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pubmed-article:9364065pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:9364065pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9364065pubmed:articleTitleNeuronal and non-neuronal collapsin-1 binding sites in developing chick are distinct from other semaphorin binding sites.lld:pubmed
pubmed-article:9364065pubmed:affiliationDepartment of Neurology, Yale University, New Haven, Connecticut 06520, USA.lld:pubmed
pubmed-article:9364065pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9364065pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:9364065pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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