Linked Life Data

8930938

Source:http://linkedlifedata.com/resource/pubmed/id/8930938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-2-20
pubmed:abstractText
Substantial evidence now exists to support a defined complex of interacting proteins, comprised of soluble, vesicle and plasma membrane components, as the core of a general membrane fusion mechanism. Specializations to the general secretory model occur based on cell-specific differences in Ca2+ regulation, secretory organelle types and secretory dynamics. The variation in secretory properties may also result, in part, from isoform diversity and selective-pairing of the molecular components of the core complex. The present report attempts to identify the SNARE proteins found in isolated peptidergic nerve endings of the rat neurohypophysis. The results demonstrate the presence of synaptosomal-associated protein of 25 kD, syntaxin and synaptobrevin as membrane-associated proteins in these nerve endings. Furthermore, we have utilized sucrose density gradient subcellular fractionation and immunoprecipitation protocols to investigate the synaptobrevin isotypes present on secretory granules and to probe using electrophysiological methods their functional relationship to secretion. Secretory granules were found to contain only the synaptobrevin 2 isoform, although the nerve endings themselves were found to possess in addition, synaptobrevin 1 and the closely related protein cellubrevin. Analysis of the secretory characteristics of single nerve endings using membrane capacitance measurements together with Botulinum B toxin dialysis demonstrated the critical importance of synaptobrevin 2 to both the rapid exocytotic release and a slower secretory process, that perhaps includes secretory granule recruitment and priming, in these peptidergic nerve endings.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0028-3835
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Characterization and distribution of SNARE proteins at neuroendocrine nerve endings.
pubmed:affiliation
Department of Physiology, University of Michigan, Ann Arbor 48109-0622, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.