Sammanfattning

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

Publicerad i

Journal of Experimental Medicine
2003, Volym: 198, nummer: 3, sidor: 423-431
Utgivare: ROCKEFELLER UNIV PRESS

SLU författare

• Pejler, Gunnar

  • Institutionen för molekylär biovetenskap, Sveriges lantbruksuniversitet
    

• Åbrink, Magnus

  • Institutionen för molekylär biovetenskap, Sveriges lantbruksuniversitet
    

Publikationens identifierare

DOI: https://doi.org/10.1084/jem.20030671

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/1090