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

Citation
Dv. Stambolsky et al., Identification of 130 kDa cell surface LDL-binding protein from smooth muscle cells as a partially processed T-cadherin precursor, BBA-BIOMEMB, 1416(1-2), 1999, pp. 155-160
Citations number
15
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
ISSN journal
00052736 → ACNP
Volume
1416
Issue
1-2
Year of publication
1999
Pages
155 - 160
Database
ISI
SICI code
0005-2736(19990112)1416:1-2<155:IO1KCS>2.0.ZU;2-Y
Abstract
Atypical cell surface lipoprotein-binding proteins of 105 kDa and 130 kDa a re present in membranes of vascular smooth muscle cells. We recently identi fied the 105 kDa protein from human aortic media as T-cadherin, an unusual glycosylphosphatidylinositol (GPI)-anchored member of the cadherin family o f cell adhesion proteins. The goal of the present study was to determine th e identity of 130 kDa lipoprotein-binding protein of smooth muscle cells. W e applied different approaches that included protein sequencing of purified protein from human aortic media, the use of human T-cadherin peptide-speci fic antisera, and enzymatic treatment of cultured cells with trypsin and CP I-specific phospholipase C. Our results indicate that the 130 kDa protein i s a partially processed form of T-cadherin which is attached to the membran e surface of smooth muscle cells via a GPI anchor and contains uncleaved N- terminal propeptide sequence. Our data disclose that, in contrast to classi cal cadherins, T-cadherin is expressed on the cell surface in both its prec ursor (130 kDa) and mature (105 kDa) forms. (C) 1999 Elsevier Science B.V. All rights reserved.