Linked Life Data

10851245

Source:http://linkedlifedata.com/resource/pubmed/id/10851245

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2000-9-21
pubmed:abstractText
alpha-Latrotoxin, a component of black widow spider venom, stimulates transmitter release from nerve terminals and intact chromaffin cells and enhances secretion from permeabilized chromaffin cells already maximally stimulated by Ca(2+). In this study we demonstrate that chromaffin cells contain a protein antigenically similar to the cloned Ca(2+)-independent receptor for alpha-latrotoxin. Although this receptor has homology to the secretin family of G-protein-linked receptors, pertussis toxin has no effect on the ability of alpha-latrotoxin to enhance secretion, suggesting that neither G(i) nor G(o) is involved in the response. Furthermore, in the absence of Ca(2+), alpha-latrotoxin does not stimulate polyphosphoinositide-specific phospholipase C. alpha-Latrotoxin specifically enhances ATP-dependent secretion in permeabilized cells. An in situ assay for protein kinase C reveals that alpha-latrotoxin augments the activation of protein kinase C by Ca(2+), and use of protein kinase inhibitors demonstrates that this activation is important for the toxin's enhancing effect. This enhancement of secretion requires Ca(2+) concentrations above 3 microm and is not supported by Ba(2+) or nonhydrolyzable guanine nucleotides, which do not stimulate protein kinase C. We conclude that alpha-latrotoxin stimulates secretion in permeabilized cells by regulating a Ca(2+)- and ATP-dependent event involving protein kinase C.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25351-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10851245-Adenosine Triphosphate, pubmed-meshheading:10851245-Animals, pubmed-meshheading:10851245-Calcium, pubmed-meshheading:10851245-Calcium Chloride, pubmed-meshheading:10851245-Cattle, pubmed-meshheading:10851245-Cell Line, pubmed-meshheading:10851245-Cell Membrane Permeability, pubmed-meshheading:10851245-Cells, Cultured, pubmed-meshheading:10851245-Chromaffin Cells, pubmed-meshheading:10851245-Concanavalin A, pubmed-meshheading:10851245-Dose-Response Relationship, Drug, pubmed-meshheading:10851245-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10851245-Humans, pubmed-meshheading:10851245-Inositol 1,4,5-Trisphosphate, pubmed-meshheading:10851245-Magnesium Chloride, pubmed-meshheading:10851245-Protein Kinase C, pubmed-meshheading:10851245-Signal Transduction, pubmed-meshheading:10851245-Spectrometry, Fluorescence, pubmed-meshheading:10851245-Spider Venoms, pubmed-meshheading:10851245-Time Factors, pubmed-meshheading:10851245-Trypsin
pubmed:year
2000
pubmed:articleTitle
Latrotoxin stimulates secretion in permeabilized cells by regulating an intracellular Ca2+ - and ATP-dependent event: a role for protein kinase C.
pubmed:affiliation
Department of Pharmacology, the University of Michigan Medical School, Ann Arbor 48109, USA. mbittner@umich.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.