Involvement of the YIGSR sequence of laminin in protein tyrosine phosphorylation

FEBS Letters

Littauer, U.Z¹  Bushkin-Harav, I¹ 

[1] Department of Neurobiology, Weizmann Institute of Science, Rehovot 76100, Israel

关键词: Cell adhesion;    Glycosyl phosphatidylinositol anchor;    Laminin;    Neuroblastoma;    67 kDa laminin binding protein;    Signal transduction;    LBP;    laminin binding protein;    GPI;    glycosyl phosphatidylinositol;    NB;    neuroblastoma;    PI-PLC;    phosphatidylinositol-specific phospholipase C;    Sulfo-MBS;    m-maleimidobezoyl-N-hydroxysulfosuccinimide ester;    C(YIGSR)3-NH2;    C(YIGSR)3-NH2 peptide amide;   

DOI  :  10.1016/S0014-5793(98)00180-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have examined the mechanism of signaling by the 67 kDa YIGSR binding protein of laminin and its properties in neuroblastoma cells. Ligand displacement analysis showed that the interaction with the C(YIGSR)₃-NH₂ peptide amide is of intermediate affinity (1.5×10⁻⁷ M). Cross-linking experiments with sulfo-MBS detected an additional protein with a molecular mass of 116 kDa that binds the YIGSR sequence. Incubation of neuroblastoma cells with C(YIGSR)₃-NH₂ peptide amide or antibody directed against the 67 kDa laminin binding protein induces tyrosine phosphorylation of proteins with a molecular mass ranging from 115 to 130 kDa and another heterogeneous protein group of 32 kDa.

【 授权许可】

Unknown