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
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.
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