Pejler, Gunnar
- Department of Molecular Biosciences, Swedish University of Agricultural Sciences
Abstract
To gain insight into the biological role of mast cell chymase we have generated a mouse strain with a targeted deletion in the gene for mast cell protease 4 (mMCP-4), the mouse chymase that has the closest relationship to the human chymase in terms of tissue localization and functional properties. The inactivation of mMCP-4 did not affect the storage of other mast cell proteases and did not affect the number of mast cells or the mast cell morphology. However, mMCP-4 inactivation resulted in complete loss of chymotryptic activity in the peritoneum and in ear tissue, indicating that mMCP-4 is the main source of stored chymotrypsin-like protease activity at these sites. The mMCP-4 null cells showed markedly impaired ability to perform inactivating cleavages of thrombin, indicating a role for mMCP-4 in regulating the extravascular coagulation system. Further, a role for mMCP-4 in connective tissue remodeling was suggested by the inability of mMCP-4 null peritonealcells to process endogenous fibronectin
Published in
Journal of Experimental Medicine
2003, volume: 198, number: 3, pages: 423-431
Publisher: ROCKEFELLER UNIV PRESS
SLU Authors
Åbrink, Magnus
- Department of Molecular Biosciences, Swedish University of Agricultural Sciences
- Department of Molecular Biosciences, Swedish University of Agricultural Sciences
UKÄ Subject classification
Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1084/jem.20030671
Permanent link to this page (URI)
https://res.slu.se/id/publ/1090