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LDL binds to surface‐expressed human T‐cadherin in transfected HEK293 cells and influences homophilic adhesive interactions
Author(s) -
Resink Thérèse J.,
Kuzmenko Yelena S.,
Kern Frances,
Stambolsky Dmitry,
Bochkov Valery N.,
Tkachuk Vsevolod A.,
Erne Paul,
Niermann Thomas
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01594-x
Subject(s) - cadherin , transfection , phospholipase c , microbiology and biotechnology , cell adhesion , intracellular , cleavage (geology) , hek 293 cells , cell adhesion molecule , chemistry , biology , biochemistry , cell , receptor , signal transduction , gene , paleontology , fracture (geology)
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 Ca 2+ ‐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 [ 125 I]‐LDL that was sensitive to PI‐PLC pre‐treatment of cells. Ca 2+ ‐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.