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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
1994-6-6
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pubmed:abstractText |
HB-GAM (heparin binding growth-associated molecule; pleiotrophin) is a secretory, extracellular matrix-associated protein that is strongly expressed in developing nervous tissues and belongs to a novel family of differentiation/growth factors. It promotes axonal growth from perinatal rat brain neurons and is suggested to be mitogenic for some cell types and to display cell-transforming activity. Since the receptors of HB-GAM in cells are unknown, we have started isolation of putative cell surface receptors from brain neurons and from perinatal rat brain. For this purpose, recombinant HB-GAM was produced with the aid of a baculovirus vector and used as an affinity matrix in receptor isolation. A detergent-solubilized component from cultured brain neurons and from brain was identified that binds specifically to HB-GAM and migrates on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a broad smear with an apparent molecular mass of about 200 kDa. This cell surface component was found to contain heparan sulfate chains, which are bound to a core protein with an apparent molecular mass of 120 kDa. Gel electrophoretic characteristics, immunochemical analysis, and partial peptide sequencing revealed that the cell surface component isolated as an HB-GAM receptor is N-syndecan (syndecan-3). In a solid phase binding assay, N-syndecan was found to bind to HB-GAM in a similar manner as to basic fibroblast growth factor (KD = 0.6 nM). Immunofluorescence microscopy indicated that in brain neurons, N-syndecan occurs at the surface of the cell soma and of the neurites that grow along HB-GAM-coated substrates. Anti-N-syndecan antibodies added to culture media had an inhibitory effect on HB-GAM-induced neurite outgrowth. We suggest that N-syndecan mediates the neurite outgrowth-promoting signal from HB-GAM to the cytoskeleton of growing neurites.
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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,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Sdc3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-3,
http://linkedlifedata.com/resource/pubmed/chemical/pleiotrophin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12999-3004
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8175719-Amino Acid Sequence,
pubmed-meshheading:8175719-Animals,
pubmed-meshheading:8175719-Antibodies,
pubmed-meshheading:8175719-Brain,
pubmed-meshheading:8175719-Carrier Proteins,
pubmed-meshheading:8175719-Cytokines,
pubmed-meshheading:8175719-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8175719-Fluorescent Antibody Technique,
pubmed-meshheading:8175719-Membrane Glycoproteins,
pubmed-meshheading:8175719-Molecular Sequence Data,
pubmed-meshheading:8175719-Nerve Tissue Proteins,
pubmed-meshheading:8175719-Neurites,
pubmed-meshheading:8175719-Neurons,
pubmed-meshheading:8175719-Proteoglycans,
pubmed-meshheading:8175719-Rats,
pubmed-meshheading:8175719-Syndecan-3
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pubmed:year |
1994
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pubmed:articleTitle |
Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3).
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pubmed:affiliation |
Laboratory of Molecular Neurobiology, University of Helsinki, Finland.
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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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