-
These findings indicate that the fine-tuning of AMPA-R trafficking by LARGE at the Golgi is critical for hippocampus-dependent memory in the brain.
-
data suggest LARGE overexpression may only be deleterious under a forced regenerative context, such as that resulting from a reduction in FKRP: in the absence of such a defect we show that systemic expression of LARGE can indeed act therapeutically, and that even dramatic LARGE overexpression is well-tolerated in heart and skeletal muscle
-
A glucuronic acid beta1,4-xylose disaccharide synthesized by B4GAT1 acts as an acceptor primer that can be elongated by LARGE with the ligand-binding heteropolysaccharide.
-
MBP1 inhibits Ab fibril formation in vitro and demonstrate the ability of MBP1 to reduce Ab pathology and improve behavioral performance.
-
The overexpression of LARGE aggravates muscular dystrophy by suppressing the muscle regeneration and this adverse effect is mediated via reduced expression of IGF-1.
-
Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of alpha-dystroglycan in cells and tissues.
-
The overexpression of LARGE leads to a shortened lifespan and worsening of the FKRP-MD phenotype
-
blocking Large during muscle regeneration results in synthesis of dystroglycan with minimal LARGE-glycan repeats in association with less compact basement membrane, immature neuromuscular junctions, and dysfunctional muscle predisposed to dystrophy
-
Muscular dystrophy defects are primarily due to the effects of LARGE and glycosylated dystroglycan in stabilizing the endplate of the neuromuscular junction.
-
LARGE could act as a bifunctional glycosyltransferase, with xylosyltransferase and glucuronyltransferase activities, which produced repeating units of [-3-xylose-alpha1,3-glucuronic acid-beta1-]; allowed alpha-DG to bind laminin-G domain-containing ECM ligands
-
Differential glycosylation of alpha-dystroglycan and proteins other than alpha-dystroglycan by like-glycosyltransferase.
-
a mechanism by which Large competes with galactosyltransferase to target GlcNAc terminals to induce the functional glycans on alpha-DG
-
results indicate that overexpression of LARGE catalyzes the glycosylation of at least one other glycoprotein in addition to alpha-DG, and that this glycosylation(s) promotes laminin binding activity
-
LARGE has a role in inducing alpha-dystroglycan hyperglycosylation in skeletal and cardiac muscle
-
Previously unreported ocular defects in mice homozygous for a new allele of the Large gene, veils, and for Large(myd) mice.
-
Alpha-dystroglycan is undetectable in the dystrophic Large mouse and laminin-binding activity is reduced.
-
These results together with the finding that O-linked glycosylation at neuromuscular junctions of Large(myd) mice is compromised indicate that the action of Large is necessary for proper neuromuscular junction development.
