Gene Symbol: Large2
Description: LARGE xylosyl- and glucuronyltransferase 2
Alias: 5730485C17Rik, AI891893, Gyltl1b, Largel, mKIAA4105, LARGE xylosyl- and glucuronyltransferase 2, glycosyltransferase-like protein LARGE2, glycoslytransferase-like 1B, glycosyltransferase-like 1B
Grewal P, McLaughlan J, Moore C, Browning C, Hewitt J. Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies. Glycobiology. 2005;15:912-23 pubmed
..Hence, they are termed dystroglycanopathies. A paralogous gene for LARGE (LARGE2 or GYLTL1B) may also have a role in DG glycosylation...
Grewal P, Hewitt J. Mutation of Large, which encodes a putative glycosyltransferase, in an animal model of muscular dystrophy. Biochim Biophys Acta. 2002;1573:216-24 pubmed
..Our results are discussed in the light of recent reports describing mutations in other glycosyltransferase genes in several forms of human muscular dystrophy. ..
Inamori K, Hara Y, Willer T, Anderson M, Zhu Z, Yoshida Moriguchi T, et al
. Xylosyl- and glucuronyltransferase functions of LARGE in ?-dystroglycan modification are conserved in LARGE2. Glycobiology. 2013;23:295-302 pubmed publisher
..Although the LARGE paralog LARGE2 (also referred to as GYLTL1B) has likewise been shown to enhance the functional modification of ?-DG in cultured cells, its enzymatic ..
Yagi H, Nakagawa N, Saito T, Kiyonari H, Abe T, Toda T, et al
. AGO61-dependent GlcNAc modification primes the formation of functional glycans on ?-dystroglycan. Sci Rep. 2013;3:3288 pubmed publisher
..These findings provide a key missing link for understanding how the physiologically critical glycan motif is displayed on ?-DG and provides new insights on the pathological mechanisms of dystroglycanopathy. ..
Inamori K, Willer T, Hara Y, Venzke D, Anderson M, Clarke N, et al
. Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of ?-dystroglycan in cells and tissues. J Biol Chem. 2014;289:28138-48 pubmed publisher
..Both LARGE and its paralog, LARGE2 (also referred to as GYLTL1B) are bifunctional glycosyltransferases with xylosyltransferase (Xyl-T) and glucuronyltransferase (GlcA-T) ..
Inamori K, Beedle A, de BernabÃ© D, Wright M, Campbell K. LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans. Glycobiology. 2016;26:1284-1296 pubmed
Both LARGE1 (formerly LARGE) and its paralog LARGE2 are bifunctional glycosyltransferases withÂ xylosy- and glucuronyltransferase activities, and are capable of synthesizing polymers composed of a repeating disaccharide [-3XylÎ±1,..
Ashikov A, Buettner F, Tiemann B, Gerardy Schahn R, Bakker H. LARGE2 generates the same xylose- and glucuronic acid-containing glycan structures as LARGE. Glycobiology. 2013;23:303-9 pubmed publisher
LARGE (like-glycosyltransferase) and LARGE2 (glycosyltransferase-like 1B (GYLTL1B)) are homologous Golgi glycosyltransferases possessing two catalytic domains with homology to members of glycosyltransferase families GT8 and GT49...
Lee J, Pamir N, Liu N, Kirk E, Averill M, Becker L, et al
. Macrophage metalloelastase (MMP12) regulates adipose tissue expansion, insulin sensitivity, and expression of inducible nitric oxide synthase. Endocrinology. 2014;155:3409-20 pubmed publisher
..We propose that MMP12 acts as a double-edged sword by promoting insulin resistance while combatting adipose tissue expansion. ..