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J Biol Chem, Vol. 275, Issue 5, 3328-3334, February 4, 2000
From the A potential target of hormone action during
prostate and mammary involution is the intercellular junction of
adjacent secretory epithelium. This is supported by the long-standing
observation that one of the first visible stages of prostate and
mammary involution is the disruption of interepithelial adhesion prior
to the onset of apoptosis. In a previous study addressing this aspect
of involution, we acquired compelling evidence indicating that the
disruption of E-cadherin-dependent adhesion initiates
apoptotic programs during prostate and mammary involution. In cultured
prostate and mammary epithelial cells, inhibition of
E-cadherin-dependent aggregation resulted in cell death
following apoptotic stimuli. Loss of cell-cell adhesion in the
nonaggregated population appeared to result from the rapid truncation
within the cytosolic domain of the mature, 120-kDa species of
E-cadherin (E-cad120). Immunoprecipitations from cell
culture and involuting mammary gland demonstrated that this truncation
removed the
Truncation of the
-Catenin Binding Domain of E-cadherin
Precedes Epithelial Apoptosis during Prostate and Mammary
Involution*
§,§¶,¶,,
,¶
Department of Surgery, Division of Urology,
the Department of Pathology and the ¶ University of
Michigan Comprehensive Cancer Center, University of Michigan Ann Arbor,
Ann Arbor, Michigan 48109, and the ** Department of Biology,
University of Toledo, Toledo Ohio 43606
-catenin binding domain from the cytoplasmic tail of
E-cadherin, resulting in a non--catenin binding, membrane-bound
97-kDa species (E-cad97) and a free cytoplasmic 35-kDa form
(E-cad35) that is bound to -catenin. Examination of
E-cadherin expression and cellular distribution during prostate and
mammary involution revealed a dramatic reduction in junctional membrane
staining that correlated with a similar reduction in
E-cad120 and accumulation of E-cad97 and
E-cad35. The observation that E-cadherin was truncated
during involution suggested that hormone depletion activated the same
apoptotic pathway in vivo as observed in vitro.
Based on these findings, we hypothesize that truncation of E-cadherin
results in the loss of -catenin binding and cellular dissociation
that may signal epithelial apoptosis during prostate and mammary
involution. Thus, E-cadherin may be central to homeostatic regulation
in these tissues by coordinating adhesion-dependent
survival and dissociation-induced apoptosis.
*
This study was supported by the SPORE in Prostate Cancer P50
CA69568 (to M. L. D.) from the National Institutes of Health and by
Grant TPRN-98-111-01 CSM from the American Cancer Society (to
M. L. D.).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: Box 0944, Rm. 6219 CGC, 1500 E. Medical Center Dr., Ann Arbor, MI 48109. Tel.: (734) 647-8121; Fax: (734) 647-9271; E-mail: mday@umich.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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