Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

2-Deoxy-D-glucose (DOG) effectively inhibited vesicular stomatitis virus (VSV) multiplication in Vero cells when pyruvate-containing medium was used as an energy source. The effectiveness of the antimetabolite was markedly reduced by substituting glucose for pyruvate in the maintenance medium. Addition of DOG at intervals during the viral growth cycle caused a notable decrease in viral yields. This inhibiting effect was reversed by mannose and to a lesser extent by glucose. VSV-RNA synthesis was greatly reduced, thereby eventually resulting in decreased levels of virus proteins. Polyacrylamide gel electrophoresis of purified VSV grown in medium containing pyruvate and DOG revealed the presence of two peaks in the region of the virus G protein. Possibly, DOG induces the synthesis of aberrant viral proteins which become incorporated into the viral membrane, resulting in noninfectious particles.
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PMID:Inhibition of vesicular stomatitis virus multiplication in Vero cells by 2-deoxy-D-glucose. 4 33

The glucagonoma syndrome is characterized by dermatitis, stomatitis, elevated serum glucagon levels, abnormal glucose tolerance, weight loss, and anemia--all in association with a glucagon-secreting alpha-cell tumor of the pancreas. A review of 21 cases showed strikingly similar features. A generalized, symmetrical dermatitis initially appeared to be asteatotic or eczematous over the perineum, buttocks, and lower extremities. Gradually, a more characteristic migratory necrolytic erythema with transient bulla formation and erosions developed in intertriginous and dependent areas. Histologically, the most specific features included necrolysis of the upper epidermis, with liquefaction necrosis of the granular cell layer and subcorneal clefting or blister formation. The dermatologist is often first to examine such patients; early recognition of this syndrome with prompt surgical removal of the primary pancreatic lesion may afford cure of the neoplasm.
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PMID:Glucagonoma syndrome. Report of two cases and literature review. 19 36

The synthesis of the complex-type oligosaccharide unit of the vesicular stomatitis virus G protein is initiated by the en bloc transfer of a high molecular weight oligosaccharide from a lipid carrier to the nascent polypeptide. Following transfer the oligosaccharide is "processed" by removal of glucose and mannose residues and the sugars that constitute the outer branches of the complex-type oligosaccharide are added. The structure of the oligosaccharide moiety of the lipid-linked precursor has been elucidated in order to further define the steps involved in processing. Since it was not feasible to obtain adequate amounts of material for standard structural studies, most of the structural studies were performed on radiolabeled material, with radioactivity incorporated differentially into glucose, mannose, and N-acetylglucosamine. Based on endo-beta-N-acetylglucosaminidase CII digestion, alpha-mannosidase digestion, acetolysis, Smith periodate degradation, methylation analysis, and periodate oxidation, we propose the following structure for the oligosaccharide moiety of the lipid-linked oligosaccharide.
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PMID:The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein. 21 34

Most, if not all, of the glucagon-producing tumours of the pancreas are malignant. For this reason an early diagnosis is essential. The glucagonoma syndrome is associated with a skin rash, stomatitis, anaemia, glucose-intolerance, hypoaminoacidaemia, weight loss, elevated sedimentation rate and hyperglucagonaemia. The more important and constant findings are the skin lesion, the low level of aminoacids in the blood and the increased glucagon concentrations. The skin lesion is not pathognomonic, but any therapy-resistant bullous dermatosis which microscopically is characterized by epidermal changes should alert the clinician to suspect a glucagonoma. The syndrome can be proved by demonstration of hyperglucagonaemia and a pancreatic tumour.
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PMID:Possible entries to the diagnosis of a glucagon-producing tumour. 22 89

The role of glucosylated oligosaccharides in the biogenesis of the glycoprotein (G protein) of vesicular stomatitis virus was studied in PhaR2.7, a mouse lymphoma cell line deficient in glucosidase II activity. As expected, the great majority of cell-associated G protein remained glucosylated in PhaR2.7, and the G protein was rapidly deglucosylated in BW5147, the parental cell line. Despite these differences in glucosylation, the rates of G protein trimerization and transport to the cell surface were as rapid and efficient in the PhaR2.7 mutant as in BW5147. Surprisingly, greater than 73% of the oligosaccharides on G proteins recovered from released virions were complex-type units. The efficient processing of the G protein oligosaccharides coincided with the efficient removal of glucose residues from its oligosaccharides. After treatment with deoxynojirimycin, an inhibitor of endoplasmic reticulum (ER) glucosidases I and II, the total percentage of G protein-associated high mannose-type oligosaccharides increased more in the parental cells than in the mutant cells. Furthermore, when the G protein was retained in the ER of PhaR2.7 cells by depletion of the cellular ATP pools with carbonyl cyanide m-chlorophenylhydrazone, its oligosaccharides remained glucosylated. Under identical conditions, BW5147 cells removed the glucose residues from > 90% of the retained G protein's oligosaccharides. Thus, PhaR2.7 cells efficiently remove glucose residues from high mannose-type oligosaccharides of selected proteins using a deoxynojirimycin-insensitive enzyme located in a post-ER compartment. The existence of a second mechanism for the deglucosylation of N-linked oligosaccharides provides evidence for the important role of glucose removal in glycoprotein maturation.
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PMID:Identification of a novel mechanism for the removal of glucose residues from high mannose-type oligosaccharides. 132 42

