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J. Biol. Chem., Vol. 277, Issue 33, 29999-30009, August 16, 2002
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From the Interdisciplinary Concentration in Animal
Molecular & Cell Biology and the Department of Animal Sciences,
University of Florida, Gainesville, Florida 32611-0910
Secretory leukocyte protease inhibitor (SLPI)
inhibits chymotrypsin, trypsin, elastase, and cathepsin G. This protein
also exhibits proliferative effects, although little is known about the
molecular mechanisms underlying this activity. We have generated SLPI-ablated epithelial sublines by stably transfecting the Ishikawa human endometrial cell line with an antisense human SLPI RNA expression vector. We demonstrate a positive correlation between cellular SLPI
production and proliferation. We further show that Ishikawa sublines
expressing low to undetectable SLPI have correspondingly increased and
decreased expression, respectively, of transforming growth factor-
Secretory Leukocyte Protease Inhibitor Mediates
Proliferation of Human Endometrial Epithelial Cells by Positive and
Negative Regulation of Growth-associated Genes*
1
and cyclin D1 genes, relative to parental cells. SLPI selectively
increased cyclin D1 gene expression, with the effect occurring in part
at the level of promoter activity. Cellular SLPI levels negatively
influenced the anti-proliferative and pro-apoptotic insulin-like
growth factor-binding protein-3 expression. We also identified lysyl
oxidase, a phenotypic inhibitor of the ras oncogenic pathway and a tumor suppressor, as SLPI-repressed gene, whose expression is up-regulated by transforming growth factor-1. Our results suggest that SLPI acts at the node(s) of at least three major
interacting growth inhibitory pathways. Because expression of SLPI is
generally high in epithelial cells exhibiting abnormal proliferation
such as in carcinomas, SLPI may define a novel pathway by which
cellular growth is modulated.
*
This work was supported by National Institutes of Health
Grant HD21961 and the Florida Agricultural Experiment Station
(Publication Series No. R-08764).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Arkansas Children's
Nutrition Center, Arkansas Children's Hospital Research Institute and
Department of Physiology & Biophysics, University of Arkansas for
Medical Sciences, Slot 512-20B, 1120 Marshall St., Little Rock, AR
72202. Tel.: 501-320-2859; Fax: 501-320-3161; E-mail: simmenfranka@uams.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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