LARGE xylosyl- and glucuronyltransferase 2 (LARGE2)

LARGE xylosyl- and glucuronyltransferase 2 (LARGE2) is a bifunctional enzyme with alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation and functional modification of alpha-dystroglycan and certain proteoglycans by glycosylation. It catalyzes the sequential addition of repeating disaccharide units (xylose and glucuronic acid) to form heteropolysaccharide chains, essential for extracellular matrix protein binding, particularly laminin. This modification is crucial for proper basement membrane stability and protein interactions. LARGE2 is mainly localized to the Golgi apparatus and exhibits a tissue distribution distinct from its paralog LARGE1, with high expression in kidney and placenta. Mutations or functional defects in LARGE2 are implicated in certain forms of muscular dystrophy associated with abnormal glycosylation of dystroglycan. Unlike LARGE1, LARGE2 can also modify specific proteoglycans beyond alpha-dystroglycan, suggesting a broader substrate specificity and specialized cellular roles in extracellular matrix organization and stability[1][2][4].

Other names

Xylosyl- and glucuronyltransferase LARGE2Alpha-1,3-xylosyltransferase LARGE2Beta-1,3-glucuronyltransferase LARGE2GYLTL1BPP5656FLJ35207Glycosyltransferase-like 1BGlycosyltransferase-like protein LARGE2Like-glycosyltransferase 2Ortholog of mouse glycosyltransferase-like 1B