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Metalloproteinase inhibition and erythroid potentiation are independent
activities of tissue inhibitor of metalloproteinases-1
L Chesler, DW Golde, N Bersch and MD Johnson
Department of Pathology, Northwestern University Medical School, Chicago,
IL 60611, USA.
Tissue inhibitor of metalloproteinases-1 (TIMP-1), the major physiological
matrix metalloproteinase inhibitor and a potent antimetastatic factor, also
stimulates the growth of erythroid progenitors (erythroid-potentiating
activity). We analyzed the relationship between the growth factor activity
and protease inhibition by preparing purified TIMP-1 "knockout" proteins
lacking in vitro antiproteolytic activity. The growth-stimulatory effect of
these N- terminal TIMP-1 point mutants, as tested in an in vitro assay
using erythroid precursors (erythroid burst-forming units) was equal to
that of unmutated TIMP-1. A fully antiproteolytic C-terminal TIMP-1
truncation also stimulated growth in the erythroid burst-forming unit
assay. The results indicate that the influence of TIMP-1 on erythroid
precursor growth is independent of its ability to inhibit
metalloproteinases. TIMP-1 is analogous to proteins that have both
proteolytic and growth factor activity, such as plasmin, thrombin, and
urokinase. However, TIMP-1 is novel in this regard because it is a
metalloproteinase inhibitor. We show that the antiproteolytic and growth
factor activities of the TIMP-1 molecule are physically and functionally
distinct.
Volume 86,
Issue 12,
pp. 4506-4515,
12/15/1995
Copyright © 1995 by The American Society of Hematology
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