Jump to main content
Jump to site search

Issue 5, 2017
Previous Article Next Article

New tricks for human farnesyltransferase inhibitor: cancer and beyond

Author affiliations

Abstract

Human protein farnesyltransferase (FTase) catalyzes the addition of a C15-farnesyl lipid group to the cysteine residue located in the COOH-terminal tetrapeptide motif of a variety of important substrate proteins, including well-known Ras protein superfamily. The farnesylation of Ras protein is required both for its normal physiological function, and for the transforming capacity of its oncogenic mutants. Over the last several decades, FTase inhibitors (FTIs) were developed to disrupt the farnesylation of oncogenic Ras as anti-cancer agents, and some of them have entered cancer clinical investigation. On the other hand, some substrates of FTase were demonstrated to be related with other human diseases, including Hutchinson–Gilford progeria syndrome, chronic hepatitis D, and cardiovascular diseases. In this review, we summarize the roles of FTase in malignant transformation, proliferation, apoptosis, angiogenesis, and metastasis of tumor cells, and the recently anticancer clinical research advances of FTIs. The therapeutic prospect of FTIs on several other human diseases is also discussed.

Graphical abstract: New tricks for human farnesyltransferase inhibitor: cancer and beyond

Back to tab navigation
Please wait while Download options loads

Publication details

The article was received on 18 Jan 2017, accepted on 15 Feb 2017 and first published on 16 Feb 2017


Article type: Review Article
DOI: 10.1039/C7MD00030H
Citation: Med. Chem. Commun., 2017,8, 841-854
  •   Request permissions

    New tricks for human farnesyltransferase inhibitor: cancer and beyond

    J. Wang, X. Yao and J. Huang, Med. Chem. Commun., 2017, 8, 841
    DOI: 10.1039/C7MD00030H

Search articles by author