Author:
Stratmann Bernd,Farr Martin,Tschesche Harald
Abstract
Abstract
The tight regulation of extracellular matrix remodeling
and degradation is of great importance in physiological
processes like development and morphogenesis,
as well as in pathological situations like tumor
invasion and metastasis. Tissue inhibitors of metalloproteinases (TIMPs) are the naturally occuring inhibitors of matrix metalloproteinases, which are involved
in matrix turnover.
In this report we describe the cloning of human
TIMP-4 from a human adenocarcinoma and an osteosarcoma cell line and the expression of the inhibitory domain in the methylotrophic yeast Pichia
pastoris. The inhibition of MMP-8, -9, -12, -13 and -14
by the Nterminal domain of TIMP-4 was analysed.
Using a fluorescent MCApeptide, K values for each
subclass of MMPs were determined. With dissociation
constants in the nanomolar range, TIMP-4 seems
to be a good inhibitor for all classes of MMPs without
remarkable preference for special MMPs.
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Cited by
19 articles.
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