메뉴 건너뛰기




Volumn 355, Issue 4, 2007, Pages 1058-1063

Critical residues of αX I-domain recognizing fibrinogen central domain

Author keywords

X 2; 2 Integrin; Binding; Fibrinogen; Fragment E; I domain

Indexed keywords

FIBRINOGEN; INTEGRIN; LIGAND;

EID: 33847630759     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.02.082     Document Type: Article
Times cited : (10)

References (30)
  • 3
    • 0034122721 scopus 로고    scopus 로고
    • CR3: a general purpose adhesion-recognition receptor essential for innate immunity
    • Ehlers M.R.W. CR3: a general purpose adhesion-recognition receptor essential for innate immunity. Microb. Infec. 2 (2000) 289-294
    • (2000) Microb. Infec. , vol.2 , pp. 289-294
    • Ehlers, M.R.W.1
  • 4
    • 0028265846 scopus 로고
    • The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous β subunit and localization of a ligand recognition site to the I-domain
    • Bilsland C.A., Diamond M.S., and Springer T.A. The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous β subunit and localization of a ligand recognition site to the I-domain. J. Immunol. 152 (1994) 4582-4589
    • (1994) J. Immunol. , vol.152 , pp. 4582-4589
    • Bilsland, C.A.1    Diamond, M.S.2    Springer, T.A.3
  • 5
    • 0033517847 scopus 로고    scopus 로고
    • Characteristics of fibrinogen binding to the domain of CD11c, an α subunit of p150,95
    • Nham S.-U. Characteristics of fibrinogen binding to the domain of CD11c, an α subunit of p150,95. Biochem. Biophys. Res. Commun. 264 (1999) 630-634
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 630-634
    • Nham, S.-U.1
  • 6
    • 18044377595 scopus 로고    scopus 로고
    • Characterization of αX I-domain binding to Thy-1
    • Choi J., Leyton L., and Nham S.-U. Characterization of αX I-domain binding to Thy-1. Biochem. Biophy. Res. Comm. 331 (2005) 557-561
    • (2005) Biochem. Biophy. Res. Comm. , vol.331 , pp. 557-561
    • Choi, J.1    Leyton, L.2    Nham, S.-U.3
  • 7
    • 0027530684 scopus 로고
    • The I-domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond M.S., Garcia-Aguilar J., Bickford J.K., Corbi A.L., and Springer T.A. The I-domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol. 120 (1993) 1031-1043
    • (1993) J. Cell Biol. , vol.120 , pp. 1031-1043
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 8
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the α Subunit of Integrin CR3 (CD11b/CD18)
    • Lee J.O., Rieu P., Arnaout M.A., and Liddington R.C. Crystal structure of the A domain from the α Subunit of Integrin CR3 (CD11b/CD18). Cell 80 (1995) 631-638
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.C.4
  • 11
    • 0028803769 scopus 로고
    • Distinct ligand binding sites in the I-domain of integrin αMβ2 that differentially affect a divalent cation-dependent conformation
    • McGuire S.L., and Bajt M.L. Distinct ligand binding sites in the I-domain of integrin αMβ2 that differentially affect a divalent cation-dependent conformation. J. Biol. Chem. 270 (1995) 25866-25871
    • (1995) J. Biol. Chem. , vol.270 , pp. 25866-25871
    • McGuire, S.L.1    Bajt, M.L.2
  • 12
    • 0033594871 scopus 로고    scopus 로고
    • Amino acid sequences within the alpha subunit of integrin αMβ2 (Mac-1) critical for specific recognition of C3bi
    • Zhang L., and Plow E.F. Amino acid sequences within the alpha subunit of integrin αMβ2 (Mac-1) critical for specific recognition of C3bi. Biochemistry 38 (1999) 8064-8071
