Linked Life Data

7542684

Source:http://linkedlifedata.com/resource/pubmed/id/7542684

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-8-31
pubmed:abstractText
We have evaluated the spectrophotometric measurement (at 401 vs. 411 nm) of nitric oxide (NO)-dependent methemoglobin formation from oxyhemoglobin in order to assess NO release from human polymorphonuclear neutrophil leukocytes (PMN). S-nitroso-D,L-acetyl-penicillamine (SNAP, 25-200 microM), a donor of NO, induced a dose-dependent methemoglobin formation. Furthermore, when PMN were activated with N-formyl-methionylleucyl-phenylalanine or phorbol myristate acetate in the presence of superoxide dismutase (SOD) and catalase, methemoglobin formation ensued. The amount of methemoglobin formed was dependent on the amounts of oxyhemoglobin and stimulus used, and the number of PMN in the assay. The NO synthase (NOS) inhibitors NG-monomethyl-L-arginine or nitro-L-arginine methyl ester did not affect methemoglobin generation from oxyhemoglobin induced by SNAP but inhibited that mediated by activated PMN with IC50 values of 250 microM and 340 microM, respectively. The substrate for NO formation from NOS, L-arginine in concentrations up to 1 mM did not significantly influence the methemoglobin formation either induced by SNAP or activated PMN. Exclusion of SOD did not affect SNAP-dependent oxidation of oxyhemoglobin. Exclusion of SOD from the cell-containing system attenuated methemoglobin formation, and if catalase was also excluded the response was further reduced. Finally, PMN from a patient with X-linked chronic granulomatous disease, unable to produce superoxide anions, showed a similar production of methemoglobin from HbO2 as did healthy PMN, activated with the respective agonists. We conclude that spectrophotometric measurement of methemoglobin formation from oxyhemoglobin in the presence of SOD and catalase is a suitable method for the measurement of NO release from PMN, with the benefits of a real-time, continuous assay.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
184
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
53-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Measurement of methemoglobin formation from oxyhemoglobin. A real-time, continuous assay of nitric oxide release by human polymorphonuclear leukocytes.
pubmed:affiliation
Department of Medicine, Karolinska Institute, Stockholm Söder Hospital, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't