Pejler, Gunnar
- Institutionen för veterinärmedicinsk kemi, Sveriges lantbruksuniversitet
Sammanfattning
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.
Nyckelord
VITRONECTIN; MAST CELL; SERINE PROTEASE; CHYMASE; HEPARIN; HEPARIN-BINDING SITE
Publicerad i
FEBS Letters
1994, volym: 346, nummer: 2-3, sidor: 189-193
Utgivare: ELSEVIER SCIENCE BV
SLU författare
UKÄ forskningsämne
Cell- och molekylärbiologi
Publikationens identifierare
- DOI: https://doi.org/10.1016/0014-5793(94)00465-X
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/52787