    • (1999) Biochemistry , vol.38 , pp. 8064-8071
    • Zhang, L.1    Plow, E.F.2
  • 13
    • 0032575509 scopus 로고    scopus 로고
    • Identification of a novel recognition sequence for αMβ2 integrin within the gamma-chain of fibrinogen
    • Ugarova T.P., Solovjov D.A., Zhang L., Loukinov D.I., Yee V.C., Medved L.V., and Plow E.F. Identification of a novel recognition sequence for αMβ2 integrin within the gamma-chain of fibrinogen. J. Biol. Chem. 273 (1998) 22519-22527
    • (1998) J. Biol. Chem. , vol.273 , pp. 22519-22527
    • Ugarova, T.P.1    Solovjov, D.A.2    Zhang, L.3    Loukinov, D.I.4    Yee, V.C.5    Medved, L.V.6    Plow, E.F.7
  • 14
    • 0037073752 scopus 로고    scopus 로고
    • A molecular basis for integrin αMβ2 ligand binding promiscuity
    • Yakubenko V.P., Lishko V.K., Lam S.C.-T., and Ugarova T.P. A molecular basis for integrin αMβ2 ligand binding promiscuity. J. Biol. Chem. 277 (2002) 48635-48642
    • (2002) J. Biol. Chem. , vol.277 , pp. 48635-48642
    • Yakubenko, V.P.1    Lishko, V.K.2    Lam, S.C.-T.3    Ugarova, T.P.4
  • 15
    • 0036086751 scopus 로고    scopus 로고
    • Loops within the CD11c I-domain critical for specific recognition of fibrinogen
    • Choi J., and Nham S.-U. Loops within the CD11c I-domain critical for specific recognition of fibrinogen. Biochem. Biophys. Res. Comm. 292 (2002) 756-760
    • (2002) Biochem. Biophys. Res. Comm. , vol.292 , pp. 756-760
    • Choi, J.1    Nham, S.-U.2
  • 16
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosseson M.W. Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 3 (2005) 1894-1904
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1894-1904
    • Mosseson, M.W.1
  • 17
    • 0020451512 scopus 로고
    • Fibrinogen and its fragment D stimulate proliferation of human hemopoietic cells in vitro
    • Hatzfields J.A., Hatzfields A., and Maigne J. Fibrinogen and its fragment D stimulate proliferation of human hemopoietic cells in vitro. Proc. Natl. Acad. Sci. USA 79 (1982) 6280-6284
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6280-6284
    • Hatzfields, J.A.1    Hatzfields, A.2    Maigne, J.3
  • 18
    • 0026074491 scopus 로고
    • FDP D-Dimer induces the secretion of Interleukin-1, urokinase-type plasminogen activator, and plasminogen activator inhibitor-2 in a human promonocytic leukemia cell line
    • Hamaguchi M., Orishita Y., Takahashi I., Ogura M., Takamatsu J., and Saito H. FDP D-Dimer induces the secretion of Interleukin-1, urokinase-type plasminogen activator, and plasminogen activator inhibitor-2 in a human promonocytic leukemia cell line. Blood 77 (1991) 94-100
    • (1991) Blood , vol.77 , pp. 94-100
    • Hamaguchi, M.1    Orishita, Y.2    Takahashi, I.3    Ogura, M.4    Takamatsu, J.5    Saito, H.6
  • 19
    • 0035745119 scopus 로고    scopus 로고
    • Fibrin fragment E stimulates the proliferation, migration and differentiation of human microvascular endothelial cells in vitro
    • Bootle-Wilbraham C.A., Tazzyman S., Thompson W.D., Stirk C.M., and Lewis C.E. Fibrin fragment E stimulates the proliferation, migration and differentiation of human microvascular endothelial cells in vitro. Angiogenesis 4 (2001) 269-275
    • (2001) Angiogenesis , vol.4 , pp. 269-275
    • Bootle-Wilbraham, C.A.1    Tazzyman, S.2    Thompson, W.D.3    Stirk, C.M.4    Lewis, C.E.5
  • 20
    • 0033611621 scopus 로고    scopus 로고
