PubMed:2510926 JSONTXT

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":1118,"end":1123},"obj":"HP_0002664"},{"id":"T2","span":{"begin":1207,"end":1212},"obj":"HP_0002664"}],"text":"Expression of UDP-GalNAc:NeuAc alpha 2,3Gal beta-R beta 1,4(GalNAc to Gal) N-acetylgalactosaminyltransferase involved in the synthesis of Sda antigen in human large intestine and colorectal carcinomas.\nN-Acetylgalactosamine beta 1,4-linked to a galactose residue substituted in O-3 with one N-acetylneuraminic acid residue is the immunodominant sugar of the human blood group Sda antigen which is also largely present in the kidney medulla and colon mucosa. A beta 1,4-N-acetylgalactosaminyltransferase very similar to that previously described in urine of Sd(a+) individuals (F. Serafini-Cessi, N. Malagolini, and F. Dall'Olio. Arch. Biochem. Biophys., 266: 573-582, 1988) has been identified in cells released from human large intestine. The higher values of beta 1,4-N-acetylgalactosaminyltransferase activity were detected in proximal and medial segments of the large intestine, suggesting a proximal-distal gradient of the enzyme expression. When the beta 1,4-N-acetylgalactosaminyltranferase activity of colorectal carcinoma specimens from 18 patients was compared with that of the normal mucosa surrounding the tumor, a constant and in several cases drastic reduction of the activity was detected in tumor cells. Three human colorectal adenocarcinoma cell lines (Colo-205, SW-48, and SW-948) have been found to lack the beta 1,4-N-acetylgalactosaminyltransferase activity. Altogether, these results support the notion that the malignant transformation drastically affects the expression of this glycosyltransferase in large bowel cells."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":159,"end":164},"obj":"https://acgg.asia/db/ggdb/info/gg171"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":402,"end":409},"obj":"https://acgg.asia/db/ggdb/info/gg171"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":460,"end":502},"obj":"https://acgg.asia/db/ggdb/info/gg107"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":460,"end":502},"obj":"https://acgg.asia/db/ggdb/info/gg106"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":460,"end":502},"obj":"https://acgg.asia/db/ggdb/info/gg105"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":674,"end":677},"obj":"https://acgg.asia/db/ggdb/info/gg135"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":723,"end":728},"obj":"https://acgg.asia/db/ggdb/info/gg171"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":761,"end":803},"obj":"https://acgg.asia/db/ggdb/info/gg107"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":761,"end":803},"obj":"https://acgg.asia/db/ggdb/info/gg106"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":761,"end":803},"obj":"https://acgg.asia/db/ggdb/info/gg105"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":866,"end":871},"obj":"https://acgg.asia/db/ggdb/info/gg171"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1327,"end":1369},"obj":"https://acgg.asia/db/ggdb/info/gg107"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1327,"end":1369},"obj":"https://acgg.asia/db/ggdb/info/gg106"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":1327,"end":1369},"obj":"https://acgg.asia/db/ggdb/info/gg105"},{"id":"PD-GlycoGenes20190927-B_T15","span":{"begin":1525,"end":1530},"obj":"https://acgg.asia/db/ggdb/info/gg171"}],"text":"Expression of UDP-GalNAc:NeuAc alpha 2,3Gal beta-R beta 1,4(GalNAc to Gal) N-acetylgalactosaminyltransferase involved in the synthesis of Sda antigen in human large intestine and colorectal carcinomas.\nN-Acetylgalactosamine beta 1,4-linked to a galactose residue substituted in O-3 with one N-acetylneuraminic acid residue is the immunodominant sugar of the human blood group Sda antigen which is also largely present in the kidney medulla and colon mucosa. A beta 1,4-N-acetylgalactosaminyltransferase very similar to that previously described in urine of Sd(a+) individuals (F. Serafini-Cessi, N. Malagolini, and F. Dall'Olio. Arch. Biochem. Biophys., 266: 573-582, 1988) has been identified in cells released from human large intestine. The higher values of beta 1,4-N-acetylgalactosaminyltransferase activity were detected in proximal and medial segments of the large intestine, suggesting a proximal-distal gradient of the enzyme expression. When the beta 1,4-N-acetylgalactosaminyltranferase activity of colorectal carcinoma specimens from 18 patients was compared with that of the normal mucosa surrounding the tumor, a constant and in several cases drastic reduction of the activity was detected in tumor cells. Three human colorectal adenocarcinoma cell lines (Colo-205, SW-48, and SW-948) have been found to lack the beta 1,4-N-acetylgalactosaminyltransferase activity. Altogether, these results support the notion that the malignant transformation drastically affects the expression of this glycosyltransferase in large bowel cells."}