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Characterization of the gene encoding mouse mast cell protease 8 (mMCP-8), and a comparative analysis of
1Department of Cell and Molecular Biology, Uppsala University, Sweden.
Abstract:
Serine proteases are important granule constituents in several of the major hematopoietic cell lineages. We present here the nucleotide sequence of the gene encoding mouse mast cell protease 8 (mMCP-8). mMCP-8 was initially isolated as a cDNA from a mouse mast cell line, but has recently been found to be expressed primarily by mouse basophils. mMCP-8 and its rat homologues, rMCP-8, -9, and -10, form a new group of mast cell/basophil proteases, which are more closely related to the T-cell granzymes and neutrophil cathepsin G than to the mast cell tryptases and chymases. A dot matrix comparison of the mMCP-8 gene with other closely related hematopoietic serine protease genes shows detectable homology only in the exonic regions of the genes. No indication for conservation in the promoter region or introns was observed. This latter finding indicates that the upstream regulatory region has evolved at a relatively high rate. However, despite the low degree of direct sequence conservation, no major differences in the sizes of introns or exons were observed between mMCP-8 and genes for the closest related hematopoietic serine proteases, the mouse T-cell granzymes and cathepsin G, indicating that after evolutionary separation from the T-cell granzymes and cathepsin G, the majority of mutations primarily involved single base pair substitutions or short insertions or deletions.
Insights
Researchers sequenced the mouse mast cell protease 8 (mMCP-8) gene, primarily expressed in basophils. This protease group is evolutionarily distinct, showing rapid upstream regulatory region evolution but conserved intron/exon structures.
Area of Science:
- Hematology
- Molecular Biology
- Genetics
Background:
- Serine proteases are key granule components in hematopoietic cells.
- Mouse mast cell protease 8 (mMCP-8) is primarily expressed in basophils, not mast cells.
- mMCP-8 and rat homologs form a distinct protease group, related to T-cell granzymes and neutrophil cathepsin G.
Purpose of the Study:
- To present the nucleotide sequence of the gene encoding mouse mast cell protease 8 (mMCP-8).
- To analyze the evolutionary relationship of mMCP-8 to other serine proteases.
- To investigate gene structure conservation and regulatory region evolution.
Main Methods:
- Nucleotide sequencing of the mMCP-8 gene.
- Dot matrix comparison of mMCP-8 gene with related hematopoietic serine protease genes.
- Analysis of exonic and intronic regions, and promoter regions.
Main Results:
- The nucleotide sequence of the mMCP-8 gene was determined.
- Homology was detected only in the exonic regions between mMCP-8 and related genes.
- No conservation was observed in the promoter region or introns, indicating rapid evolution of the regulatory region.
- Intron and exon sizes were conserved between mMCP-8 and T-cell granzymes/cathepsin G.
Conclusions:
- mMCP-8 represents a new group of mast cell/basophil proteases with unique evolutionary characteristics.
- The upstream regulatory region of mMCP-8 has evolved rapidly, primarily through single base substitutions or small indels, rather than major structural changes.
