C1GALT1 in health and disease (Review)
Xiaojie Sun, Mengru Zhan, Xun Sun, Wanqi Liu, Xiangwei Meng
Abstract
O‑linked glycosylation (<em>O</em>‑glycosylation) and N‑linked glycosylation (<em>N</em>‑glycosylation) are the two most important forms of protein glycosylation, which is an important post‑translational modification. The regulation of protein function involves numerous mechanisms, among which protein glycosylation is one of the most important. Core 1 synthase glycoprotein‑N‑acetylgalactosamine 3‑β‑galactosyltransferase 1 (<em>C1GALT1</em>) serves an important role in the regulation of O‑glycosylation and is an essential enzyme for synthesizing the core 1 structure of mucin‑type O‑glycans. Furthermore, <em>C1GALT1</em> serves a vital role in a number of biological functions, such as angiogenesis, platelet production and kidney development. Impaired <em>C1GALT1</em> expression activity has been associated with different types of human diseases, including inflammatory or immune‑mediated diseases, and cancer. <em>O</em>‑glycosylation exists in normal tissues, as well as in tumor tissues. Previous studies have revealed that changes in the level of glycosyltransferase in different types of cancer may be used as potential therapeutic targets. Currently, numerous studies have reported the dual role of <em>C1GALT1</em> in tumors (carcinogenesis and cancer suppression). The present review reports the role of <em>C1GALT1</em> in normal development and human diseases. Since the mechanism and regulation of <em>C1GALT1</em> and <em>O</em>‑glycosylation remain elusive, further studies are required to elucidate their effects on development and disease.