Identification of 130 kDa cell surface LDL-binding protein from smooth muscle cells as a partially processed T-cadherin precursor
| Autor: | Andrej A. Azmuko, Natalia M. Kashirina, Vsevolod A. Tkachuk, Tanya N. Vlasik, Zhanna D. Bespalova, Dmitry Stambolsky, Maria Philippova, Thérèse J. Resink, Valery N. Bochkov, Yelena S. Kuzmenko |
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| Rok vydání: | 1999 |
| Předmět: |
Vascular smooth muscle
Immunoblotting Biophysics Biology Biochemistry Epitope Muscle Smooth Vascular Cell membrane Epitopes HSPA2 medicine Humans Protein Precursors Protein precursor Cell adhesion Lipoprotein Aorta Cells Cultured Cadherin Immune Sera Cell Membrane Cell Biology Cadherins Molecular biology Cell biology T-cadherin Molecular Weight medicine.anatomical_structure Receptors LDL Vascular smooth muscle cell |
| Zdroj: | Biochimica et biophysica acta. 1416(1-2) |
| ISSN: | 0006-3002 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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