Golgi Glycosylation
نویسندگان
چکیده
منابع مشابه
Asparagine-linked glycosylation in the yeast Golgi.
The Golgi complex is the site where the terminal carbohydrate modification of proteins and lipids occurs. These carbohydrates play a variety of biological roles, ranging from the stabilization of glycoprotein structure to the provision of ligands for cell-cell interactions to the regulation of cell surface properties. Progress in our understanding of the biosynthesis and regulation of glycoconj...
متن کاملGolgi glycosylation and human inherited diseases.
The Golgi factory receives custom glycosylates and dispatches its cargo to the correct cellular locations. The process requires importing donor substrates, moving the cargo, and recycling machinery. Correctly glycosylated cargo reflects the Golgi's quality and efficiency. Genetic disorders in the specific equipment (enzymes), donors (nucleotide sugar transporters), or equipment recycling/reorga...
متن کاملGolgi glycosylation defect in Pompe iPSC-cardiomyocytes
Background: How the absence of lysosomal enzyme acid α-glucosidase causes hypertrophic cardiomyopathy in Pompe disease is unknown. Results: Pompe patient induced pluripotent stem cell-derived cardiomyocytes have normal autophagic and contractile function, but exhibit a deficit of golgi-based protein glycosylation. Conclusions: Loss of lysosomal glycogen hydrolyzing ability results in protein gl...
متن کاملConserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery.
Cell surface lectin staining, examination of Golgi glycosyltransferases stability and localization, and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis were employed to investigate conserved oligomeric Golgi (COG)-dependent glycosylation defects in HeLa cells. Both Griffonia simplicifolia lectin-II and Galanthus nivalus lectins were specifically bound to the plas...
متن کاملMembrane fusion and glycosylation in the rat hepatic Golgi apparatus
When purified Golgi fractions were incubated with UDP-[3H]galactose in the absence of Triton-X-100, radioactivity was incorporated into an endogenous lipid and several peptide acceptors. Electron microscope analysis of Golgi fractions incubated in the endogenous galactosyl transferase assay medium revealed extensive fusion of Golgi saccules. Systematic removal of constituents in the galactosyl ...
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ژورنال
عنوان ژورنال: Cold Spring Harbor Perspectives in Biology
سال: 2011
ISSN: 1943-0264
DOI: 10.1101/cshperspect.a005199