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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1990-5-7
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pubmed:abstractText |
Recent biochemical and sequence data suggest a possible relationship between Pgp-1 (identical to CD44/Hermes 1/p85) and a hyaluronic acid-binding function. Here, we have studied the hyaluronic acid-binding activity of a series of murine hematopoietic cell lines using several assays: cell aggregation by hyaluronic acid, binding of fluorescein-conjugated hyaluronic acid, and cell adhesion to hyaluronic acid-coated dishes. Certain Pgp-1-positive T and B cell lines show hyaluronic acid binding that is highly specific and is not competed for by other glycosaminoglycans. Monoclonal antibodies against Pgp-1, but not antibodies against other major cell surface glycoproteins, inhibited hyaluronic acid-induced cell aggregation and cell adhesion to hyaluronic acid-coated dishes. Additionally, some anti-Pgp-1 antibodies inhibited binding of fluorescein-hyaluronic acid to hyaluronic acid-binding lines. We found no Pgp-1-negative lines that bound, but many Pgp-1-positive cell lines did not bind hyaluronic acid. Two Pgp-1-positive thymomas that did not bind hyaluronic acid were induced by phorbol ester to bind hyaluronic acid with the same specificity as other hyaluronic acid-binding lines. Normal hematopoietic cells, including those which express high levels of Pgp-1, such as bone marrow myeloid cells and splenic lymphocytes, showed no detectable hyaluronic acid-binding activity. We discuss several models that might account for these observations: (1) the hyaluronic acid receptor is Pgp-1, but it normally exists in an inactive state; (2) hyaluronic acid receptors are a subset of a family of molecules recognized by anti-Pgp-1 antibodies; (3) the hyaluronic acid receptor is not Pgp-1, but is closely associated with Pgp-1 on the surface of cells which express hyaluronic acid-binding activity.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
224-33
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2180732-Animals,
pubmed-meshheading:2180732-Antibodies, Monoclonal,
pubmed-meshheading:2180732-Antigens, Differentiation,
pubmed-meshheading:2180732-B-Lymphocytes,
pubmed-meshheading:2180732-Cell Adhesion Molecules,
pubmed-meshheading:2180732-Cell Aggregation,
pubmed-meshheading:2180732-Cell Line,
pubmed-meshheading:2180732-Hyaluronic Acid,
pubmed-meshheading:2180732-Kinetics,
pubmed-meshheading:2180732-Mice,
pubmed-meshheading:2180732-Receptors, Lymphocyte Homing,
pubmed-meshheading:2180732-T-Lymphocytes,
pubmed-meshheading:2180732-Tumor Cells, Cultured
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pubmed:year |
1990
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pubmed:articleTitle |
Binding of hyaluronic acid to lymphoid cell lines is inhibited by monoclonal antibodies against Pgp-1.
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pubmed:affiliation |
Salk Institute, San Diego, California 92138.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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