Mouse Mast Cell Protease 9, a Novel Member of the Chromosome 14 Family of Serine Proteases that is Selectively Expressed in Uterine Mast Cells *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 272, Issue: 46, Page: 29158-29166
1997
- 53Citations
- 17Captures
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Metrics Details
- Citations53
- Citation Indexes53
- 53
- CrossRef48
- Captures17
- Readers17
- 17
Article Description
Mouse mast cell protease (mMCP) 1, mMCP-2, mMCP-4, and mMCP-5 are members of a family of related serine proteases whose genes reside within an ∼850 kilobase (kb) complex on chromosome 14 that does not readily undergo crossover events. While mapping the mMCP-1 gene, we isolated a novel gene that encodes a homologous serine protease designated mMCP-9. The mMCP-9 and mMCP-1 genes are only ∼7 kb apart on the chromosome and are oriented back to back. The proximity of the mMCP-1 and mMCP-9 genes now suggests that the low recombination frequency of the complex is due to the closeness of some of its genes. The mMCP-9 transcript and protein were observed in the jejunal submucosa of Trichinella spiralis -infected BALB/c mice. However, in normal BALB/c mice, mMCP-9 transcript and protein were found only in those mast cells that reside in the uterus. Thus, the expression of mMCP-9 differs from that of all other chymases. The observation that BALB/c mouse bone marrow-derived mast cells developed with interleukin (IL) 10 and c- kit ligand contain mMCP-9 transcript, whereas those developed with IL-3 do not, indicates that the expression of this particular chymase is regulated by the cytokine microenvironment. Comparative protein structure modeling revealed that mMCP-9 is the only known granule protease with three positively charged regions on its surface. This property may allow mMCP-9 to form multimeric complexes with serglycin proteoglycans and other negatively charged proteins inside the granule. Although mMCP-9 exhibits a >50% overall amino acid sequence identity with its homologous chymases, it has a unique substrate-binding cleft. This finding suggests that each member of the chromosome 14 family of serine proteases evolved to degrade a distinct group of proteins.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818508693; http://dx.doi.org/10.1074/jbc.272.46.29158; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=14444268722&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9360993; https://linkinghub.elsevier.com/retrieve/pii/S0021925818508693; https://dx.doi.org/10.1074/jbc.272.46.29158
Elsevier BV
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