Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-7-26
pubmed:abstractText
Somatostatin was degraded by the synaptic membrane from rat hippocampus. Cleavage products were separated by reversed phase high performance liquid chromatography and identified by amino acid composition analyses and N-terminal amino acid and sequence determinations around the cleavage sites. Fragments produced from the cleavages at both or either sites between the Phe6-Phe7 and/or between the Thr10-Phe11, together with free phenylalanine and tryptophan, were major cleavage products, followed by that produced from the cleavage of the Asn5-Phe6 bond. The accumulation of the major cleavage products, as well as the initial cleavage of somatostatin, was strongly inhibited by metal chelators and also by specific inhibitors of endopeptidase-24.11 (EC 3.4.24.11), phosphoramidon and thiorphan. The inhibitor susceptibility of the synaptic membrane toward somatostatin was similar to that toward Leu-enkephalin, a natural substrate of endopeptidase-24.11. Furthermore, endopeptidase-24.11 purified from rat brain hydrolyzed somatostatin at the cleavage sites identical to those by the hippocampal synaptic membrane. Thus, it can be concluded that endopeptidase-24.11 plays a major role in the initial stage of somatostatin degradation in rat hippocampus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
287-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
The degradation of somatostatin by synaptic membrane of rat hippocampus is initiated by endopeptidase-24.11.
pubmed:affiliation
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't