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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1997-12-15
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pubmed:abstractText |
The collapsin and semaphorin family of extracellular proteins contributes to axonal path finding by repulsing axons and collapsing growth cones. To explore the mechanism of collapsin-1 action, we expressed and purified a truncated collapsin-1-alkaline phosphatase fusion protein (CAP-4). This protein retains biological activity as a DRG growth cone collapsing agent and saturably binds to DRG neurons with low nanomolar affinity. Specific CAP-4 binding sites are present on DRG neurons, sympathetic neurons, and motoneurons, but not on retinal, cortical, or brainstem neurons. Outside the nervous system, high levels of CAP-4 binding sites are present in the mesenchyme surrounding major blood vessels and developing bone and in lung. These sites provide a substrate for the collapsin-1-dependent patterning of non-neuronal tissues perturbed in sema III (-/-) mice. The staining patterns for mouse semaphorin D/III and chick collapsin-1 fusion proteins are indistinguishable from one another but quite separate from that for semaphorin B and M-semaphorin F fusion proteins. These data imply that a family of high-affinity semaphorin binding sites similar in complexity to the semaphorin ligand family exists.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Avian Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Fetal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotrophin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Semaphorin-3A
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0270-6474
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9183-93
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9364065-Animals,
pubmed-meshheading:9364065-Avian Proteins,
pubmed-meshheading:9364065-Axons,
pubmed-meshheading:9364065-Binding Sites,
pubmed-meshheading:9364065-Cells, Cultured,
pubmed-meshheading:9364065-Central Nervous System,
pubmed-meshheading:9364065-Chick Embryo,
pubmed-meshheading:9364065-DNA, Complementary,
pubmed-meshheading:9364065-Fetal Proteins,
pubmed-meshheading:9364065-Ganglia, Spinal,
pubmed-meshheading:9364065-Glycoproteins,
pubmed-meshheading:9364065-Lung,
pubmed-meshheading:9364065-Membrane Proteins,
pubmed-meshheading:9364065-Mesoderm,
pubmed-meshheading:9364065-Mice,
pubmed-meshheading:9364065-Motor Neurons,
pubmed-meshheading:9364065-Multigene Family,
pubmed-meshheading:9364065-Nerve Growth Factors,
pubmed-meshheading:9364065-Nerve Tissue Proteins,
pubmed-meshheading:9364065-Neurons,
pubmed-meshheading:9364065-Neurotrophin 3,
pubmed-meshheading:9364065-Organ Specificity,
pubmed-meshheading:9364065-Rats,
pubmed-meshheading:9364065-Rats, Sprague-Dawley,
pubmed-meshheading:9364065-Receptors, Cell Surface,
pubmed-meshheading:9364065-Recombinant Fusion Proteins,
pubmed-meshheading:9364065-Semaphorin-3A
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pubmed:year |
1997
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pubmed:articleTitle |
Neuronal and non-neuronal collapsin-1 binding sites in developing chick are distinct from other semaphorin binding sites.
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pubmed:affiliation |
Department of Neurology, Yale University, New Haven, Connecticut 06520, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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