Linked Life Data

9705869

Source:http://linkedlifedata.com/resource/pubmed/id/9705869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-9-17
pubmed:abstractText
Analogs of L-arginine represent the largest and potentially most useful class of NOS inhibitors. However, no competitive protein inhibitors of NOS activity are known so far. The effect of aprotinin (Kunitz inhibitor) on NOS activity is reported here, aprotinin being one of the most extensively studied globular proteins. Present data indicate that aprotinin, clinically used as a trypsin-like serine proteinase inhibitor, inhibits NOS-I and NOS-II with Ki values of 5.0 x 10(-5) M and 7.8 x 10(-5) M, respectively, at pH 7.5 and 37.0 degrees C, thereby representing the first competitive protein inhibitor of NOS activity. Therefore, the clinical use of aprotinin, as a drug, should be under careful control. In addition, aprotinin and aprotinin-like domains are present in a variety of organs, as well as in the Alzheimer's amyloid beta-protein precursor. Thus, the present findings open the way to novel mechanisms likely to be involved in the modulation of NOS activity, under physiological and pathological conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
249
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Aprotinin, the first competitive protein inhibitor of NOS activity.
pubmed:affiliation
Department of Biology, Third University of Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't