scholarly journals CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse

1981 ◽  
Vol 199 (2) ◽  
pp. 393-398 ◽  
Author(s):  
K Grankvist ◽  
S L Marklund ◽  
I B Täljedal
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Pancreatic Islets ◽  
Islet Cells ◽  
Blood Contamination ◽  
Tissue Samples ◽  
Mouse Islets ◽  
Cuzn Superoxide Dismutase ◽  
Endogenous Enzymes

Exogenous superoxide dismutase, catalase and scavengers of the hydroxyl radical protect pancreatic-islet cells against the toxic actions of alloxan in vitro [Grankvist et al. (1979) Biochem. J. 182, 17--25]. To test whether the extraordinary sensitivity of islet cells to alloxan is due to a deficiency of endogenous enzymes protecting against oxygen-reduction products, we assayed CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in mouse islets and other tissues. To correct for any blood contamination, haemoglobin was also measured in the tissue samples. Pancreatic islets were found to belong to tissues with relatively little activity of the protective enzymes. However, the deviation from other tissues in this respect is probably not large enough to explain the especially great susceptibility of islet cells to alloxan.

Vanadium effect on the activity of horseradish peroxidase, catalase, glutathione peroxidase, and superoxide dismutase in vitro

1992 ◽  
Vol 46 (3) ◽  
pp. 161-174 ◽  
Author(s):  
Miguel Ángel Serra ◽  
Enrico Sabbioni ◽  
Alessandro Pintar ◽  
Luigi Casella
Keyword(s):  
Superoxide Dismutase ◽  
Horseradish Peroxidase ◽  
Glutathione Peroxidase

scholarly journals Enhanced N-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Toxicity in Mice Deficient in CuZn-Superoxide Dismutase or Glutathione Peroxidase

2000 ◽  
Vol 59 (1) ◽  
pp. 53-61 ◽  
Author(s):  
Jing Zhang ◽  
Doyle G. Graham ◽  
Thomas J. Montine ◽  
Ye-Shih Ho
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Cuzn Superoxide Dismutase

In vitro lymphocyte recognition of islet cells following in vivo priming with allogeneic murine pancreatic islets

1984 ◽  
Vol 105 (1) ◽  
pp. 87-92 ◽  
Author(s):  
Joanne Scott ◽  
Peter G. MacKay ◽  
Åke Lernmark
Keyword(s):  
Lymph Node ◽  
Pancreatic Islets ◽  
Islet Cell ◽  
Islet Cells ◽  
Culture Conditions ◽  
Pancreatic Tissue ◽  
Insulin Dependent ◽  
Lymph Node Cells

Abstract. Lymphocytes from patients with insulin-dependent diabetes have been shown to be sensitized to pancreatic tissue antigens. Mice immunized with homologous pancreatic islets have been found to develop glucose intolerance and insulitis. Since lymphocytes may be involved in diabetogenesis, we wished to determine if lymph node cells from islet-immunized mice can recognize and respond to islet cells in vitro. A.TL female mice were immunized with an emulsion of BALB/c islet homogenate and complete Freund's adjuvant (CFA); sham-treated A.TL mice were injected with adjuvant and water. Mice were sacrificed 7–8 days later and the draining lymph nodes were removed. The lymph node cells were co-cultured with freshly prepared irradiated BALB/c islet cell, which served as stimulator cells. The co-cultures were incubated for 24–26 h at 37°C, followed by a 16 h [3H]thymidine (TdR) pulse. A significant proliferation of lymph node cells from islet-primed mice was induced during the in vitro stimulation with irradiated islet cells when compared with lymph node cells from sham-treated mice (P < 0.001). The response may be islet-cell-specific, since irradiated lymph node cells from BALB/c mice failed to proliferative response under the same culture conditions (P > 0.80).

scholarly journals Superoxide dismutase, catalase and scavengers of hydroxyl radical protect against the toxic action of alloxan on pancreatic islet cells in vitro

1979 ◽  
Vol 182 (1) ◽  
pp. 17-25 ◽  
Author(s):  
K Grankvist ◽  
S Marklund ◽  
J Sehlin ◽  
I B Täljedal
Keyword(s):  
Superoxide Dismutase ◽  
Singlet Oxygen ◽  
Trypan Blue ◽  
Islet Cells ◽  
Direct Reaction ◽  
Oxygen Scavenger ◽  
Isolated Pancreatic Islets ◽  
Cytotoxicity Assays ◽  
Redox Cycles

Experiments with isolated pancreatic islets or dispersed islet cells from non-inbred ob/ob mice were performed to test the hypothesis that free radicals, notably OH., mediate the diabetogenic toxicity of alloxan. Accumulation of 86Rb+ by whole islets and exclusion of Trypan Blue by dispersed cells were used as previously validated criteria of islet-cell viability. Alloxan alone drastically inhibited the Rb+ accumulation and significantly decreased the frequency of cells excluding Trypan Blue. Enzymic scavengers of O2.- and H2O2 or non-enzymic scavengers of OH. or singlet oxygen were added to the incubation medium and tested for their ability to protect against these effects of alloxan. Superoxide dismutase, catalase, dimethyl sulphoxide, benzoate, and mannitol counteracted the effects of alloxan in both cytotoxicity assays. Significant protection of the Rb+-accumulating capacity was also afforded by butanol, caffeine, theophylline, NADH, NADPH and, to a small extent, NAD+. Urea has a poor affinity for OH. and did not protect against alloxan. No effect was obtained with the singlet-oxygen scavenger, histidine. Except for the protection by NADH and NADPH, which may be due to a direct reaction with alloxan in the medium, the results strongly support the hypothesis. beta-Cells may be particularly vulnerable to alloxan because their metabolic specialization facilitates reduction of the drug and perhaps of other substrates for O2.–yielding redox cycles.

