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

• Published in: FEBS letters 1998-01, Vol.421 (3), p.208-212
• Main Authors: Tkachuk, Vsevolod A, Bochkov, Valery N, Philippova, Maria P, Stambolsky, Dmitry V, Kuzmenko, Elena S, Sidorova, Maria V, Molokoedov, Alexander S, Spirov, Valentin G, Resink, Therese J
• Format: Article
• Language: English
• Subjects: 2-D, two-dimensional; Amino Acid Sequence; Animals; Aorta - chemistry; Cadherin; Cadherins - chemistry; Cadherins - isolation & purification; Cadherins - metabolism; GPI, glycosylphosphatidylinositol; Humans; IEF, isoelectric focusing; LDL, low density lipoprotein; Lipoprotein; Lipoproteins, LDL - metabolism; mAb, monoclonal antibody; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Muscle, Smooth, Vascular - chemistry; Phosphatidylinositol Diacylglycerol-Lyase; Protein Binding; Rabbits; Trypsin - metabolism; Tumor Cells, Cultured; Type C Phospholipases - metabolism; Vascular smooth muscle cell; VSMC, vascular smooth muscle cell
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)01562-7

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.