메뉴 건너뛰기




Volumn 10, Issue 2, 2012, Pages 289-297

A mutation in the β 3 cytoplasmic tail causes variant Glanzmann thrombasthenia by abrogating transition of α IIbβ 3 to an active state

Author keywords

IIb; 3; Glanzmann thrombasthenia; Integrins; Variant Glanzmann thrombasthenia

Indexed keywords

ALPHA2B BETA3 INTEGRIN; BETA3 INTEGRIN; CYSTEINE; FIBRINOGEN; INTEGRIN; SERINE; UNCLASSIFIED DRUG;

EID: 84856558611     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2011.04577.x     Document Type: Article
Times cited : (5)

References (39)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002; 110: 673-87.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
  • 3
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: dynamic scaffolds for adhesion and signaling in platelets
    • Shattil SJ, Newman PJ. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood 2004; 104: 1606-15.
    • (2004) Blood , vol.104 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 5
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes PE, O'Toole TE, Ylanne J, Shattil SJ, Ginsberg MH. The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J Biol Chem 1995; 270: 12411-17.
    • (1995) J Biol Chem , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 6
    • 3042609771 scopus 로고    scopus 로고
    • Talin controls integrin activation
    • Calderwood DA. Talin controls integrin activation. Biochem Soc Trans 2004; 32: 434-7.
    • (2004) Biochem Soc Trans , vol.32 , pp. 434-437
    • Calderwood, D.A.1
  • 10
    • 0026331047 scopus 로고
    • Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb
    • O'Toole TE, Mandelman D, Forsyth J, Shattil SJ, Plow EF, Ginsberg MH. Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb. Science 1991; 254: 845-7.
    • (1991) Science , vol.254 , pp. 845-847
    • O'Toole, T.E.1    Mandelman, D.2    Forsyth, J.3    Shattil, S.J.4    Plow, E.F.5    Ginsberg, M.H.6
  • 11
    • 0027263655 scopus 로고
    • Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesions
    • Ylanne J, Chen Y, O'Toole TE, Loftus JC, Takada Y, Ginsberg MH. Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J Cell Biol 1993; 122: 223-33.
    • (1993) J Cell Biol , vol.122 , pp. 223-233
    • Ylanne, J.1    Chen, Y.2    O'Toole, T.E.3    Loftus, J.C.4    Takada, Y.5    Ginsberg, M.H.6
  • 12
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo BH, Springer TA, Takagi J. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol 2004; 2: 776-86.
    • (2004) PLoS Biol , vol.2 , pp. 776-786
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 13
    • 0031181648 scopus 로고    scopus 로고
    • The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1
    • Lu CF, Springer TA. The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1. J Immunol 1997; 159: 268-78.
    • (1997) J Immunol , vol.159 , pp. 268-278
    • Lu, C.F.1    Springer, T.A.2
  • 14
    • 0035805633 scopus 로고    scopus 로고
    • Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state
    • Lu C, Takagi J, Springer TA. Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state. J Biol Chem 2001; 276: 14642-8.
    • (2001) J Biol Chem , vol.276 , pp. 14642-14648
    • Lu, C.1    Takagi, J.2    Springer, T.A.3
  • 15
    • 33744764617 scopus 로고    scopus 로고
    • Regulation of integrin alphaIIbbeta3 activation by distinct regions of its cytoplasmic tails
    • Ma YQ, Yang J, Pesho MM, Vinogradova O, Qin J, Plow EF. Regulation of integrin alphaIIbbeta3 activation by distinct regions of its cytoplasmic tails. Biochemistry 2006; 45: 6656-62.
    • (2006) Biochemistry , vol.45 , pp. 6656-6662
