Linked Life Data

6083791

Source:http://linkedlifedata.com/resource/pubmed/id/6083791

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-2-4
pubmed:abstractText
Neuronal and astroblast-rich cultures from rat brain degrade exogenously added substance P. The rate of degradation is decreased by diisopropylfluorophosphate, phosphoramidon and bacitracin, but not by N-ethylmaleimide or bestatin. When diisopropylfluorophosphate, phosphoramidon and bacitracin are simultaneously present in the culture medium, the degradation of substance P is completely inhibited. These results indicate that the hydrolysis of substance P by intact cells is catalyzed by the post-proline dipeptidylaminopeptidase (EC 3.4.14.5), the thermolysin-like metallopeptidase ("enkephalinase", EC 3.4.24.11) and a yet uncharacterized bacitracin-sensitive activity. While the thermolysin-like metallopeptidase is mainly associated with glial cells, the specific activity of the other enzymes is five times higher in the neuronal culture.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
728-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Degradation of substance P by neurones and glial cells.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't