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      CD44 is the principal cell surface receptor for hyaluronate.

      Cell
      Amino Acid Sequence, Animals, Antibodies, Monoclonal, diagnostic use, Antigens, CD44, Antigens, Differentiation, genetics, Base Sequence, Binding, Competitive, Cell Adhesion Molecules, metabolism, Cell Line, Cells, Cultured, Cricetinae, Endothelium, Glycosaminoglycans, pharmacology, Lymph Nodes, immunology, Membrane Glycoproteins, Molecular Sequence Data, Oligonucleotide Probes, Rats, Receptors, Cell Surface, Receptors, Lymphocyte Homing, Recombinant Fusion Proteins, Sequence Homology, Nucleic Acid

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          Abstract

          CD44 is a broadly distributed cell surface protein thought to mediate cell attachment to extracelular matrix components or specific cell surface ligands. We have created soluble CD44-immunoglobulin fusion proteins and characterized their reactivity with tissue sections and lymph node high endothelial cells in primary culture. The CD44 target on high endothelial cells is sensitive to enzymes that degrade hyaluronate, and binding of soluble CD44 is blocked by low concentrations of hyaluronate or high concentrations of chondroitin 4- and 6-sulfates. A mouse anti-hamster hyaluonate receptor antibody reacts with COS cells expressing hamster CD44 cDNA. In sections of all tissues examined, including lymph nodes and Peyer's patches, predigestion with hyaluronidase eliminated CD44 binding.

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          Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease

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            A tissue-specific endothelial cell molecule involved in lymphocyte homing.

            An endothelial cell surface molecule that is selectively expressed in mucosal organs is required for lymphocyte homing to mucosal lymphoid tissues. This 'vascular addressin' appears to function as a tissue-specific marker or address signal for recognition by lymphocytes circulating in the blood.
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              A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family.

              Monoclonal antibodies in the Hermes family recognize a lymphocyte structure that participates in lymphocyte adhesion to endothelium and has been suggested to be the human homolog of the murine Mel-14 lymph node homing receptor. Recently, antibodies against the Hermes antigen, the polymorphic glycoprotein Pgp-1 antigen, and the broadly expressed CDw44 antigen have been shown to recognize the same structure. In this work, cDNA clones encoding the CDw44 antigen were isolated and expressed in COS cells. Two forms were identified: a lymphoid form expressed in hematopoietic cells, and an epithelial form weakly expressed in normal epithelium but highly expressed in carcinomas. The extracellular domain of CDw44 bears homology to cartilage link proteins and a related segment of proteoglycan core protein. However, comparison with the recently identified sequence of the Mel-14 antigen shows that CDw44 and Mel-14 are unrelated.
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