Linked Life Data

10085090

Source:http://linkedlifedata.com/resource/pubmed/id/10085090

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1999-4-29
pubmed:abstractText
The myeloid cell-derived calcium-binding murine protein, S100A8, is secreted to act as a chemotactic factor at picomolar concentrations, stimulating recruitment of myeloid cells to inflammatory sites. S100A8 may be exposed to oxygen metabolites, particularly hypochlorite, the major oxidant generated by activated neutrophils at inflammatory sites. Here we show that hypochlorite oxidizes the single Cys residue (Cys41) of S100A8. Electrospray mass spectrometry and SDS-polyacrylamide gel electrophoresis analysis indicated that low concentrations of hypochlorite (40 microM) converted 70-80% of S100A8 to the disulfide-linked homodimer. The mass was 20,707 Da, 92 Da more than expected, indicating additional oxidation of susceptible amino acids (possibly methionine). Phorbol 12-myristate 13-acetate activation of differentiated HL-60 granulocytic cells generated an oxidative burst that was sufficient to efficiently oxidize exogenous S100A8 within 10 min, and results implicate involvement of the myeloperoxidase system. Moreover, disulfide-linked dimer was identified in lung lavage fluid of mice with endotoxin-induced pulmonary injury. S100A8 dimer was inactive in chemotaxis and failed to recruit leukocytes in vivo. Positive chemotactic activity of recombinant Ala41S100A8 indicated that Cys41 was not essential for function and suggested that covalent dimerization may structurally modify accessibility of the chemotactic hinge domain. Disulfide-dependent dimerization may be a physiologically significant regulatory mechanism controlling S100A8-provoked leukocyte recruitment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8561-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10085090-Animals, pubmed-meshheading:10085090-Antigens, Differentiation, pubmed-meshheading:10085090-Bronchoalveolar Lavage Fluid, pubmed-meshheading:10085090-Calcium-Binding Proteins, pubmed-meshheading:10085090-Calgranulin A, pubmed-meshheading:10085090-Chemotactic Factors, pubmed-meshheading:10085090-Cysteine, pubmed-meshheading:10085090-Dimerization, pubmed-meshheading:10085090-Disulfides, pubmed-meshheading:10085090-HL-60 Cells, pubmed-meshheading:10085090-Humans, pubmed-meshheading:10085090-Hypochlorous Acid, pubmed-meshheading:10085090-Inflammation, pubmed-meshheading:10085090-Leukocytes, pubmed-meshheading:10085090-Mass Spectrometry, pubmed-meshheading:10085090-Mice, pubmed-meshheading:10085090-Mutation, pubmed-meshheading:10085090-Oxidants, pubmed-meshheading:10085090-Peroxidase, pubmed-meshheading:10085090-Recombinant Proteins, pubmed-meshheading:10085090-Tetradecanoylphorbol Acetate
pubmed:year
1999
pubmed:articleTitle
Oxidation regulates the inflammatory properties of the murine S100 protein S100A8.
pubmed:affiliation
Cytokine Research Unit, School of Pathology, The University of New South Wales, Kensington, New South Wales 2052, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't