Disease relevance of Mcpt2

• A novel 28,000 Mr serine protease, designated mouse mast cell protease-2 (MMCP-2), that is stored in the secretory granules of Kirsten sarcoma virus-immortalized mouse mast cells (KiSV-MC) has been identified and its NH2-terminal amino acid sequence has been determined [1].

High impact information on Mcpt2

• Cultured mast cells of WBB6F1(-)+/+ mice that expressed MMCP-2 mRNA were transplanted into the stomach wall of genetically mast-cell-deficient WBB6F1(-)W/Wv mice [2].
• Mast cells that appeared in the mucosa expressed the MMCP-2 mRNA, but mast cells that appeared in the muscularis propria did not, indicating the adaptation of cultured mast cells into a new environment [2].
• A significant amount of MMCP-2 mRNA was not expressed in the skin of all +/+, Wv/Wv and mi/mi mice [3].
• After affinity purification, this antibody, anti-mMCP-2(56-71) IgG, reacted in SDS-PAGE/immunoblots against a 28-kDa protein in BMMCW+IL-10 that had the N-terminal amino acid sequence of mMCP-2 [4].
• Reversible expression of mouse mast cell protease 2 mRNA and protein in cultured mast cells exposed to IL-10 [4].

Biological context of Mcpt2

• DNA blot analysis using the full-length MMCP-2 cDNA indicated the existence of a family of highly related serine protease genes in the mouse genome [1].
• The fact that the steady-state levels of mMCP-2 mRNA and protein in BMMC can both be reversibly altered by culturing these mast cells in the presence and absence of rIL-10 suggests that the phenotype of mast cells is not fixed [4].

Anatomical context of Mcpt2

• The MMCP-2 mRNA remained to be expressed after the settlement in either the mucosa or the muscularis propria [2].
• BALB/cJ mouse mast cells derived by culturing bone marrow progenitor cells in WEHI-3 cell-conditioned medium (BMMCW) do not contain mouse mast cell protease 2 (mMCP-2) mRNA, but these cells can be induced to express this transcript after exposure to rIL-10 [4].

Other interactions of Mcpt2

• Moreover, we show that in the rat, the Mcpt8-family diversified relatively recently together with sequences related to the beta-chymase Mcpt2 [5].
• The amino acid identity was of 74% with RMCP2, and of 76%, 65% and 90% with the mouse proteases MMCP1, MMCP2 and MMCP4, respectively [6].
• They included four proteases (mouse mast cell protease 2, granzyme B, pepsinogen F and serine protease 1) and two metabolic enzymes (adenine phosphoribosyltransferase and fructose1,6-bisphosphatase) [7].

References