Key:ODUOJXZPIYUATO-UHFFFAOYSA-N N N Y Racecadotril, also known as acetorphan, is an drug which acts as a peripherally acting. Unlike other medications used to treat diarrhea, which, racecadotril has an effect—it reduces the secretion of water and into the intestine. It is available in (where it was first introduced in ~1990) and other European countries (including,, the,, and the ) as well as most of South America and some countries (including, and ), but not in the United States. It is sold under the tradenames Hidrasec or, in France, Tiorfan. In Italy it is sold under the tradename Tiorfix. In India it's available as Redotril. Is the active metabolite of racecadotril, which exerts the bulk of its inhibitory actions on enkephalinase.

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Apr 19, 2002  Bax and Bak Independently Promote Cytochrome cRelease from Mitochondria* Kurt Degenhardt. Your IP Address has been logged. Your Installation Location has been logged.

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Contents • • • • Pharmacokinetics [ ] Racecadotril is rapidly absorbed after oral administration and doses of 30 mg, 100 mg and 300 mg reached Cmax within 60 min. Food does not affect bioavailability of racecadotril. Racecadotril is rapidly and effectively metabolized to the active metabolite thiorphan which inhibits enkephainase enzyme and exhibits anti-secretory effect. Medical uses [ ] Racecadotril can be used for treatment of acute diarrhea patients and has better tolerability than loperamide. Several guidelines have recommended racecadotril use in addition to oral rehydration treatment in children with acute diarrhea. See also [ ] •, the ( S)-enantiomer of racecadotril • • References [ ].

• Agonists (abridged; see for a full list): • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • () • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • PAMs: • • Antagonists: • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • Unknown/unsorted: • • • • •.

Abstract Pro-apoptotic Bax and Bak have been implicated in the regulation of p53-dependent apoptosis. We assessed the ability of primary baby mouse kidney (BMK) epithelial cells from bax −/−, bak −/−, and bax −/− bak −/− mice to be transformed by E1A alone or in conjunction with dominant-negative p53 (p53DD). Although E1A alone transformed BMK cells from p53-deficient mice, E1A alone did not transform BMK cells from bax −/−, bak −/−, or bax −/− bak −/− mice. Thus, the loss of both Bax and Bak was not sufficient to relieve p53-dependent suppression of transformation in epithelial cells. To test the requirement for Bax and Bak in other death signaling pathways, stable E1A plus p53DD-transformed BMK cell lines were derived from the bax −/−, bak −/−, and bax −/− bak −/− mice and characterized for their response to tumor necrosis factor-α (TNF-α)-mediated apoptosis.

The loss of both Bax and Bak severely impaired TNF-α-mediated apoptosis, but the presence of either Bax or Bak alone was sufficient for cell death. Cytochrome c was released from mitochondria, and caspase-9 was activated in Bax- or Bak-deficient cells in response to TNF-α but not in cells deficient in both. Thus, either Bax or Bak is required for death signaling through mitochondria in response to TNF-α, but both are dispensable for p53-dependent transformation inhibition. Apoptosis can be initiated in transformed cells by an intrinsic mechanism when deregulation of the cell cycle initiates an apoptotic response mediated by the tumor suppressor p53. Apoptosis can also be initiated by an extrinsic mechanism when TNF-α 1 or Fas ligand initiates an apoptotic response mediated by death receptors.

When the adenovirus E1A oncogene stimulates proliferation during transformation, the cellular response is apoptosis mediated by p53 (,). Activation of p53 results in altered transcription of a wide variety of genes that are involved in many facets of cell metabolism, cell cycle regulation, and apoptosis (, ). Genes transcriptionally up-regulated by p53 that have been implicated in promoting apoptosis include the Bcl-2 family members bax, bak, puma, and noxa (). Evidence suggests that Bax and Bak function is required for the release of cytochrome c from the mitochondria to the cytosol during apoptosis (, ). Cytochrome c release from the mitochondria occurs in many apoptotic signaling pathways including those implemented by p53 and TNF-α ().