Brockhausen Inka
Department of Medicine and Biochemistry, Human Mobility Research Centre, Queen's University, Kingston General Hospital, Angada 1, Kingston, Ontario K7L 2V7, Canada.
EMBO Rep. 2006 Jun;7(6):599-604. doi: 10.1038/sj.embor.7400705.
The glycoproteins of tumour cells are often abnormal, both in structure and in quantity. In particular, the mucin-type O-glycans have several cancer-associated structures, including the T and Tn antigens, and certain Lewis antigens. These structural changes can alter the function of the cell, and its antigenic and adhesive properties, as well as its potential to invade and metastasize. Cancer-associated mucin antigens can be exploited in diagnosis and prognosis, and in the development of cancer vaccines. The activities and Golgi localization of glycosyltransferases are the basis for the glycodynamics of cancer cells, and determine the ranges and amounts of specific O-glycans produced. This review focuses on the glycosyltransferases of colon and breast cancer cells that determine the pathways of mucin-type O-glycosylation, and the proposed functional and pathological consequences of altered O-glycans.
肿瘤细胞的糖蛋白在结构和数量上常常异常。特别是,粘蛋白型O-聚糖具有几种与癌症相关的结构,包括T和Tn抗原以及某些Lewis抗原。这些结构变化可改变细胞的功能、抗原性和黏附特性,以及其侵袭和转移的潜能。癌症相关的粘蛋白抗原可用于诊断、预后评估以及癌症疫苗的研发。糖基转移酶的活性和高尔基体定位是癌细胞糖动力学的基础,并决定了特定O-聚糖的产生范围和数量。本综述重点关注决定粘蛋白型O-糖基化途径的结肠癌细胞和乳腺癌细胞的糖基转移酶,以及O-聚糖改变所带来的潜在功能和病理后果。