FEBS Letters · 1998 · 51 citations · 26 references
Life SciencesBiochemistryMolecular BiologyProtein BiochemistryProtein-protein InteractionsProteomicsCardiovascular Molecular PhysiologyCardiovascular PathophysiologyLipid-protein InteractionsLipoprotein AnalysisProtein BindingProtein-lipid InteractionsCell Adhesion ProteinsLipoprotein InteractionsLipoprotein Receptors
We have previously described an atypical lipoprotein-binding protein of about 105 kDa (p105) in membranes of vascular smooth muscle cells (VSMCs) that is distinct from currently known lipoprotein receptors. In the present work we have developed a procedure for purification of p105 from human aortic media. Partial sequencing of purified protein has revealed identity of p105 with human T-cadherin. Anti-peptide antisera raised against human T-cadherin recognized a protein spot corresponding to the purified p105 on two-dimensional Western blots. The antisera also inhibited LDL binding to p105 on ligand blots. We conclude that the 105 kDa lipoprotein-binding protein present in human VSMCs is T-cadherin, an unusual glycosylphosphatidylinositol-anchored member of the cadherin family of cell-cell adhesion proteins.
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