Loss of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 and Reduced O-glycosylation in Colon Carcinoma Cells Selected for Hepatic Metastasis

Overview

Journal Glycoconj J

Publisher Springer

Specialties Biochemistry
Endocrinology

Date 2010 Jan 16

PMID 20077002

Citations 11

Authors

Kentaro Kato

Hideyuki Takeuchi

Akira Kanoh

Naoki Miyahara

Yoko Nemoto-Sasaki

Megumi Morimoto-Tomita

Azusa Matsubara

Yoshimi Ohashi

Michihiko Waki

Katsuaki Usami

Ulla Mandel

Henrik Clausen

Nobuaki Higashi

Tatsuro Irimura

Affiliations

Soon will be listed here.

Abstract

O-glycosylation of mucin is initiated by the attachment of N-acetyl-D-galactosamine (GalNAc) to serine or threonine residues in mucin core polypeptides by UDPGalNAc:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts). It is not well understood how GalNAc attachment is regulated by multiple ppGalNAc-Ts in each cell. In the present study, the expression levels of murine ppGalNAc-Ts (mGalNAc-Ts), T1, T2, T3, T4, T6, and T7 were compared between mouse colon carcinoma colon 38 cells and variant SL4 cells, selected for their metastatic potentials, by using the competitive RT-PCR method. The expression levels of mGalNAc-T1, T2, and T7 were slightly higher in the SL4 cells than in the colon 38 cells, whereas the expression level of mGalNAc-T3 in the SL4 cells was 1.5% of that in the colon 38 cells. Products of enzymatic incorporations of GalNAc residues into FITCPTTTPITTTTK peptide by the use of microsome fractions of these cells as the enzyme source were separated and characterized for the number of attached GalNAc residues and their positions. The maximum number of attached GalNAc residues was 6 and 4 when the microsome fractions of the colon 38 cells and SL4 cells were used, respectively. When the microsome fractions of the colon 38 cells were treated with a polyclonal antibody raised against mGalNAc-T3, the maximum number of incorporated GalNAc residues was 4. These results strongly suggest that mGalNAc-T3 in colon 38 cells is involved in additional transfer of GalNAc residues to this peptide.

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