Pejler, Gunnar
- Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences
Abstract
Rat mast cell protease 1 (RMCP-1) is a chymotrypsin-like serine protease specifically expressed by connective tissue-type mast cells. The enzyme is stored in the secretory granules in a macromolecular complex with heparin proteoglycan. In the present investigation it was shown that RMCP-1 is inhibited by vitronectin (VN), an RGD-containing adhesive glycoprotein with heparin-binding properties. RMCP-1 that had been separated from heparin proteoglycan was less susceptible to inhibition than RMCP-1 present in complex with heparin proteoglycan. Pre-incubation of VN with purified heparin partially blocked the RMCP-1 inhibiting activity of VN. Plasma VN had negligible RMCP-1-inhibiting activity. However, heat treatment of plasma VN, which is known to expose the heparin-binding domain, induced RMCP-1-inhibiting activity. Affinity chromatography on immobilized VN showed that RMCP-1 bound with high affinity to VN. The binding of RMCP-1 to VN was not heparin-dependent since free RMCP-1 bound with equal affinity to the immobilized VN as RMCP-1 present in complex with heparin. The inhibition of RMCP-1 by VN was shown to be reversible.
Keywords
VITRONECTIN; MAST CELL; SERINE PROTEASE; CHYMASE; HEPARIN; HEPARIN-BINDING SITE
Published in
FEBS Letters
1994, volume: 346, number: 2-3, pages: 189-193
Publisher: ELSEVIER SCIENCE BV
SLU Authors
UKÄ Subject classification
Cell and Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1016/0014-5793(94)00465-X
Permanent link to this page (URI)
https://res.slu.se/id/publ/52787