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Volume 272, Number 13, Issue of March 28, 1997 pp. 8125-8128
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Cell Anchorage Regulates Apoptosis through the Retinoblastoma Tumor Suppressor/E2F Pathway

(Received for publication, December 24, 1996, and in revised form, January 21, 1997)

Mark L. Day Dagger , Rosalinda G. Foster , Kathleen C. Day Dagger , Xin Zhao Dagger , Peter Humphrey ** , Paul Swanson ** , Antonio A. Postigo Dagger Dagger , Steven H. Zhang Dagger Dagger and Douglas C. Dean Dagger Dagger

From the Dagger  Department of Surgery, Division of Urology, and the University of Michigan Comprehensive Cancer Center, University of Michigan, Ann Arbor, Michigan 48109, the Dagger Dagger  Department of Medicine and Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110, and the ** Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110

Epithelial cells are dependent upon adhesion to extracellular matrix for survival. We show that loss of beta 1 integrin receptor contact with extracellular matrix signals the inhibition of G1 cyclin-dependent kinase activity. This loss of cyclin-dependent kinase activity leads to accumulation of the hypophosphorylated (active) form of the retinoblastoma tumor suppressor protein (Rb). We present evidence that in epithelial cells deprived of matrix contact, the growth suppression signal elicited by hypophosphorylated Rb opposes stimulatory signals from serum growth factors, leading to a cell cycle conflict that triggers apoptosis. This apoptotic pathway is modulated by Bcl-2 through a novel mechanism that regulates Rb phosphorylation. We present evidence that the Rb-dependent apoptotic pathway functions in vivo in the apoptosis of the prostate glandular epithelium following castration.


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