TY - JOUR
AU - Raz, A
AB - The primary structure of galectin-3, a approximately 30 kDa galactoside-binding protein (aka CBP-35, mL-34, hL-31, L-29, Mac-2, and epsilon BP), reveals two structural domains: an amino-terminal domain consists of a Pro-Gly-rich motif, and a globular carboxyl-terminal domain containing a carbohydrate-binding site. In this study, we report that the amino-terminal domain of galectin-3 contains a cleavage site for two members of the matrix metalloproteinase family of enzymes: the 72 kDa (gelatinase A, MMP-2) and the 92 kDa (gelatinase B, MMP-9) proteinases. The major cleavage site for the gelatinases in galectin-3 is at the Ala62-Tyr63 bond, and its hydrolysis by these enzymes was inhibited by TIMP-2. Cell-surface expression of galectin-3 was reduced following treatment of viable T47D human breast carcinoma cells with gelatinase A. These results suggest that galectin-3 may be a substrate for gelatinases and that its degradation may play a role in modulating the biological activities of galectin-3.
TI - Galectin-3 is a novel substrate for human matrix metalloproteinases-2 and -9.
JF - Biochemistry
DO - 10.1021/bi00251a020
DA - 1994-12-28
UR - https://www.deepdyve.com/lp/pubmed/galectin-3-is-a-novel-substrate-for-human-matrix-metalloproteinases-2-CKD25BdPg3
SP - 14109
EP - 14
VL - 33
IS - 47
DP - DeepDyve
ER -