Abstract
We previously have identified a novel cell surface heparan sulfate/heparin (HS/HP)-interacting protein (HIP) found in human uterine epithelia and a variety of other human epithelial and endothelial cells and cell lines (Liu, S., Smith, S. E., Julian, J., Rohde, L. H., Karin, N. J., and Carson, D. D. (1996) J. Biol. Chem. 271, 11817-11823; Rohde, L. H., Julian, J., Babaknia, A., and Carson, D. D. (1996) J. Biol. Chem. 271, 11824-11830). The amino acid sequence predicted for HIP revealed a potential HS/HP-binding motif. In the present studies, a synthetic peptide corresponding to this putative HS/HP-binding motif, HIP peptide, was synthesized and examined with regard to its HS/HP binding and cell attachment promoting activity. Results using solid phase binding assays demonstrate that HIP peptide binds HS/HP with high selectivity and has high affinity for bulk HP (50% saturation congruent with 300 nM) and even higher affinity for a subset of polysaccharides found in commercial [3H]HP (half-saturation congruent with 10 nM). Moreover, HIP peptide binds subsets of cell and extracellular matrix-associated HS and dermatan sulfate expressed by RL95 cells, a human uterine adenocarcinoma cell line. HIP peptide also binds a similar fractio...Continue Reading
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