Linked Life Data

7864886

Source:http://linkedlifedata.com/resource/pubmed/id/7864886

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-3-23
pubmed:abstractText
S-nitrosylation by sodium nitroprusside, a nitric oxide-generating agent, inactivates, almost completely at neutral pH, the proteolytic activity of the high Ca2+ requiring calpain form (m-calpain) from skeletal muscle. This inhibition is reversed by treating the inactivated proteinase with dithiothreitol. When exposed to sodium nitroprusside, the single m-calpain-like isoform from human neutrophils is inactivated too. On the contrary, the activities of muscle mu-calpain isoform and the human erythrocyte single mu-calpain-like isoform are poorly affected by nitric oxide treatment at neutral pH; however, inactivation is progressively enhanced if the pH of incubation mixtures is shifted to acidic values, a condition which conversely reduces NO-mediated inactivation of m-calpain. On the basis of these results, it is conceivable to postulate that nitric oxide may exert a regulatory role of muscle calpain activity by modulation of either one or the other proteinase isoform, also in concomitance with fluctuations of hydrogen ions in contracting cells occurring in physiological or pathological conditions. The regulatory role of nitric oxide is also supported by the observation that S-nitrosylation induces inactivation of calpain also in intact human neutrophils. Furthermore, the reversibility of the inactivation of calpain by nitric oxide may be exploited to study the relationship between the molecular structure and the catalytic and regulatory mechanisms of this neutral proteinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
207
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1009-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Reversible inactivation of calpain isoforms by nitric oxide.
pubmed:affiliation
Institute of Biological Chemistry, Genoa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't