[HTML][HTML] Thrombospondin type 1 repeats interact with matrix metalloproteinase 2: regulation of metalloproteinase activity
K Bein, M Simons - Journal of Biological Chemistry, 2000 - ASBMB
Thrombospondins are thought to function as inhibitors of angiogenesis. However, the
mechanism (s) of this activity is not well understood. In this study, we have used the yeast
two-hybrid system to identify proteins that interact with the thrombospondins 1 (TSP1) and 2
(TSP2) properdin-like type 1 repeats (TSR). One of the proteins identified that interacted with
both TSR was matrix metalloproteinase 2 (MMP2). The isolated MMP2 cDNA clone encoded
amino acid residues 237–633, which include the fibronectin-like gelatin binding region …
mechanism (s) of this activity is not well understood. In this study, we have used the yeast
two-hybrid system to identify proteins that interact with the thrombospondins 1 (TSP1) and 2
(TSP2) properdin-like type 1 repeats (TSR). One of the proteins identified that interacted with
both TSR was matrix metalloproteinase 2 (MMP2). The isolated MMP2 cDNA clone encoded
amino acid residues 237–633, which include the fibronectin-like gelatin binding region …