Lec23 Chinese hamster ovary (CHO) cells have been shown to possess a unique lectin resistance phenotype and genotype compared with previously isolated CHO glycosylation mutants (Stanley, P., Sallustio, S., Krag, S. S., and Dunn, B. (1990) Somatic Cell Mol. Genet. 16, 211-223). In this paper, a biochemical basis for the lec23 mutation is identified. The carbohydrates associated with the G glycoprotein of vesicular stomatitis virus (VSV) grown in Lec23 cells (Lec23/VSV) were found to possess predominantly oligomannosyl carbohydrates that bound strongly to concanavalin A-Sepharose, eluted 3 sugar eq beyond a Man9GlcNAc marker oligosaccharide on ion suppression high pressure liquid chromatography, and were susceptible to digestion with jack bean alpha-mannosidase. Monosaccharide analyses revealed that the oligomannosyl carbohydrates contained glucose, indicating a defect in alpha-glucosidase activity. This was confirmed by further structural characterization of the Lec23/VSV oligomannosyl carbohydrates using purified rat mammary gland alpha-glucosidase I, jack bean alpha-mannosidase, and 1H NMR spectroscopy at 500 MHz. [3H]Glucose-labeled Glc3Man9GlcNAc was prepared from CHO/VSV labeled with [3H]galactose in the presence of the processing inhibitors castanospermine and deoxymannojirimycin. Subsequently, [3H]Glc2Man9GlcNAc was prepared by purified alpha-glucosidase I digestion of [3H]Glc3Man9GlcNAc. When these oligosaccharides were used as alpha-glucosidase substrates it was revealed that Lec23 cells are specifically defective in alpha-glucosidase I, a deficiency not previously identified among mammalian cell glycosylation mutants.
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PMID:A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I. 166 Apr 60

A 49-year-old woman suffered from recurrent episodes of necrolytic migratory erythema over the lower legs, lower abdomen, and buttocks for more than two years. Stomatitis, glossitis and vaginitis were the accompanying symptoms and signs during each episode. The result of skin biopsy revealed superficial necrosis in the upper half of the epidermis. Laboratory examinations revealed mild glucose intolerance and hypoaminoacidemia. Fasting plasma glucagon level measured by radioimmunoassay was 890 pg/mL. Oral glucose loading test showed a paradoxical increase in plasma glucagon level up to 1,500 pg/mL. Abdominal echo, computerized axial tomography, and celiac angiography demonstrated a hypervascular tumor, 4 cm in diameters, located at the pancreatic head. Glucagonoma syndrome was confirmed and diagnosed. The patient underwent surgical resection of the tumor mass. Necrolytic migratory erythema disappeared thereafter, and the plasma glucagon level declined to 120 pg/mL. Histologically, the tumor revealed an islet cell carcinoma composed of moderately uniform cells with a few mitosis, arranged in cords and nests. Abundant characteristic secretory granules of the pancreatic A cell were found within the tumor cells by electron microscopic examination.
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PMID:[Necrolytic migratory erythema as the first manifestation of glucagonoma]. 168 96

The mechanism by which cells increase their rate of glucose uptake in response to stress is unclear. Using an immunofluorescence technique to localize the glucose transporter protein in BHK cells, we found that hyperthermia, treatment with arsenite, infection with vesicular stomatitis virus or Semliki Forest virus, and treatment with insulin cause the transporter to move from an intracellular site in the perinuclear region to the plasma membrane; the degree of translocation correlates approximately with the increase in glucose uptake. We conclude that stress induces an insulin-like distribution of certain membrane proteins.
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PMID:Cellular stress induces a redistribution of the glucose transporter. 215 42

Murine bone-marrow-culture-derived-macrophages can be differentially activated to lyse either vesicular stomatitis virus infected BALB/c3T3 cells or the tumor target P815. Macrophages were activated in a manner so that they could lyse both targets. The ability of this activated population to lyse either target type was differentially inhibited by varying the assay conditions. The lysis of P815 targets was more sensitive to inhibition by the proteinase inhibitor N-p-tosyl-L-lysine chloromethyl ketone than was the lysis of virally infected cells. On the other hand, reduction of the concentration of glucose in the assay medium, which inhibits the production of oxygen metabolites by the hexose monophosphate shunt, or the addition of anti-tumor necrosis factor (anti-TNF) serum were able to decrease the lysis of virally infected targets but not P815 targets. Thus, the observed differences in the lysis of these two targets were due to both the activation state of the macrophages and the differential susceptibility of the targets to different effector mechanisms.
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PMID:Activated macrophages use different cytolytic mechanisms to lyse a virally infected or a tumor target. 216 99

Cells infected with a temperature-sensitive mutant of vesicular stomatitis virus, ts045, or transfected with the plasmid vector pdTM12 produce mutant forms of the G protein that remain within the ER. The mutant G proteins were isolated by immunoprecipitation from cells metabolically labeled with [2-3H]mannose to facilitate analysis of the protein-linked oligosaccharides. The 3H-labeled glycopeptides recovered from the immunoprecipitated G proteins contained high mannose-type oligosaccharides. Structural analysis, however, indicated that 60-78% of the 3H-mannose-labeled oligosaccharides contained a single glucose residue and no fewer than eight mannose residues. The 3H-labeled ts045 oligosaccharides were deglucosylated and processed to complex-type units after the infected cells were returned to the permissive temperature. When shifted to the permissive temperature in the presence of a proton ionophore, the G protein oligosaccharides were deglucosylated but remained as high mannose-type units. The glucosylated state was observed, therefore, when the G protein existed in an altered conformation. The ts045 G protein oligosaccharides were deglucosylated in vitro by glucosidase II at both the permissive and nonpermissive temperatures. G protein isolated from ts045-infected cells labeled with [6-3H]galactose in the presence of cycloheximide contained 3H-glucose-labeled monoglucosylated oligosaccharides, indicating that the high mannose oligosaccharides were glucosylated in a posttranslational process. These results suggest that aberrant G proteins are selectively modified by resident ER enzymes to retain monoglucosylated oligosaccharides.
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PMID:Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins. 253 36


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