Synthesis and processing of protein-linked oligosaccharides in vivo.
10 Jun 1979-Journal of Biological Chemistry (American Society for Biochemistry and Molecular Biology)-Vol. 254, Iss: 11, pp 4568-4576
About: This article is published in Journal of Biological Chemistry.The article was published on 1979-06-10 and is currently open access. It has received 245 citations till now. The article focuses on the topics: In vivo.
Citations
More filters
TL;DR: This review summarizes how perturbation of three major functions of the endoplasmic reticulum in eukaryotic cells causes ER stress and activates signaling pathways collectively termed the unfolded protein response (UPR), and how the UPR reestablishes homeostasis.
Abstract: In homeostasis, cellular processes are in a dynamic equilibrium. Perturbation of homeostasis causes stress. In this review I summarize how perturbation of three major functions of the endoplasmic reticulum (ER) in eukaryotic cells–protein folding, lipid and sterol biosynthesis, and storing intracellular Ca2+ – causes ER stress and activates signaling pathways collectively termed the unfolded protein response (UPR). I discuss how the UPR reestablishes homeostasis, and summarize our current understanding of how the transition from protective to apoptotic UPR signaling is controlled, and how the UPR induces inflammatory signaling.
642 citations
626 citations
TL;DR: The results provided an explanation for trimming and reglucosylation activities in the endoplasmic reticulum and established a direct correlation between glycosylation and folding.
543 citations
Cites background from "Synthesis and processing of protein..."
...It has been known for many years that glycoproteins acquire their N-linked oligosaccharides in the ER and that these undergo extensive processing prior to transport to the Golgi complex (Hubbard and Robbins, 1979; Kornfeld and Kornfeld, 1985; Elbein, 1991)....
[...]
...The outermost of the three glucoses is rapidly removed by glucosidase I, followed by the hydrolysis of the middle glucose by glucosidase II (Hubbard and Robbins, 1979; Michael and Kornfeld, 1980; Atkinson and Lee, 1984; Heftkamp et al., 1984)....
[...]
441 citations
TL;DR: Findings suggest that once complexes between calnexin and glycoproteins are formed, oligosaccharide binding does not contribute significantly to the overall interaction, however, it is likely that the binding of Glc1Man9GlcNAc2 oligosACcharides is a crucial event during the initial recognition of newly synthesized glycoprotein by cal Nexin.
414 citations
References
More filters
TL;DR: The title of the Nobel Lecture of George Palade (1 August, p. 347) should have been "Intracellular aspects of the process of protein secretion."
Abstract: The title of the Nobel Lecture of George Palade (1 August, p. 347) should have been "Intracellular aspects of the process of protein secretion."
3,129 citations
TL;DR: Of all the biologically occurring macromolecules the glycoproteins, which consist of carbohydrate moieties convalently linked to a polypeptide backbone, represent the most diverse group, ranging from substances in which the carbohydrate component represents less than 1% of the total weight to those in which it represents over 80% ofThe total.
Abstract: Glycoproteins have a wide distribution in nature and serve a vast number of functions. There are glycoprotein enzymes and hormones; glycoproteins are found in blood and secretions, in cell membranes, and in connective tissue. Of all the biologically occurring macromolecules the glycoproteins, which consist of carbohydrate moieties convalently linked to a polypeptide backbone, represent the most diverse group, ranging from substances in which the carbohydrate component represents less than 1% of the total weight to those in which it represents over 80% of the total. The proteoglycans, which are classified separately from other glycoproteins and include the chondroitin sulfates, dermatan sulfates, and heparin primarily carbohydrate in the form of numerous heteropolysaccharide chains attached to a polypeptide chain at closely spaced intervals. The sugars that commonly occur in glycoproteins include galactose, mannose, glucose. N-acetylglucosamine, N-acetylgalactosamine, sialic acids, fucose, and xylose. The proteoglycans also contain various uronic and sulfated amino sugars.
717 citations
TL;DR: The chiral stationary phase for lipid-Linked Monosaccharides showed good chiral recognition ability towards various lipids, and this property has been generalized to other lipids as well.
Abstract: PERSPECTIVES AND SUMMARY .... 95 MONOSACCHARIDE DERIVATIVES OF DOLICHOL .... ........ ..... ..... ......... 97 Biosynthesis and Structure 97 Other Lipid-Linked Monosaccharides 102 OLIGOSACCHARIDE-LIPIDS 103 Glucose-Containing Oligosaccharide-Lipids 103 Mannose-Containing Oligosaccharide-Lipids "'''''''''''''''''''''''''''''''''''''''''''''''''''''''''' 104
629 citations
TL;DR: The apparent location of the glycosyltransferases in the Golgi apparatus suggests that these enzymes may be involved in terminating the synthesis of plasma glycoproteins by the liver during secretion, and may possibly be required for secretion of these proteins.
579 citations
TL;DR: It is proposed that during glycosylation of asparagine residues, a common oligosaccharide is transferred from the lipid carrier to protein and is subsequently processed to yield the so-called "high mannose" and "complex" oligOSaccharides.
452 citations