    • Fragment E derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages
    • Lee M.-E., Lee K.-J., and Nham S.-U. Fragment E derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages. Mol. Cells 28 (1999) 7-13
    • (1999) Mol. Cells , vol.28 , pp. 7-13
    • Lee, M.-E.1    Lee, K.-J.2    Nham, S.-U.3
  • 21
    • 0032514899 scopus 로고    scopus 로고
    • Endothelial cell VE-cadherin functions as a receptor for the β15-42 sequence of fibrin
    • Bach T.L., Barsigian C., Yaen C.H., and Martinez J. Endothelial cell VE-cadherin functions as a receptor for the β15-42 sequence of fibrin. J. Biol. Chem. 273 (1998) 30719-30728
    • (1998) J. Biol. Chem. , vol.273 , pp. 30719-30728
    • Bach, T.L.1    Barsigian, C.2    Yaen, C.H.3    Martinez, J.4
  • 22
    • 0037177243 scopus 로고    scopus 로고
    • 2-terminal portions of the fibrin β chains
    • 2-terminal portions of the fibrin β chains. Biochemistry 41 (2002) 4107-4116
    • (2002) Biochemistry , vol.41 , pp. 4107-4116
    • Gorlatov, S.1    Medved, L.2
  • 23
    • 0027468975 scopus 로고
    • The structural motif glycine 190-valine 202 of the fibrinogen γ chain interacts with CD11b/CD18 integrin αMβ2 (Mac-1) and promotes leukocyte adhesion
    • Altieri D.C., Plescia J., and Plow E.D. The structural motif glycine 190-valine 202 of the fibrinogen γ chain interacts with CD11b/CD18 integrin αMβ2 (Mac-1) and promotes leukocyte adhesion. J. Biol. Chem. 268 (1993) 1847-1853
    • (1993) J. Biol. Chem. , vol.268 , pp. 1847-1853
    • Altieri, D.C.1    Plescia, J.2    Plow, E.D.3
  • 24
    • 0035958074 scopus 로고    scopus 로고
    • Identification of the binding site for fibrinogen recognition peptide (γ383-395 within the αM I-domain of integrin αMβ2
    • Yakubenko V.P., Solovjov D.A., Zhang L., Yee V.C., Plow E.F., and Ugarova T.P. Identification of the binding site for fibrinogen recognition peptide (γ383-395 within the αM I-domain of integrin αMβ2. J. Biol. Chem. 275 (2001) 13995-14003
    • (2001) J. Biol. Chem. , vol.275 , pp. 13995-14003
    • Yakubenko, V.P.1    Solovjov, D.A.2    Zhang, L.3    Yee, V.C.4    Plow, E.F.5    Ugarova, T.P.6
  • 27
    • 0034964396 scopus 로고    scopus 로고
    • Recognition of fibrinogen by leukocyte integrins
    • Ugarova T.P., and Yakubenko V.P. Recognition of fibrinogen by leukocyte integrins. Ann. N. Y. Acad. Aci. 936 (2001) 368-385
    • (2001) Ann. N. Y. Acad. Aci. , vol.936 , pp. 368-385
    • Ugarova, T.P.1    Yakubenko, V.P.2
  • 29
    • 13444294243 scopus 로고    scopus 로고
    • Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin
    • Vorup-Jensen T., Carman C.V., Shimaoka M., Schuck P., Svitel J., and Springer T.A. Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin. Proc. Nat. Acad. Sci. USA 102 (2005) 1614-1619
    • (2005) Proc. Nat. Acad. Sci. USA , vol.102 , pp. 1614-1619
    • Vorup-Jensen, T.1    Carman, C.V.2    Shimaoka, M.3    Schuck, P.4    Svitel, J.5    Springer, T.A.6
  • 30
    • 33744469804 scopus 로고    scopus 로고
    • Fibrin(ogen) and its fragments in the pathophysiology and treatment of myocardial infarction
    • Zacharowski K., Zacharowski P., Reingruber S., and Petzelbauer P. Fibrin(ogen) and its fragments in the pathophysiology and treatment of myocardial infarction. J. Mol. Med. 84 (2006) 469-477
    • (2006) J. Mol. Med. , vol.84 , pp. 469-477
    • Zacharowski, K.1    Zacharowski, P.2    Reingruber, S.3    Petzelbauer, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.