Specific binding of albumin to cultured aortic endothelium.
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概要
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Confluent monolayers of cultured bovine aortic endothelial cells (BAEC) at 4°C bound specifically, saturably, and with high affinity radioiodinated bovine serum albumin ([<SUP>125</SUP>I] -BSA). Unlike bovine transferrin, fibrinogen, and immunoglobulin G, albumin significantly displaced [<SUP>125</SUP>I] -BSA binding to the cell surface; 50% inhibition was reached at 15 nM of unlabeled albumin. Binding was reversible, and 45% of the surface associated radioactivity was lost after 2.5 min. The binding data calculated from Scatchard plots were consistent with a single saturable interaction of high affinity with a K<SUB>d</SUB> of 1.6 pmoles, and a B<SUB>max</SUB> of 45 fmoles/2.5 ×10<SUB>5</SUB> cells. The interaction was pH-dependent with an optimum at pH 6.0. Binding was diminished 40% by heparin, 25% by 1 M NaCl but was not markedly affected by cell surface treatment with hyaluronidase and chondroitinase-ABC. Ligand blotting experiments performed with [<SUP>125</SUP>I] -BSA showed that extracts of BAEC expressed two albumin binding peptides of apparent molecular mass of 18 and 31 kDa. The albumin binding to BAEC surface was also demonstrated immunohistochemically.
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