N-Myristoyltransferase overexpression in human colorectal adenocarcinomas.

Full Abstract

Modification of proteins by myristoylation has been proposed as a chemotherapeutic target against colon cancer because it is important in the function of various signal transduction proteins. Recently we reported that the enzyme that catalyzes this modification, N-myristoyltransferase (NMT), is elevated in colorectal adenocarcinomas [Magnuson, B. A., Raju, R. V. S., Moyana, T. N., and Sharma, R. K. (1995) J. Natl. Cancer. Inst. 87, 1630-1635]. The purpose of the present study was to investigate whether the elevated activity of NMT in colorectal adenocarcinomas is due to an increase in the production of NMT or a change in the structure of the preexisting enzyme. The expression of NMT in normal colonic mucosa and adenocarcinomas from human colorectal surgical specimens was studied by immunoblotting, and its localization was confirmed by immunohistochemistry. The molecular weight of NMT was determined by fast protein liquid chromatography. In both normal mucosa and colorectal adenocarcinomas, NMT with a molecular mass of 48.5 kDa was identified with anti-human NMT and anti-peptide antibody. However, the expression of NMT was found to be higher in the colorectal tumors. This finding was further confirmed by immunohistochemical studies which showed stronger cytoplasmic staining in the tumors. These findings represent the first description of NMT overexpression in colorectal adenocarcinomas. This has implications with regard to (i) the design of chemotherapeutic drugs and (ii) prognosis, for instance, in monitoring colorectal cancer recurrence or metastases.

Author information

Author/s: Raju, R V (RV); Moyana, T N (TN); Sharma, R K (RK);

Affiliation: Saskatoon Cancer Centre, University of Saskatchewan, Saskatoon, Saskatchewan, S7N 4H4, Canada.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Experimental cell research (Exp Cell Res), published in UNITED STATES. (Language: eng)

Reference: 1997-Aug; vol 235 (issue 1) : pp 145-54

Dates: Created 1997/09/30; Completed 1997/09/30; Revised 2006/11/15;

PMID: 9281363, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Acyltransferases - analysis; biosynthesis; chemistry
Adenocarcinoma - enzymology; pathology; surgery
Amino Acid Sequence
Antibodies - isolation & purification
Chromatography, Affinity
Cloning, Molecular
Colon - enzymology; pathology
Colorectal Neoplasms - enzymology; pathology; surgery
Escherichia coli

Associated Chemicals: Antibodies (0) ; Peptide Fragments (0) ; Recombinant Proteins (0) ; Acyltransferases (EC 2.3.-) ; glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97)

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