Mouse Mast Cell Protease 9, a Novel Member of the Chromosome 14 Family of Serine Proteases that is Selectively Expressed in Uterine Mast Cells
| Autor: | Eric Feyfant, Michael F. Gurish, Chifu Huang, Richard L. Stevens, K. Frank Austen, Andrej Sali, N Ghildyal, Hunt Je, Daniel S. Friend, S Stechschulte |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Proteases medicine.medical_treatment Molecular Sequence Data Static Electricity Biochemistry Protein Structure Secondary Serine Mice parasitic diseases medicine Animals Serglycin Amino Acid Sequence Mast Cells RNA Messenger Cloning Molecular Molecular Biology Peptide sequence Gene Serine protease Mice Inbred BALB C Protease Base Sequence Sequence Homology Amino Acid biology Serine Endopeptidases Uterus Chymase Chromosome Mapping Cell Biology Immunohistochemistry Molecular biology biology.protein Female |
| Zdroj: | Journal of Biological Chemistry. 272:29158-29166 |
| ISSN: | 0021-9258 |
| Popis: | 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 approximately 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 approximately 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. |
| Databáze: | OpenAIRE |
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