Aberrant α1→2Fucosyltransferases Found in Human Colorectal Carcinoma Involved in the Accumulation of Leb and Y Antigens in Colorectal Tumors

• Published in: Japanese Journal of Cancer Research Vol. 84; no. 9; pp. 989 - 995
• Main Authors: Yazawa, Shin, Nakamura, Jun‐ichi, Asao, Takayuki, Nagamachi, Yukio, Sagi, Morihisa, Malta, Khushi L., Achikawa, Tetsuya T, Akamatsu, Masaru
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.09.1993; Japanese Cancer Association
• Subjects: Biological and medical sciences; Colorectal cancer; Gastroenterology. Liver. Pancreas. Abdomen; Leb and Y antigen; Medical sciences; Stomach. Duodenum. Small intestine. Colon. Rectum. Anus; Tumors; Tumor‐associated antigen; α1→2Fucosyltransferase; Human; Rectal disease; Carcinoma; Tumor associated antigen; Enzyme; Transferases; Glycosyltransferases; Malignant tumor; Galactoside 2-α-L-fucosyltransferase; Colonic disease; Antigen; Lewis system; Blood group; Rectum; Intestinal disease; Hexosyltransferases; Colon; Biological accumulation
• ISSN: 0910-5050; 1349-7006; 1876-4673
• DOI: 10.1111/j.1349-7006.1993.tb00190.x

Evidence indicates that the presence of aberrant α1→2fucosylation pathways is responsible for the accumulation of large quantities of Leb and Y antigens in human colorectal carcinoma. Significantly higher activities of α1→2 as well as α1→3 and α1→4fucosyltransferases were found in most of the tissues from carcinoma than in the adjacent normal tissues and in healthy subjects. α1→2Fucosyl‐transferases associated with the synthesis of Leb (Fucal→2Galβ1→3[Fucc1→4]GlcNAcβ) and Y (Fucα1→2Ga1β→4[Fucα1→3]GlcNAcβ) structures from Le→ (GaIβ1→3[Fucal→4]GlcNAcβ) and X (Galβ1→4[Fucα 1→3]GlcNAcβ) ones, respectively, were demonstrated in colorectal carcinomas and in colorectal carcinoma cell lines (COLO201, LS174T and SW1116). The activation of α1→2fucosyltransferase with such new substrate specificities in colorectal carcinoma might result in the preferential synthesis of Leb and Y structures from Le→ and X rather than from H type 1 and H type 2 structures.