Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1993-9-30
pubmed:databankReference
pubmed:abstractText
Exposure of mouse peritoneal macrophages to oxidative and sulfhydryl-reactive agents in vitro enhances synthesis of a few cellular proteins that may be important in a self-defense system. A cDNA encoding a novel stress-inducible protein, designated MSP23 (macrophage 23-kDa stress protein), was cloned from a cDNA library of the macrophages by differential screening. A 1.0-kilobase mRNA transcript hybridized with the MSP23 cDNA gradually increased in macrophages upon culture in vitro. Treatment with diethylmaleate or glucose/glucose oxidase, which generates H2O2, markedly enhanced the induction of the transcript after several hours. Cadmium chloride and sodium arsenite also induced the transcript. An antiserum raised against recombinant MSP23 reacted with the 23-kDa stress-inducible protein of the macrophages. The amounts of 23-kDa protein in the cells rapidly increased during culture with diethylmaleate. The mRNA was detected in various tissues, and it was especially high in content in the liver. A search of databases revealed that six proteins of various species from bacteria to the mouse have a sequence homology to MSP23. One of the proteins is the C22 component of alkyl hydroperoxide reductase, which is induced by hydrogen peroxide in Salmonella typhimurium.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18633-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:8360158-Amino Acid Sequence, pubmed-meshheading:8360158-Animals, pubmed-meshheading:8360158-Arsenic, pubmed-meshheading:8360158-Arsenites, pubmed-meshheading:8360158-Base Sequence, pubmed-meshheading:8360158-Blotting, Northern, pubmed-meshheading:8360158-Cells, Cultured, pubmed-meshheading:8360158-Cloning, Molecular, pubmed-meshheading:8360158-DNA, pubmed-meshheading:8360158-Heat-Shock Proteins, pubmed-meshheading:8360158-Hydrogen Peroxide, pubmed-meshheading:8360158-Immunoblotting, pubmed-meshheading:8360158-Immunosorbent Techniques, pubmed-meshheading:8360158-Macrophages, pubmed-meshheading:8360158-Maleates, pubmed-meshheading:8360158-Mice, pubmed-meshheading:8360158-Molecular Sequence Data, pubmed-meshheading:8360158-Molecular Weight, pubmed-meshheading:8360158-Nucleic Acid Hybridization, pubmed-meshheading:8360158-Peritoneal Cavity, pubmed-meshheading:8360158-Peroxidases, pubmed-meshheading:8360158-Peroxiredoxins, pubmed-meshheading:8360158-Protein Biosynthesis, pubmed-meshheading:8360158-RNA, Messenger, pubmed-meshheading:8360158-Sodium Compounds, pubmed-meshheading:8360158-Tissue Distribution
pubmed:year
1993
pubmed:articleTitle
Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein.
pubmed:affiliation
Department of Biochemistry, University of Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't