A novel action of collapsin: collapsin-1 increases antero- and retrograde axoplasmic transport independently of growth cone collapse

J Neurobiol. 1997 Sep;33(3):316-28. doi: 10.1002/(sici)1097-4695(199709)33:3<316::aid-neu9>3.0.co;2-4.


Chick collapsin-1, a member of the semaphorin family, has been implicated in axonal pathfinding as a repulsive guidance cue. Collapsin-1 induces growth cone collapse via a pathway which may include CRMP-62 and heterotrimeric G proteins. CRMP-62 protein is related to UNC-33, a nematode neuronal protein required for appropriately directed axonal extension. Mutations in unc-33 affect neural microtubules, the basic cytoskeletal elements for axoplasmic transport. Using computer-assisted video-enhanced differential interference contrast microscopy, we now demonstrate that collapsin-1 potently promotes axoplasmic transport. Collapsin-1 doubles the number of antero- and retrograde-transported organelles but not their velocity. Collapsin-1 decreases the number of stationary organelles, suggesting that the fraction of time during which a particle is moving is increased. Collapsin-1-stimulated transport occurs by a mechanism distinct from that causing growth cone collapse. Pertussis toxin (PTX) but not its B oligomer blocks collapsin-induced growth cone collapse. The holotoxin does not affect collapsin-stimulated axoplasmic transport. Mastoparan and a myelin protein NI-35 induce PTX-sensitive growth cone collapse but do not stimulate axoplasmic transport. These results provide evidence that collapsin has a unique property to activate axonal vesicular transport systems. There are at least two distinct pathways through which collapsin exerts its actions in developing neurons.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Axonal Transport / drug effects*
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • GTP-Binding Proteins / metabolism
  • Ganglia, Spinal / cytology
  • Glycoproteins / pharmacology*
  • Intercellular Signaling Peptides and Proteins
  • Mice
  • Mice, Inbred C57BL
  • Myelin Proteins / pharmacology
  • Nerve Growth Factors / pharmacology
  • Neurites / drug effects
  • Neurites / physiology*
  • Organelles / metabolism
  • Peptides
  • Pertussis Toxin
  • Semaphorin-3A
  • Virulence Factors, Bordetella / pharmacology
  • Wasp Venoms / pharmacology


  • Glycoproteins
  • Intercellular Signaling Peptides and Proteins
  • Myelin Proteins
  • Nerve Growth Factors
  • Peptides
  • Semaphorin-3A
  • Virulence Factors, Bordetella
  • Wasp Venoms
  • mastoparan
  • Pertussis Toxin
  • GTP-Binding Proteins