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Cited by 265

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Galectin-3 Is a Novel Substrate for Human Matrix Metalloproteinases-2 and -9

Ochieng, Josiah, Fridman, Rafael, Nangia-Makker, Pratima, Kleiner, David E., Liotta, Lance A., Stetler-Stevenson, William G., Raz, Avraham·1994·Biochemistry

Abstract

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.

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Metadata

Authors
Ochieng, J., Fridman, R., Nangia-Makker, P., Kleiner, D. E., Liotta, L. A., Stetler-Stevenson, W. G., & Raz, A.
Venue
Biochemistry
Published
1994-11-01
Volume
33
Issue
47
Pages
14109-14114
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W1985965035
Cited by
265
References
1
FWCI
2.01
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Galectin-3 Is a Novel Substrate for Human Matrix Metalloproteinases-2 and -9. https://app.cochat.ai/papers/10.1021/bi00251a020
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Ochieng, J., Fridman, R., Nangia-Makker, P., Kleiner, D. E., Liotta, L. A., Stetler-Stevenson, W. G., & Raz, A. (1994). Galectin-3 Is a Novel Substrate for Human Matrix Metalloproteinases-2 and -9. Biochemistry. https://doi.org/10.1021/bi00251a020

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