    • Ma, Y.Q.1    Yang, J.2    Pesho, M.M.3    Vinogradova, O.4    Qin, J.5    Plow, E.F.6
  • 16
    • 0042672885 scopus 로고    scopus 로고
    • Critical roles for the COOH-terminal NITY and RGT sequences of the integrin beta3 cytoplasmic domain in inside-out and outside-in signaling
    • Xi X, Bodnar RJ, Li Z, Lam SC, Du X. Critical roles for the COOH-terminal NITY and RGT sequences of the integrin beta3 cytoplasmic domain in inside-out and outside-in signaling. J Cell Biol 2003; 162: 329-39.
    • (2003) J Cell Biol , vol.162 , pp. 329-339
    • Xi, X.1    Bodnar, R.J.2    Li, Z.3    Lam, S.C.4    Du, X.5
  • 17
    • 65149095905 scopus 로고    scopus 로고
    • Antithrombotic effects of targeting alphaIIbbeta3 signaling in platelets
    • Ablooglu AJ, Kang J, Petrich BG, Ginsberg MH, Shattil SJ. Antithrombotic effects of targeting alphaIIbbeta3 signaling in platelets. Blood 2009; 113: 3585-92.
    • (2009) Blood , vol.113 , pp. 3585-3592
    • Ablooglu, A.J.1    Kang, J.2    Petrich, B.G.3    Ginsberg, M.H.4    Shattil, S.J.5
  • 18
    • 0025821346 scopus 로고
    • Detection of the Glanzmann's thrombasthenia mutations in Arab and Iraqi-Jewish patients by polymerase chain reaction and restriction analysis of blood or urine samples
    • Peretz H, Seligsohn U, Zwang E, Coller BS, Newman PJ. Detection of the Glanzmann's thrombasthenia mutations in Arab and Iraqi-Jewish patients by polymerase chain reaction and restriction analysis of blood or urine samples. Thromb Haemost 1991; 66: 500-4.
    • (1991) Thromb Haemost , vol.66 , pp. 500-504
    • Peretz, H.1    Seligsohn, U.2    Zwang, E.3    Coller, B.S.4    Newman, P.J.5
  • 20
    • 0037777629 scopus 로고    scopus 로고
    • Major mutations in calf-1 and calf-2 domains of glycoprotein IIb in patients with Glanzmann thrombasthenia enable GPIIb/IIIa complex formation, but impair its transport from the endoplasmic reticulum to the Golgi apparatus
    • Rosenberg N, Yatuv R, Sobolev V, Peretz H, Zivelin A, Seligsohn U. Major mutations in calf-1 and calf-2 domains of glycoprotein IIb in patients with Glanzmann thrombasthenia enable GPIIb/IIIa complex formation, but impair its transport from the endoplasmic reticulum to the Golgi apparatus. Blood 2003; 101: 4808-15.
    • (2003) Blood , vol.101 , pp. 4808-4815
    • Rosenberg, N.1    Yatuv, R.2    Sobolev, V.3    Peretz, H.4    Zivelin, A.5    Seligsohn, U.6
  • 21
    • 34247896877 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia
    • Nurden AT. Glanzmann thrombasthenia. Orphanet J Rare Dis 2006; 1: 10-7.
    • (2006) Orphanet J Rare Dis , vol.1 , pp. 10-17
    • Nurden, A.T.1
  • 22
    • 0032402117 scopus 로고    scopus 로고
    • R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic domain of the integrin IIb subunit in a patient with a Glanzmann's thrombasthenia-like syndrome
    • Peyruchaud O, Nurden AT, Milet S, Macchi L, Pannochia A, Bray PF, Kieffer N, Bourre F. R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic domain of the integrin IIb subunit in a patient with a Glanzmann's thrombasthenia-like syndrome. Blood 1998; 92: 4178-87.
    • (1998) Blood , vol.92 , pp. 4178-4187
    • Peyruchaud, O.1    Nurden, A.T.2    Milet, S.3    Macchi, L.4    Pannochia, A.5    Bray, P.F.6    Kieffer, N.7    Bourre, F.8
  • 23
    • 77954507827 scopus 로고    scopus 로고
    • L718P mutation in the membrane-proximal cytoplasmic tail of beta 3 promotes abnormal alpha IIb beta 3 clustering and lipid microdomain coalescence, and associates with a thrombasthenia-like phenotype
