Identification of an atypical lipoprotein‐binding protein from human aortic smooth muscle as T‐cadherin

FEBS Letters

Molokoedov, Alexander S¹  Tkachuk, Vsevolod A³  Stambolsky, Dmitry V³  Sidorova, Maria V¹  Philippova, Maria P³  Spirov, Valentin G⁴  Kuzmenko, Elena S²  Bochkov, Valery N³  Resink, Therese J² 

[1] Laboratory of Peptide Synthesis, Institute of Experimental Cardiology, Cardiology Research Center, 121552 Moscow, Russia;Laboratory of Hypertension, Department of Research, Basel University Hospitals, 4031 Basel, Switzerland;Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, 121552 Moscow, Russia;Laboratory of Protein Engineering, Institute of Experimental Cardiology, Cardiology Research Center, 121552 Moscow, Russia

关键词: Lipoprotein;    Cadherin;    Vascular smooth muscle cell;    VSMC;    vascular smooth muscle cell;    LDL;    low density lipoprotein;    mAb;    monoclonal antibody;    IEF;    isoelectric focusing;    2-D;    two-dimensional;    GPI;    glycosylphosphatidylinositol;   

DOI  :  10.1016/S0014-5793(97)01562-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have previously described an atypical lipoprotein-binding protein of about 105 kDa (p105) in membranes of vascular smooth muscle cells (VSMCs) that is distinct from currently known lipoprotein receptors. In the present work we have developed a procedure for purification of p105 from human aortic media. Partial sequencing of purified protein has revealed identity of p105 with human T-cadherin. Anti-peptide antisera raised against human T-cadherin recognized a protein spot corresponding to the purified p105 on two-dimensional Western blots. The antisera also inhibited LDL binding to p105 on ligand blots. We conclude that the 105 kDa lipoprotein-binding protein present in human VSMCs is T-cadherin, an unusual glycosylphosphatidylinositol-anchored member of the cadherin family of cell-cell adhesion proteins.

【 授权许可】

Unknown