Lack of expression of the tryptase mouse mast cell protease 7 in mast cells of the C57BL/6J mouse

Namit Ghildyal*, Daniel S. Friend, Rachel Freelund, K. Frank Austen, H. Patrick McNeil, Vera Schiller, Richard L. Stevens

*Corresponding author for this work

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Although the steady-state level of the mouse mast cell protease (mMCP) 7 transcript is below detection in the serosal and mucosal mast cells of the BALB/cJ mouse, the IL-3-dependent, bone marrow-derived mast cells (mBMMC) of this strain and four other strains contain a high steady-state level of the mMCP-7 transcript. To further analyze the expression of this mast cell tryptase, a mMCP-7-specific IgG was obtained by immunizing a rabbit with a 19-residue synthetic peptide that corresponds to its unique amino acid sequence at residues 160 to 178 (anti-mMCP-7((160-178)). In a SDS- PAGE/immunoblot analysis of lysates of BALB/cJ mBMMC, anti-mMCP-7((160- 178)), IgG recognized a diffuse 31- to 36-kDa protein, which shifted to a sharp 27-kDa protein after treatment with N-glycanase. As assessed immunohistochemically, mMCP-7 protein is present not only in the secretory granules of BALB/cJ mBMMC, but also in the ear mast cells of this strain. In contrast, the ear mast cells of the C57BL/6J mouse do not contain detectable levels of mMCP-7 protein, although the ear mast cells of both mouse strains contain mMCP-5 protein. Because mMCP-7 mRNA and protein also were not detected in mBMMC from the C57BL/6J mouse, the failure of the ear mast cells of this strain to express mMCP-7 is most likely a consequence of an intrinsic abnormality in the mast cell-committed progenitor cells themselves, or in the bone marrow microenvironment that induces its mast cell progenitor cells to express this tryptase.

Original languageEnglish
Pages (from-to)2624-2630
Number of pages7
JournalJournal of Immunology
Volume153
Issue number6
Publication statusPublished - 15 Sep 1994
Externally publishedYes

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