    • Jayo A, Conde I, Lastres P, Martinez C, Rivera J, Vicente V, Gonzalez-Manchon C. L718P mutation in the membrane-proximal cytoplasmic tail of beta 3 promotes abnormal alpha IIb beta 3 clustering and lipid microdomain coalescence, and associates with a thrombasthenia-like phenotype. Haematologica 2010; 95: 1158-66.
    • (2010) Haematologica , vol.95 , pp. 1158-1166
    • Jayo, A.1    Conde, I.2    Lastres, P.3    Martinez, C.4    Rivera, J.5    Vicente, V.6    Gonzalez-Manchon, C.7
  • 25
    • 0030664425 scopus 로고    scopus 로고
    • Truncation of the cytoplasmic domain of beta3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin alpha(IIb)beta3 complex
    • Wang R, Shattil SJ, Ambruso DR, Newman PJ. Truncation of the cytoplasmic domain of beta3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin alpha(IIb)beta3 complex. J Clin Invest 1997; 100: 2393-403.
    • (1997) J Clin Invest , vol.100 , pp. 2393-2403
    • Wang, R.1    Shattil, S.J.2    Ambruso, D.R.3    Newman, P.J.4
  • 26
    • 0026614923 scopus 로고
    • Ser-752-->Pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia
    • Chen YP, Djaffar I, Pidard D, Steiner B, Cieutat AM, Caen JP, Rosa JP. Ser-752-->Pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia. Proc Natl Acad Sci USA 1992; 89: 10169-73.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10169-10173
    • Chen, Y.P.1    Djaffar, I.2    Pidard, D.3    Steiner, B.4    Cieutat, A.M.5    Caen, J.P.6    Rosa, J.P.7
  • 28
    • 77952931584 scopus 로고    scopus 로고
    • Effects of limiting extension at the alphaIIb genu on ligand binding to integrin alphaIIbbeta3
    • Blue R, Li J, Steinberger J, Murcia M, Filizola M, Coller BS. Effects of limiting extension at the alphaIIb genu on ligand binding to integrin alphaIIbbeta3. J Biol Chem 2010; 285: 17604-13.
    • (2010) J Biol Chem , vol.285 , pp. 17604-17613
    • Blue, R.1    Li, J.2    Steinberger, J.3    Murcia, M.4    Filizola, M.5    Coller, B.S.6
  • 29
    • 0026063230 scopus 로고
    • Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger AL 3rd, Du XP, Plow EF, Ginsberg MH. Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J Biol Chem 1991; 266: 17106-11.
    • (1991) J Biol Chem , vol.266 , pp. 17106-17111
    • Frelinger 3rd, A.L.1    Du, X.P.2    Plow, E.F.3    Ginsberg, M.H.4
  • 30
    • 0029039630 scopus 로고
    • Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin beta 3 subunit
    • Honda S, Tomiyama Y, Pelletier AJ, Annis D, Honda Y, Orchekowski R, Ruggeri Z, Kunicki TJ. Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin beta 3 subunit. J Biol Chem 1995; 270: 11947-54.
    • (1995) J Biol Chem , vol.270 , pp. 11947-11954
    • Honda, S.1    Tomiyama, Y.2    Pelletier, A.J.3    Annis, D.4    Honda, Y.5    Orchekowski, R.6    Ruggeri, Z.7    Kunicki, T.J.8
  • 31
    • 1642504824 scopus 로고    scopus 로고
    • Critical cysteine residues for regulation of integrin alphaIIbbeta3 are clustered in the epidermal growth factor domains of the beta3 subunit
    • Kamata T, Ambo H, Puzon-McLaughlin W, Tieu KK, Handa M, Ikeda Y, Takada Y. Critical cysteine residues for regulation of integrin alphaIIbbeta3 are clustered in the epidermal growth factor domains of the beta3 subunit. Biochem J 2004; 378: 1079-82.
    • (2004) Biochem J , vol.378 , pp. 1079-1082
    • Kamata, T.1    Ambo, H.2    Puzon-McLaughlin, W.3    Tieu, K.K.4    Handa, M.5    Ikeda, Y.6    Takada, Y.7
  • 32
    • 50349098094 scopus 로고    scopus 로고
    • Specific cysteines in beta3 are involved in disulfide bond exchange-dependent and -independent activation of alphaIIbbeta3
