lampugnani, M.G.1    Resnati, M.2    Dejana, E.3    Marchisio, P.C.4
  • 46
    • 68149124272 scopus 로고    scopus 로고
    • JAM-C induces endothelial cell permeability through its association and regulation of beta3 integrins
    • Li X, Stankovic M, Lee BP, et al. JAM-C induces endothelial cell permeability through its association and regulation of beta3 integrins. Arterioscler Thromb Vasc Biol. 2009;29(8):1200-1206.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , Issue.8 , pp. 1200-1206
    • Li, X.1    Stankovic, M.2    Lee, B.P.3
  • 47
    • 3342896372 scopus 로고    scopus 로고
    • Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion
    • DOI 10.1083/jcb.200312013
    • Yano H, Mazaki Y, Kurokawa K, Hanks SK, Matsuda M, Sabe H. Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion. J Cell Biol. 2004;166(2):283-295. (Pubitemid 38988780)
    • (2004) Journal of Cell Biology , vol.166 , Issue.2 , pp. 283-295
    • Yano, H.1    Mazaki, Y.2    Kurokawa, K.3    Hanks, S.K.4    Matsuda, M.5    Sabe, H.6
  • 48
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: Subcellular localization and expression during murine development
    • DOI 10.1016/j.yexcr.2006.06.030, PII S0014482706002266
    • Ussar S, Wang HV, Linder S, Fassler R, Moser M. The Kindlins: subcellular localization and expression during murine development. Exp Cell Res. 2006;312(16):3142-3151. (Pubitemid 44292664)
    • (2006) Experimental Cell Research , vol.312 , Issue.16 , pp. 3142-3151
    • Ussar, S.1    Wang, H.-V.2    Linder, S.3    Fassler, R.4    Moser, M.5
  • 49
    • 49549083034 scopus 로고    scopus 로고
    • Colocalization of kindlin-1, kindlin-2, and migfilin at keratinocyte focal adhesion and relevance to the pathophysiology of Kindler syndrome
    • Lai-Cheong JE, Ussar S, Arita K, Hart IR, McGrath JA. Colocalization of kindlin-1, kindlin-2, and migfilin at keratinocyte focal adhesion and relevance to the pathophysiology of Kindler syndrome. J Invest Dermatol. 2008;128(9):2156-2165.
    • (2008) J Invest Dermatol , vol.128 , Issue.9 , pp. 2156-2165
    • Lai-Cheong, J.E.1    Ussar, S.2    Arita, K.3    Hart, I.R.4    McGrath, J.A.5
  • 50
    • 41349088227 scopus 로고    scopus 로고
    • Role of pericytes in angiogenesis
    • Teicher BA, Ellis LM, eds. 2nd ed. Humana Press; Totowa, NJ
    • Lu C, Sood AK. Role of pericytes in angiogenesis. In: Teicher BA, Ellis LM, eds. Antiangiogenic Agents in Cancer Therapy. 2nd ed. Humana Press; Totowa, NJ; 2008:117-132.
    • (2008) Antiangiogenic Agents in Cancer Therapy , pp. 117-132
    • Lu, C.1    Sood, A.K.2
  • 51
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • DOI 10.1038/nm1722, PII NM1722
    • Moser M, Nieswandt B, Ussar S, Pozgajova M, Fassler R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med. 2008;14(3):325-330. (Pubitemid 351347914)
    • (2008) Nature Medicine , vol.14 , Issue.3 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5


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