Mini-review. Inhibition of Ras prenylation: a signaling target for novel anti-cancer drug design

Authors: Lerner E.; Hamilton A.¹; Sebti S.²

Source: Anti-Cancer Drug Design, Volume 12, Number 4, 1997 , pp. 229-238(10)

Publisher: Cognizant Communication Corporation

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Abstract:

The cancer-causing activity of Ras requires the prenylation of a cysteine fourth from its carboxyl terminus. Rational design of peptidomimetics of the carboxyl terminal tetrapeptide prenylation site on Ras resulted in pharmacological agents capable of inhibiting Ras processing, selectively antagonizing oncogenic signaling and suppressing human tumor growth in mouse models without side effects. This mini-review describes the efforts of several groups to design, synthesize and evaluate the biological activities of farnesyltransferase and geranylgeranyltransferase I inhibitors. Among the important issues that will be discussed are the mechanism of action of these inhibitors and the potential mechanisms of resistance to inhibition of K-Ras farnesylation.

Document Type: Research article

Affiliations: 1: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15261, USA 2: Corresponding authors

Publication date: 1997-06-01