    • Mor-Cohen R, Rosenberg N, Landau M, Lahav J, Seligsohn U. Specific cysteines in beta3 are involved in disulfide bond exchange-dependent and -independent activation of alphaIIbbeta3. J Biol Chem 2008; 283: 19235-44.
    • (2008) J Biol Chem , vol.283 , pp. 19235-19244
    • Mor-Cohen, R.1    Rosenberg, N.2    Landau, M.3    Lahav, J.4    Seligsohn, U.5
  • 33
    • 23844457919 scopus 로고    scopus 로고
    • Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain
    • Arias-Salgado EG, Lizano S, Shattil SJ, Ginsberg MH. Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain. J Biol Chem 2005; 280: 29699-707.
    • (2005) J Biol Chem , vol.280 , pp. 29699-29707
    • Arias-Salgado, E.G.1    Lizano, S.2    Shattil, S.J.3    Ginsberg, M.H.4
  • 34
    • 41949106260 scopus 로고    scopus 로고
    • Cooperative role of the membrane-proximal and -distal residues of the integrin beta3 cytoplasmic domain in regulation of talin-mediated alpha IIb beta3 activation
    • Hato T, Yamanouchi J, Tamura T, Yakushijin Y, Sakai I, Yasukawa M. Cooperative role of the membrane-proximal and -distal residues of the integrin beta3 cytoplasmic domain in regulation of talin-mediated alpha IIb beta3 activation. J Biol Chem 2008; 283: 5662-8.
    • (2008) J Biol Chem , vol.283 , pp. 5662-5668
    • Hato, T.1    Yamanouchi, J.2    Tamura, T.3    Yakushijin, Y.4    Sakai, I.5    Yasukawa, M.6
  • 35
    • 77954507827 scopus 로고    scopus 로고
    • L718P mutation in the membrane-proximal cytoplasmic tail of beta 3 promotes abnormal alpha IIb beta 3 clustering and lipid microdomain coalescence, and associates with a thrombasthenia-like phenotype
    • Jayo A, Conde I, Lastres P, Martinez C, Rivera J, Vicente V, Gonzalez-Manchon C. L718P mutation in the membrane-proximal cytoplasmic tail of beta 3 promotes abnormal alpha IIb beta 3 clustering and lipid microdomain coalescence, and associates with a thrombasthenia-like phenotype. Haematologica 2010; 95: 1158-66.
    • (2010) Haematologica , vol.95 , pp. 1158-1166
    • Jayo, A.1    Conde, I.2    Lastres, P.3    Martinez, C.4    Rivera, J.5    Vicente, V.6    Gonzalez-Manchon, C.7
  • 36
    • 34147140579 scopus 로고    scopus 로고
    • Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets
    • Zou Z, Chen H, Schmaier AA, Hynes RO, Kahn ML. Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets. Blood 2007; 109: 3284-90.
    • (2007) Blood , vol.109 , pp. 3284-3290
    • Zou, Z.1    Chen, H.2    Schmaier, A.A.3    Hynes, R.O.4    Kahn, M.L.5
  • 37
    • 0035068162 scopus 로고    scopus 로고
    • Evidence from site-directed mutagenesis that the cytoplasmic domain of the beta3 subunit influences the conformational state of the alphaVbeta3 integrin ectodomain
    • Schaffner-Reckinger E, Brons NH, Kieffer N. Evidence from site-directed mutagenesis that the cytoplasmic domain of the beta3 subunit influences the conformational state of the alphaVbeta3 integrin ectodomain. Thromb Haemost 2001; 85: 716-23.
    • (2001) Thromb Haemost , vol.85 , pp. 716-723
    • Schaffner-Reckinger, E.1    Brons, N.H.2    Kieffer, N.3
  • 39
    • 0028146157 scopus 로고
    • A point mutation in the integrin beta 3 cytoplasmic domain (S752-->P) impairs bidirectional signaling through alphaIIbbeta3 (platelet glycoprotein IIb-IIIa)
    • Chen YP, O'Toole TE Ylanne J, Rosa JP, Ginsberg MH. A point mutation in the integrin beta 3 cytoplasmic domain (S752-->P) impairs bidirectional signaling through alphaIIbbeta3 (platelet glycoprotein IIb-IIIa). Blood 1994; 84: 1857-65.
    • (1994) Blood , vol.84 , pp. 1857-1865
    • Chen, Y.P.1    O'Toole, T.E.2    Ylanne, J.3    Rosa, J.P.4    Ginsberg, M.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.