SP220K is a novel matrix serine proteinase

✍ Scribed by Sabine Thaon; Patrick Auberger; Bernard Rossi; Claudine Poustis-Delpont

• Book ID: 101236162
• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: French
• Weight: 149 KB
• Volume: 77
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/(sici)1097-0215(19980717)77:2<264::aid-ijc16>3.0.co;2-b

✦ Synopsis

Matrix proteinases play a critical role in extracellular matrix remodeling, which is particularly involved in cancer invasion and metastasis. We have previously characterized and purified a new tetrameric serine proteinase (SP220K) from human kidney clear cell carcinoma plasma membranes. Here, we report that SP220K exhibits gelatinase activity as assessed both in solution and by zymography. Optimum gelatinase activity ranges between pH 7.5 to pH 9.0. Fibronectin and type I collagen were hydrolyzed by SP220K, at variance with laminin and type IV collagen. Like other trypsin-like fibronectin degrading proteinases, SP220K released the 29-kDa N-terminal heparin-binding domain of fibronectin. By using a panel of proteinase inhibitors, we found that the inhibition profile of SP220K was different from that of other known serine proteinases such as thrombin, trypsin, plasmin, plasminogen activators and tryptase. Altogether, our results indicate that SP220K corresponds to a novel matrix proteinase that exhibits a marked specificity for fibronectin and type I collagen. Int.