Calpain Activity Promotes the Sealing of Severed Giant Axons

A barrier (seal) must form at the cut ends of a severed axon if a neuron is to survive and eventually regenerate. Following severance of crayfish medial giant axons in physiological saline, vesicles accumulate at the cut end and form a barrier (seal) to ion and dye diffusion. In contrast, squid gian...

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Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 94; no. 9; pp. 4751 - 4756
Main Authors:	Godell, Christopher M., Smyers, Mark E., Eddleman, Christopher S., Ballinger, Martis L., Fishman, Harvey M., Bittner, George D.
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences of the United States of America 29-04-1997 National Acad Sciences National Academy of Sciences The National Academy of Sciences of the USA
Subjects:	Animals Astacoidea Axons Axons - drug effects Axons - physiology Biological Sciences Calpain - pharmacology Cell Membrane - drug effects Cell Membrane - physiology Crayfish Current density Cysteine Proteinase Inhibitors - pharmacology Decapodiformes Dyes Electric Conductivity Fluorescence Loligo pealei Marine Membrane Fusion - drug effects Membrane Potentials Membranes Molecular biology Neurobiology Neurology Neuroscience P branes Proteins Seals Sepioteuthis lessoniana Species Specificity Squid
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Summary:	A barrier (seal) must form at the cut ends of a severed axon if a neuron is to survive and eventually regenerate. Following severance of crayfish medial giant axons in physiological saline, vesicles accumulate at the cut end and form a barrier (seal) to ion and dye diffusion. In contrast, squid giant axons do not seal, even though injury-induced vesicles form after axonal transection and accumulate at cut axonal ends. Neither axon seals in Ca2+-free salines. The addition of calpain to the bath saline induces the sealing of squid giant axons, whereas the addition of inhibitors of calpain activity inhibits the sealing of crayfish medial giant axons. These complementary effects involving calpain in two different axons suggest that endogenous calpain activity promotes plasmalemmal repair by vesicles or other membranes which form a plug or a continuous membrane barrier to seal cut axonal ends.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 To whom reprint requests should be addressed at: Department of Zoology, University of Texas, Austin, TX 78712-1064 Donald Kennedy, Stanford University, Stanford, CA
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.94.9.4751