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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0010453,
umls-concept:C0010853,
umls-concept:C0027882,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0085103,
umls-concept:C0152060,
umls-concept:C0332120,
umls-concept:C0596901,
umls-concept:C1444748,
umls-concept:C1627358,
umls-concept:C1707798,
umls-concept:C1880352,
umls-concept:C2263455,
umls-concept:C2349975
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pubmed:issue |
10
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pubmed:dateCreated |
1991-11-25
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pubmed:abstractText |
Neurites of cultured septal neurons were transected with a laser under sterile conditions, and the subsequent membrane resealing was assayed using a dye exclusion method. In agreement with findings in other preparations, Ca2+ enhanced resealing: in normal culture medium the percentage of lesioned neurons that resealed within 20-30 min after transection increased with increasing bath [Ca2+] over the range 10(-7) to 2 x 10(-3) M; about 75% of cells resealed in 2 mM Ca2+. Mn2+ and Sr2+ also enhanced resealing, but Mg2+ inhibited it. The percentage of resealing neurons was sensitive to agents known to alter the stability of cytoskeletal components. Agents that tend to disassemble microtubules and/or neurofilaments (e.g., colchicine, low-ionic-strength media) strongly promoted resealing, whereas treatments that tend to stabilize microtubules (taxol, Mg2+) inhibited resealing. Addition of exogenous proteases (papain, trypsin, or dispase) enhanced resealing, whereas inhibitors of cysteine proteases (including a specific inhibitor of calpain, a Ca-activated neutral protease) strongly inhibited resealing. Calmodulin inhibitors inhibited resealing, consistent with reports that calmodulin facilitates calpain-mediated proteolysis of fodrin, a component of the cortical cytoskeleton. Based on these results, we hypothesize that one of the major mechanisms involved in resealing is activation of endogenous proteases by Ca2+ entry into the injured neurite. The resulting changes in the cellular cytoskeleton might promote fusion and resealing of the cut ends of the plasma membrane by enhancing membrane mobility and/or by removing structures that normally prevent membrane-membrane contact.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0270-6474
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3257-67
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1941083-Animals,
pubmed-meshheading:1941083-Axons,
pubmed-meshheading:1941083-Calcium,
pubmed-meshheading:1941083-Cell Membrane,
pubmed-meshheading:1941083-Cells, Cultured,
pubmed-meshheading:1941083-Cytoskeleton,
pubmed-meshheading:1941083-Denervation,
pubmed-meshheading:1941083-Endopeptidases,
pubmed-meshheading:1941083-Neurons,
pubmed-meshheading:1941083-Protease Inhibitors,
pubmed-meshheading:1941083-Rats,
pubmed-meshheading:1941083-Septum Pellucidum
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pubmed:year |
1991
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pubmed:articleTitle |
Membrane resealing in cultured rat septal neurons after neurite transection: evidence for enhancement by Ca(2+)-triggered protease activity and cytoskeletal disassembly.
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pubmed:affiliation |
Department of Physiology and Biophysics, University of Miami School of Medicine, Florida 33101.
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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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