Identification of 130 kDa cell surface LDL-binding protein from smooth muscle cells as a partially processed T-cadherin precursor

被引:19
|
作者
Stambolsky, DV
Kuzmenko, YS
Philippova, MP
Bochkov, VN [1 ]
Bespalova, ZD
Azmuko, AA
Kashirina, NM
Vlasik, TN
Tkachuk, VA
Resink, TJ
机构
[1] Cardiol Res Ctr, Inst Expt Cardiol, Mol Endocrinol Lab, Moscow 121552, Russia
[2] Cardiol Res Ctr, Inst Expt Cardiol, Lab Peptide Synth, Moscow 121552, Russia
[3] Cardiol Res Ctr, Inst Expt Cardiol, Lab Prot Engn, Moscow 121552, Russia
[4] Univ Basel Hosp, Dept Res, Cardiovasc Labs, CH-4031 Basel, Switzerland
来源
关键词
lipoprotein; cadherin; vascular smooth muscle cell;
D O I
10.1016/S0005-2736(98)00218-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 CPI-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. (C) 1999 Elsevier Science B.V. All rights reserved.
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页码:155 / 160
页数:6
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