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Volumn 40, Issue 3, 2008, Pages 446-448

Molecular structure of the extracellular region of Lutheran blood group glycoprotein and location of the laminin binding site

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; GLYCOPROTEIN; LAMININ;

EID: 41949140173     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2008.01.004     Document Type: Letter
Times cited : (13)

References (11)
  • 1
    • 0029078165 scopus 로고
    • The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver
    • Parsons S.F., Mallinson G., Holmes C.H., Houlihan J.M., Simpson K.L., Mawby W.J., Spurr N.K., Warne D., Barclay A.N., and Anstee D.J. The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver. PNAS 92 (1995) 5496-5500
    • (1995) PNAS , vol.92 , pp. 5496-5500
    • Parsons, S.F.1    Mallinson, G.2    Holmes, C.H.3    Houlihan, J.M.4    Simpson, K.L.5    Mawby, W.J.6    Spurr, N.K.7    Warne, D.8    Barclay, A.N.9    Anstee, D.J.10
  • 3
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    • The LG1-3 tandem of laminin {alpha}5 harbors the binding sites of Lutheran/basal cell adhesion molecule and {alpha}3beta1/{alpha}6beta1 Integrins
    • Kikkawa Y., Sasaki T., Nguyen M.T., Nomizu M., Mitaka T., and Miner J.H. The LG1-3 tandem of laminin {alpha}5 harbors the binding sites of Lutheran/basal cell adhesion molecule and {alpha}3beta1/{alpha}6beta1 Integrins. J. Biol. Chem. 282 (2007) 14853-14860.
    • (2007) J. Biol. Chem. , vol.282
    • Kikkawa, Y.1    Sasaki, T.2    Nguyen, M.T.3    Nomizu, M.4    Mitaka, T.5    Miner, J.H.6
  • 4
    • 0035161468 scopus 로고    scopus 로고
    • Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind {alpha}5 chain-containing human laminin with high affinity
    • Parsons S.F., Lee G., Spring F.A., Willig T.-N., Peters L.L., Gimm J.A., Tanner M.J.A., Mohandas N., Anstee D.J., and Chasis J.A. Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind {alpha}5 chain-containing human laminin with high affinity. Blood 97 (2001) 312-320
    • (2001) Blood , vol.97 , pp. 312-320
    • Parsons, S.F.1    Lee, G.2    Spring, F.A.3    Willig, T.-N.4    Peters, L.L.5    Gimm, J.A.6    Tanner, M.J.A.7    Mohandas, N.8    Anstee, D.J.9    Chasis, J.A.10
  • 5
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: the laminin family of heterotrimers
    • Colognato H., and Yurchenco P.D. Form and function: the laminin family of heterotrimers. Dev. Dyn. 218 (2000) 213-234
    • (2000) Dev. Dyn. , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 6
    • 0742322846 scopus 로고    scopus 로고
    • B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease
    • Zen Q., Batchvarova M., Twyman C.A., Eyler C.E., Qiu H., De Castro L.M., and Telen M.J. B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. Am. J. Hematol. 75 (2004) 63-72
    • (2004) Am. J. Hematol. , vol.75 , pp. 63-72
    • Zen, Q.1    Batchvarova, M.2    Twyman, C.A.3    Eyler, C.E.4    Qiu, H.5    De Castro, L.M.6    Telen, M.J.7
  • 7
    • 0033534462 scopus 로고    scopus 로고
    • Critical factors in basal cell adhesion molecule/Lutheran-mediated adhesion to laminin
    • Zen Q., Cottman M., Truskey G., Fraser R., and Telen M.J. Critical factors in basal cell adhesion molecule/Lutheran-mediated adhesion to laminin. J. Biol. Chem. 274 (1999) 728-734
    • (1999) J. Biol. Chem. , vol.274 , pp. 728-734
    • Zen, Q.1    Cottman, M.2    Truskey, G.3    Fraser, R.4    Telen, M.J.5
  • 8
    • 0042736851 scopus 로고    scopus 로고
    • Distinct requirements for heparin and [alpha]-dystroglycan binding revealed by structure-based mutagenesis of the Laminin [alpha]2 LG4-LG5 domain pair
    • Wizemann H., Garbe J.H.O., Friedrich M.V.K., Timpl R., Sasaki T., and Hohenester E. Distinct requirements for heparin and [alpha]-dystroglycan binding revealed by structure-based mutagenesis of the Laminin [alpha]2 LG4-LG5 domain pair. J. Mol. Biol. 332 (2003) 635-642
    • (2003) J. Mol. Biol. , vol.332 , pp. 635-642
    • Wizemann, H.1    Garbe, J.H.O.2    Friedrich, M.V.K.3    Timpl, R.4    Sasaki, T.5    Hohenester, E.6
  • 9
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    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 10
    • 0025946698 scopus 로고
    • How thick is the glycocalyx of human erythrocytes?
    • Linss W., Pilgrim C., and Feuerstein H. How thick is the glycocalyx of human erythrocytes?. Acta Histochem. 91 (1991) 101-104
    • (1991) Acta Histochem. , vol.91 , pp. 101-104
    • Linss, W.1    Pilgrim, C.2    Feuerstein, H.3
  • 11
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    • Molecular bases of the antigens of the Lutheran blood group system
    • Crew V.K., Green C., and Daniels G. Molecular bases of the antigens of the Lutheran blood group system. Transfusion 43 (2003) 1729-1737
    • (2003) Transfusion , vol.43 , pp. 1729-1737
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.