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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-8-5
pubmed:databankReference
pubmed:abstractText
We have isolated a cDNA (NC28) transcribed from a mRNA which is transiently induced in U937 promonocytic cells by PMA and super-induced by cycloheximide. NC28 cDNA encodes a new member of the chemokine family, MCP-3, recently purified from MG-63 osteosarcoma cells by Van Damme et al. [1]. The MCP-3 protein sequence shows 74% identity with human monocyte chemoattractant protein 1 (MCP-1) and, like MCP-1, recombinant MCP-3 protein shows chemotactic activity for monocytes but not for neutrophils. However the secreted MCP-3 protein differs from MCP-1 in being N-glycosylated. The 3' noncoding regions of MCP-3 and MCP-1 mRNAs are more diverged (44%), allowing specific cDNA probes to be made, and indicating that the two genes are evolutionarily distant. Sequence comparisons of the 3' noncoding regions suggest that MCP-3 may be the human homologue of the mouse MARC gene [2], and that MCP-1 and MCP-3 genes arose by a gene duplication event before the mammalian radiation. Both MCP-1 and MCP-3 mRNAs are expressed by PBMC, principally by monocytes, with MCP-1 mRNA being expressed at levels 2-4 times that of MCP-3 mRNA. However, while MCP-1 mRNA is also expressed at high levels in fibroblast or astrocytoma cell lines after IL-1 and TNF stimulation, MCP-3 mRNA is expressed only at very low levels in these cells. The cellular origin of MCP-3 is thus more restricted than that of MCP-1. In our experiments on PBMC, LPS is not a consistent inducer of MCP-1 and MCP-3 mRNAs. In some experiments, it actually decreases levels of these two mRNAs, while concomitantly increasing IL-6 and TNF-alpha mRNA levels. Levels of MCP-1 and MCP-3 mRNAs in PBMC are both increased by IFN-gamma, although IL-6 mRNA is not induced. They are also increased by PHA-P and are decreased, in most cases, by IL-13 [3]. MCP-1 and MCP-3 mRNAs are thus co-ordinately regulated in monocytes in response to a number of inducing or inhibitory agents, in a manner differing in several respects from that of other monokines such as IL-6.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1148-5493
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
99-110
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:8318676-Amino Acid Sequence, pubmed-meshheading:8318676-Animals, pubmed-meshheading:8318676-Base Sequence, pubmed-meshheading:8318676-Biological Evolution, pubmed-meshheading:8318676-Cells, Cultured, pubmed-meshheading:8318676-Chemokine CCL7, pubmed-meshheading:8318676-Chemotactic Factors, pubmed-meshheading:8318676-Cloning, Molecular, pubmed-meshheading:8318676-Cytokines, pubmed-meshheading:8318676-DNA, pubmed-meshheading:8318676-Gene Expression Regulation, pubmed-meshheading:8318676-Humans, pubmed-meshheading:8318676-Mice, pubmed-meshheading:8318676-Molecular Sequence Data, pubmed-meshheading:8318676-Monocyte Chemoattractant Proteins, pubmed-meshheading:8318676-Monocytes, pubmed-meshheading:8318676-RNA, Messenger, pubmed-meshheading:8318676-Rats, pubmed-meshheading:8318676-Sequence Homology, Amino Acid, pubmed-meshheading:8318676-Species Specificity
pubmed:articleTitle
Molecular cloning of the MCP-3 chemokine gene and regulation of its expression.
pubmed:affiliation
Sanofi Elf Bio Recherches, Labège, France.
pubmed:publicationType
Journal Article