Identification of 130 kDa cell surface LDL-binding protein from smooth muscle cells as a partially processed T-cadherin precursor |
| |
Authors: | DV Stambolsky YS Kuzmenko MP Philippova VN Bochkov ZD Bespalova AA Azmuko NM Kashirina TN Vlasik VA Tkachuk TJ Resink |
| |
Affiliation: | Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, 121552, Moscow, Russia. |
| |
Abstract: | Atypical cell surface lipoprotein-binding proteins of 105 kDa and 130 kDa are present in membranes of vascular smooth muscle cells. We recently identified the 105 kDa protein from human aortic media as T-cadherin, an unusual glycosylphosphatidylinositol (GPI)-anchored member of the cadherin family of cell adhesion proteins. The goal of the present study was to determine the identity of 130 kDa lipoprotein-binding protein of smooth muscle cells. We applied different approaches that included protein sequencing of purified protein from human aortic media, the use of human T-cadherin peptide-specific antisera, and enzymatic treatment of cultured cells with trypsin and GPI-specific phospholipase C. Our results indicate that the 130 kDa protein is a partially processed form of T-cadherin which is attached to the membrane surface of smooth muscle cells via a GPI anchor and contains uncleaved N-terminal propeptide sequence. Our data disclose that, in contrast to classical cadherins, T-cadherin is expressed on the cell surface in both its precursor (130 kDa) and mature (105 kDa) forms. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|