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Constitutive expression of mouse mast cell protease‐1 in normal BALB/c mice and its up‐regulation during intestinal nematode infection
Author(s) -
WASTLING J. M.,
SCUDAMORE C. L.,
THORNTON E. M.,
NEWLANDS G. F. J.,
MILLER H. R. P.
Publication year - 1997
Publication title -
immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.297
H-Index - 133
eISSN - 1365-2567
pISSN - 0019-2805
DOI - 10.1046/j.1365-2567.1997.00155.x
Subject(s) - biology , jejunum , mast cell , microbiology and biotechnology , proteases , secretion , endocrinology , medicine , immunology , enzyme , biochemistry
Rodent intestinal mucosal mast cells (IMMC) store and secrete soluble granule serine proteases, the β ‐chymases, which may promote epithelial permeability during intestinal hypersensitivity reactions. The β ‐chymase mouse mast cell protease‐1 (mMCP‐1) is generally considered to be expressed late in the in vitro differentiation of mast cells. The purpose of this study was to determine the kinetics of mMCP‐1 transcription and expression in vivo during nematode‐induced IMMC hyperplasia. Concentrations of mMCP‐1 in blood and jejunum of BALB/c mice were quantified by enzyme‐linked immunosorbent assay before and at various stages after infection with the intestinal nematode Nippostrongylus brasiliensis . Mature mMCP‐1 enzyme was detected in jejunal homogenate (194 ng/mg soluble protein) and in blood (8·3 ng/ml serum) from normal uninfected BALB/c mice. Maximal IMMC hyperplasia occurred 7–14 days post infection and was significantly correlated with increased levels of mMCP‐1 in jejunum ( r =0·58, P <0·001) and with raised concentrations of mMCP‐1 in serum ( r =0·66, P <0·001). Transcription of the mMCP‐1 gene was detected by RNA blotting in normal, uninfected jejunum, but transcription was up‐regulated after infection with maximal transcription occurring on days 7 and 14. In conclusion, mMCP‐1 transcription, storage and secretion occur constitutively in normal BALB/c jejunum but this basal secretion is up‐regulated during nematode infection, suggesting both a physiological and pathological function for this protease.