Disease relevance of Endoplasmic Reticulum, Rough

• PAP is almost absent from normal acinar cells; after acute pancreatitis, it appears in rough endoplasmic reticulum, it is strongly present in normal and abnormal zymogen granules, and it remains an important component of the fibrous material [1].
• Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum [2].
• 0. The vesicular stomatitis virus encoded membrane glycoprotein (G protein) resident in the rough endoplasmic reticulum (labeled with [35S]methionine) or Golgi complex (labeled with [3H]palmitate) of 15B cells at the time of fusion can reach Golgi complexes from wild-type cells after fusion; G protein present in the plasma membrane cannot [3].
• Mutations blocking the transport of the influenza virus hemagglutinin between the rough endoplasmic reticulum and the Golgi apparatus [4].
• Mutants ts1 and ts227 of fowl plague virus have a temperature-sensitive defect in the transport of the hemagglutinin from the rough endoplasmic reticulum to the Golgi apparatus [4].

High impact information on Endoplasmic Reticulum, Rough

• Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus [5].
• Our results suggest that assembly of VP4 precedes that of VP7, the major outer shell protein, and that VP4 may play an important role in the receptor recognition and budding process through the rough endoplasmic reticulum during virus maturation [6].
• Oligosaccharyltransferase catalyzes the N-linked glycosylation of asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum (RER) [7].
• SC is synthesized as a core glycosylated transmembrane glycoprotein on the rough endoplasmic reticulum [8].
• A purification to apparent homogeneity of a negatively charged protein (ERp180) of relative molecular mass 180,000 (180 K) was reported which was proposed to function as a rough endoplasmic reticulum ribosome receptor [9].

Chemical compound and disease context of Endoplasmic Reticulum, Rough

• The effect of progesterone on the movement of sterols from the cell surface to the rough endoplasmic reticulum (ER) was examined in rat hepatoma cells [10].
• In the hepatoma cells, AFP synthesis was found to occur through ribosomes of the rough endoplasmic reticulum, since AFP was demonstrated around ribosomes of the rough endoplasmic reticulum by the peroxidase antibody technique [11].
• The perinatal hypoxia also led to a significantly lower volume and volume density of the secretory apparatus (rough endoplasmic reticulum and secretory granules) on day 7 in 10% O2-born rats [12].

Biological context of Endoplasmic Reticulum, Rough

• The SFFV env gene encodes a membrane glycoprotein, gp55, which is located on the cell surface and in the rough endoplasmic reticulum and is essential both for the induction of leukaemia in vivo and erythroblast proliferation in vitro [13].
• It is proposed that the intact precursor occurs in rough endoplasmic reticulum and Golgi; thereafter, in the immature electron-dense granules, and subsequently in electron-lucent granules, biosynthetic processing liberates gastrin 17 and gastrin 34, which are the major active products of gastrin gene expression [14].
• Inositol trisphosphate modification of ion transport in rough endoplasmic reticulum [15].
• Invariant chain (Ii) is a nonpolymorphic, non-major histocompatibility complex (MHC)-encoded glycoprotein that rapidly associates with newly synthesized class II MHC alpha and beta chains in the rough endoplasmic reticulum [16].
• Membrane dimensions from Golgi apparatus and rough endoplasmic reticulum were cell-size dependent, and these organelles matured within 2 months of postnatal life [17].

Anatomical context of Endoplasmic Reticulum, Rough

• The results are incompatible with bulk-phase movement of the luminal contents of the endoplasmic reticulum, and suggest that there is a membrane-bound receptor that selectively mediates the transport of secretory proteins from the rough endoplasmic reticulum to the Golgi [18].
• The processing of endogenously synthesized gp160 for recognition by CD4+ T cells required that the protein, after synthesis on the rough endoplasmic reticulum and during subsequent cellular transport, remain attached to the luminal/extracellular membrane face by a hydrophobic anchor sequence [19].
• These observations of the rough endoplasmic reticulum, Golgi apparatus, and secretory granules were correlated with histologic interpretations and flow cytometric measurements of abnormalities of DNA content [20].
• Detailed ultrastructural and morphometric studies revealed a decrease of visible microtubules, and a displacement of the smooth and rough endoplasmic reticulum and Golgi apparatus [21].
• The progesterone receptor in uterine stromal cells was mainly localized in the nucleus; however, a small fraction of antigen was present in the cytoplasm, where it was associated with the rough endoplasmic reticulum and with free ribosomes [22].

Associations of Endoplasmic Reticulum, Rough with chemical compounds

• Most eukaryotic secretory and membrane proteins insert co-translationally into the membrane of the rough endoplasmic reticulum (RER), and are targeted there by one or more NH2-terminal or internal signal sequences [23].
• Retention of nonhelical procollagen containing cis-hydroxyproline in rough endoplasmic reticulum [24].
• One deletion mutant, delta 1473, codes for a protein that remains in the rough endoplasmic reticulum (Rose, J. K., and J. E. Bergmann, 1982, Cell, 30:753-762) and contains only high mannose-type oligosaccharides [25].
• As expected, dimer formation, which occurs in the rough endoplasmic reticulum, was unaffected by monensin [26].
• Short pulse labeling in the presence of [35S]methionine resulted in two precursor species (Mr = 44,000 and 47,000), present in a microsomal fraction with a density of 1.18 g/ml in sucrose, presumably derived from the rough endoplasmic reticulum [27].

Gene context of Endoplasmic Reticulum, Rough

• Furthermore, the endoglycosidase H-sensitive EPO-R is more stable than in the absence of gp55, a result suggesting that interaction of gp55 with the EPO-R causes it to remain within the rough endoplasmic reticulum [28].
• Although such mutations induce enlarged rough endoplasmic reticulum (rER) as a morphological change, the metabolic trafficking of mutated COMP remains unclear [29].
• These results indicate that the system responsible for the degradation of the probe in the rough endoplasmic reticulum and the intramembrane cleavage by gamma-secretase that produces soluble, secreted Abeta are distinct and opposing processes [30].
• The heavy chains of the HLA-A and -B antigens were inserted asymmetrically into the rough endoplasmic reticulum of BRI 8 cells as transmembrane polypeptides [31].
• This cleavage step is regulated by a putative sterol-sensing molecule, SREBP-activating protein (SCAP), that forms a complex with SREBPs and traffics between the rough endoplasmic reticulum and Golgi [32].

Analytical, diagnostic and therapeutic context of Endoplasmic Reticulum, Rough

• Immunofluorescence data show an apparent concentration of the TG protein in the rough endoplasmic reticulum [33].
• Immunofluorescence and immunoelectron microscopy showed that truncation before D409 blocks the movement from rough endoplasmic reticulum to the Golgi apparatus [34].
• By immunoprecipitation from Triton X-114 lysates of radiolabeled J774 cells, we determined that the mature 60-kDa receptor is a transmembrane glycoprotein which is synthesized in the rough endoplasmic reticulum as a 53-kDa precursor [35].
• Primary cell cultures were incubated in radioactively labeled amino acids, and a subcellular fraction containing secretory granules was separated from a subcellular fraction containing rough endoplasmic reticulum and Golgi apparatus by centrifugation of homogenates on gradients on Percoll (Pharmacia Fine Chemicals) [36].
• Pulse-chase experiments in the colon cell line LS 174T combined with subcellular fractionation by sucrose density gradient centrifugation showed that the initial dimerization of the MUC2 apomucin started directly after translocation of the apomucin into the rough endoplasmic reticulum as detected by calnexin reactivity [37].

References