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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0007412,
umls-concept:C0030685,
umls-concept:C0084484,
umls-concept:C0333117,
umls-concept:C0376604,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C0851827,
umls-concept:C1283071,
umls-concept:C1444748,
umls-concept:C1517945,
umls-concept:C1701901,
umls-concept:C1707520,
umls-concept:C1963578
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pubmed:issue |
5
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pubmed:dateCreated |
1992-11-20
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pubmed:abstractText |
Exposure of chromaffin cells to digitonin causes the loss of many cytosolic proteins. Here we report that scinderin (a Ca(2+)-dependent actin-filament-severing protein), but not gelsolin, is among the proteins that leak out from digitonin-permeabilized cells. Chromaffin cells that were exposed to increasing concentrations (15-40 microM) of digitonin for 5 min released scinderin into the medium. One-minute treatment with 20 microM digitonin was enough to detect scinderin in the medium, and scinderin leakage levelled off after 10 min of permeabilization. Elevation of free Ca2+ concentration in the permeabilizing medium produced a dose-dependent retention of scinderin. Results were confirmed by immunofluorescence microscopy of digitonin-permeabilized cells. Subcellular fractionation of permeabilized cells showed that scinderin leakage was mainly from the cytoplasm (80%); the remaining scinderin (20%) was from the microsomal fraction. Other Ca(2+)-binding proteins released by digitonin and also retained by Ca2+ were calmodulin, protein kinase C, and calcineurins A and B. Scinderin leakage was parallel to the loss of the chromaffin cell secretory response. Permeabilization in the presence of increasing free Ca2+ concentrations produced a concomitant enhancement in the subsequent Ca(2+)-dependent catecholamine release. The experiments suggest that: (1) scinderin is an intracellular target for Ca2+, (2) permeabilization of chromaffin cells with digitonin in the presence of micromolar Ca2+ concentrations retained Ca(2+)-binding proteins including scinderin, and (3) the retention of these proteins may be related to the increase in the subsequent Ca(2+)-dependent catecholamine release observed in permeabilized chromaffin cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Catecholamines,
http://linkedlifedata.com/resource/pubmed/chemical/Digitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Gelsolin,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/scinderin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1717-28
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1402916-Adrenal Medulla,
pubmed-meshheading:1402916-Animals,
pubmed-meshheading:1402916-Calcium,
pubmed-meshheading:1402916-Catecholamines,
pubmed-meshheading:1402916-Cattle,
pubmed-meshheading:1402916-Cells, Cultured,
pubmed-meshheading:1402916-Cytosol,
pubmed-meshheading:1402916-Digitonin,
pubmed-meshheading:1402916-Dose-Response Relationship, Drug,
pubmed-meshheading:1402916-Gelsolin,
pubmed-meshheading:1402916-Microfilament Proteins,
pubmed-meshheading:1402916-Subcellular Fractions
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pubmed:year |
1992
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pubmed:articleTitle |
Loss and Ca(2+)-dependent retention of scinderin in digitonin-permeabilized chromaffin cells: correlation with Ca(2+)-evoked catecholamine release.
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pubmed:affiliation |
Department of Pharmacology, Faculty of Medicine, University of Ottawa, Ontario, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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