N-linked oligosaccharide processing is not necessary for glycoprotein secretion in plants
نویسندگان
چکیده
منابع مشابه
Carbohydrate-deficient glycoprotein syndrome: not an N-linked oligosaccharide processing defect, but an abnormality in lipid-linked oligosaccharide biosynthesis?
The carbohydrate-deficient glycoprotein syndrome (CDGS) is a developmental disease associated with an abnormally high isoelectric point of serum transferrin. Carbohydrate analyses of this glycoprotein initially suggested a defect in N-linked oligosaccharide processing, although more recent studies indicate a defect in the attachment of these sugar chains to the protein. We studied both serum gl...
متن کاملDolichol is not a necessary moiety for lipid-linked oligosaccharide substrates of the mannosyltransferases involved in in vitro N-linked-oligosaccharide assembly.
Dolichol is utilized in vivo as an unusually large anchor on which the precursor for N-linked oligosaccharides is assembled by a series of glycosyltransferases. The role of dolichol in enzyme substrate recognition is investigated. Thus the biosynthetic intermediate NN'-diacetylchitobiose was chemically linked to either dolichol or the much shorter fully saturated tetraisoprenoid phytanol. Both ...
متن کاملProcessing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop. Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained ...
متن کاملN-Linked Oligosaccharide Chains
Many of the proteins that are translocated into the endoplasmic reticulum are glycosylated with the addition of a 14saccharide core unit (Glc,Man,GlcNAc,) to specific asparagine residues of the nascent polypeptide. Glucose residues are then removed by endoplasmic reticulum-located glucosidases, with diglucosylated and monoglucosylated intermediates being formed. In this study, we used a cell-fr...
متن کاملCharacterization of endomannosidase inhibitors and evaluation of their effect on N-linked oligosaccharide processing during glycoprotein biosynthesis.
Endo-alpha-D-mannosidase is a Golgi-located processing enzyme that achieves deglucosylation of N-linked carbohydrate units through its unique property of cleaving the oligosaccharide chain internally with the release of glucose-substituted mannose (Glc1-3Man). By chemically modifying the characteristic disaccharide product, Glc alpha 1-->3Man, a number of potent inhibitors of the endomannosidas...
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ژورنال
عنوان ژورنال: The Plant Journal
سال: 1996
ISSN: 0960-7412,1365-313X
DOI: 10.1046/j.1365-313x.1996.10040713.x