LDL binds to surface‐expressed human T‐cadherin in transfected HEK293 cells and influences homophilic adhesive interactions

FEBS Letters

Kern, Frances³  Tkachuk, Vsevolod A.²  Stambolsky, Dmitry³  Kuzmenko, Yelena S.³  Bochkov, Valery N.²  Erne, Paul¹  Niermann, Thomas³  Resink, Thérèse J.³ 

[1] Division of Cardiology, Kantonsspital Luzerne, Luzerne, Switzerland;Laboratory for Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, 121552 Moscow, Russia;Laboratory for Cardiovascular Research, Department of Research, Basel University Hospital, CH 4031 Basel, Switzerland

关键词: T-cadherin;    Low density lipoprotein;    Binding;    Intercellular adhesion;    Transfection;    HEK293 cell;    SMC;    smooth muscle cell;    LDL;    low density lipoprotein;    HDL;    high density lipoprotein;    GPI;    glycosylphosphatidylinositol;    PI-PLC;    phosphatidylinositol-specific phospholipase C;    T-cad+;    HEK293 cells stably transfected with human pre-pro T-cad;    wt;    parental HEK293 cells;    mock;    mock-transfected HEK293 cells;   

DOI  :  10.1016/S0014-5793(99)01594-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

T-cadherin (T-cad) is an unusual glycosylphosphatidylinositol-anchored member of the cadherin family of cell adhesion molecules. Binding of low density lipoproteins (LDLs) to T-cad can be demonstrated on Western blots of smooth muscle cell lysates, membranes and purified proteins. Using HEK293 cells transfected with human T-cad cDNA (T-cad+), we have investigated the adhesion properties of expressed mature and precursor proteins and examined the postulate that LDL represents a physiologically relevant ligand for T-cad. T-cad+ exhibits an increased Ca²⁺-dependent aggregation (vs. control) that was reduced by selective proteolytic cleavage of precursor T-cad and abolished after either proteolytic or phosphatidylinositol-specific phospholipase C (PI-PLC) cleavage of both mature and precursor proteins, indicating that both proteins function in intercellular adhesion. T-cad+ exhibited a significantly increased specific cell surface-binding of [¹²⁵I]-LDL that was sensitive to PI-PLC pre-treatment of cells. Ca²⁺-dependent intercellular adhesion of T-cad+ was significantly inhibited by LDL. Our results support the suggestion that LDL is a physiologically relevant ligand for T-cad.

【 授权许可】

Unknown