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Am J Physiol Cell Physiol 274: C1363-C1372, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 5, C1363-C1372, May 1998

Dying enterocytes downregulate signaling pathways converging on Ras: rescue by protease inhibition

Lawrence A. Scheving1, Wen-Hui Jin1, Kang-Mei Chong1, Wendi Gardner1, and Frederick O. Cope2

1 Division of Gastroenterology and Nutrition, Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232; and 2 Neoprobe Corporation, Columbus, Ohio 43017

Organ and cell cultures of the small intestine serve as excellent in vitro models for programmed cell death (PCD). Cells cultured in serum-free, minimal medium rapidly died, as evidenced by histological changes, internucleosomal DNA cleavage, and TdT-mediated dUTP nick end labeling. Cell death was pervasive, although nonepithelial cells within the fibrovascular villus core were spared. PCD did not require a functional p53 gene. Serine and cysteine protease inhibitors, but not FCS, suppressed it. Relative to structural and functional proteins, dying enterocytes rapidly downregulated Ras-convergent proteins, including epidermal growth factor receptor, Erb-B2, and the son of sevenless guanine nucleotide exchangers. Reductions in the steady-state levels of both protein and mRNA were observed. These reductions were prevented by a combination of death-defying serine and caspase inhibitors, indicating a requirement for the initiation of death. Thus, during catastrophic PCD, intestinal epithelial cells delete cell surface signaling pathways responsible for Ras activation.

epidermal growth factor receptor; son of sevenless guanine nucleotide exchangers; Erb-B2; caspases; serine proteases


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