TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 275, No. 34, Issue of August 25, pp. 26411–26415, 2000 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Received for publication, February 11, 2000, and in revised form, May 18, 2000 Published, JBC Papers in Press, May 25, 2000, DOI 10.1074/jbc.M001270200 Zhiping Wang, Ruth Juttermann, and Paul D. Soloway‡ From the Roswell Park Cancer Institute, Department of Molecular and Cellular Biology, Buffalo, New York 16263 Matrix metalloproteinases (MMPs) are synthesized as teinase inhibitor a -macroglobulin (18) and by four known latent proenzymes. A proteolytic cleavage event involv- MMP-specific tissue inhibitors of metalloproteinases or TIMPs ing processing of the cysteine-rich N-terminal propep- (19 –22). The mechanisms by which MMPs are proteolytically tide is required for their full activation. Previous in processed from their latent to their activated forms and how vitro studies indicated that activation of proMMP-2 can they are regulated by inhibitors are important to understand- occur through formation of a trimolecular complex be- ing their contributions to normal developmental and patholog- tween MMP-14, TIMP-2, and proMMP-2 at the cell sur- ical processes. face. Using TIMP-2-deficient mice and cells derived from Evidence exists for several mechanisms 
TI - TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m001270200
DA - 2000-08-01
UR - https://www.deepdyve.com/lp/unpaywall/timp-2-is-required-for-efficient-activation-of-prommp-2-in-vivo-Bi78aZQgTQ
DP - DeepDyve
ER -