Quantitative Analysis of the Expression of Human N-myristoyltransferase 1 (hNMT-1) in Cancers



Lifeng Chen, Binbing Ling, Jane Alcorn, Jian Yang*
College of Pharmacy and Nutrition, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada


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© 2009 Chen et al.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the College of Pharmacy and Nutrition, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada; Tel: 306-966-6361; Fax: 306-966-6377; E-mail: jian.yang@usask.ca


Abstract

Human N-myristoyltransferase 1 (hNMT-1) catalyzes the covalent attachment of myristic acid to N-terminal glycine residues (myristoylation) of numerous protein substrates. Overexpression of hNMT-1 in colorectal and gallbladder cancers makes it a potential biomarker and drug design target for such cancers. In this study, we investigated hNMT-1 expression during the progression of eight different human cancers using quantitative RT-PCR. The study results showed that hNMT-1 was up-regulated in breast, colon, lung and ovarian cancers but not kidney, liver, prostate and thyroid cancers. This suggests a role for hNMT-1 as a biomarker for detection of breast, colon, lung and ovarian cancers. This study also suggests the available hNMT-1 inhibitors may be potential therapeutic agents against breast and lung cancers through all disease stages, although their use would likely be limited to early stage colon and ovarian cancers.