Identification of iduronate-2-sulfatase in mouse pancreatic islets

2004 ◽  
Vol 287 (5) ◽  
pp. E983-E990 ◽  
Author(s):  
I. Coronado-Pons ◽  
A. Novials ◽  
S. Casas ◽  
A. Clark ◽  
R. Gomis
Keyword(s):  
Pancreatic Islets ◽  
Cell Function ◽  
Dermatan Sulfate ◽  
Islet Cells ◽  
Secretory Response ◽  
High Rate ◽  
Insulin Content ◽  
Dependent Manner ◽  
Mouse Pancreatic Islets ◽  
Mouse Islets

The lysosomal enzyme iduronate-2-sulfatase (IDS) is expressed in pancreatic islets and is responsible for degradation of proteoglycans, such as perlecan and dermatan sulfate. To determine the role of IDS in islets, expression and regulation of the gene and localization of the enzyme were investigated in mouse pancreatic islets and clonal cells. The Ids gene was expressed in mouse islets and β- and α-clonal cells, in which it was localized intracellularly in lysosomes. The transcriptional expression of Ids in mouse islets increased with glucose in a dose-dependent manner (11.5, 40.2, 88, and 179% at 5.5, 11.1, 16.7, and 24.4 mM, respectively, P < 0.01 for 16.7 and 24.4 mM glucose vs. 3 mM glucose). This increase was not produced by glyceraldehyde (1 mM) or 6-deoxyglucose (21.4 mM) and was blocked by the addition of mannoheptulose (21.4 mM). Neither insulin content nor secretory response to glucose (16.7 mM) was altered in mouse islets infected with lentiviral constructs carrying the IDS gene in sense orientation. Furthermore, no decrease in islet cell viability was observed in mouse islets carrying lentiviral contracts compared with controls. However, insulin content was reduced (35% vs. controls, P < 0.001) in islets infected with IDS antisense construct, while the secretory response of those islets to glucose was maintained. Inhibition of IDS by antisense infection led to an increase in lysosomal size and a high rate of insulin granule degradation via the crinophagic route in pancreatic β-cells. We conclude that IDS is localized in lysosomes in pancreatic islet cells and expression is regulated by glucose. IDS has a potential role in the normal pathway of lysosomal degradation of secretory peptides and is likely to be essential to maintain pancreatic β-cell function.

No effect of superoxide dismutase on spontaneous development of diabetes in db/db mice

1988 ◽  
Vol 117 (1) ◽  
pp. 99-102
Author(s):  
Ove Berglund ◽  
Kjell Grankvist ◽  
Carina Albiin ◽  
Stefan L. Marklund
Keyword(s):  
Superoxide Dismutase ◽  
B Cells ◽  
Superoxide Radical ◽  
Superoxide Radicals ◽  
Cuzn Superoxide Dismutase

Abstract. B-cells have previously been shown to be very susceptible to damage induced by superoxide radicals, and protection against such damage has been achieved both in vitro and in vivo with superoxide dismutase. During maturation, db/db mice develop diabetes and accumulation of potentially superoxide radical-producing leucocytes can be demonstrated in the islets during the process. To test for the possibility that superoxide radical-induced damage contributes to the development of diabetes, db/db mice were given daily ip injections of 200 mg/kg polyethylene glycolsubstituted CuZn superoxide dismutase. No effect of the treatment could be demonstrated.

Indole-3-Carbinol Inhibits Nasopharyngeal Carcinoma

2010 ◽  
Vol 29 (2) ◽  
pp. 185-192 ◽  
Author(s):  
Wei Zhu ◽  
Wenxue Li ◽  
Guangyu Yang ◽  
Quanxin Zhang ◽  
Ming Li ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Nasopharyngeal Carcinoma ◽  
Glutathione Peroxidase ◽  
Tumor Growth ◽  
Caspase 3 ◽  
Caspase 9 ◽  
Human Nasopharyngeal Carcinoma ◽  
Induced Apoptosis

This study explored the effects of indole-3-carbinol on the proliferation of human nasopharyngeal carcinoma, both in vitro and in vivo, and the underlying mechanisms in inducing apoptosis of CNE1 cells. Proliferation, apoptosis, malondialdehyde, superoxide dismutase, glutathione peroxidase, expressions of caspase-9, and caspase-3 in human nasopharyngeal carcinoma cells CNE1 were examined. Indole-3-carbinol suppressed proliferation, induced apoptosis, decreased malondialdehyde level, increased the activity of superoxide dismutase and glutathione peroxidase, and up-regulated the expression of active fragments of caspase-9 and caspase-3 both in vitro and in vivo. It was concluded that indole-3-carbinol could inhibit proliferation and induce apoptosis of CNE1 cells and inhibit tumor growth in mice. Increased activity of superoxide dismutase and glutathione peroxidase and activated expression of caspase-9 and caspase-3 were also observed in indole-3-carbinol–treated tumors or tumor cells, suggesting that stress- and apoptosis-related molecules are involved in the indole-3-carbinol–induced apoptosis and inhibition of tumor growth.

Liquid storage of ram semen in the absence or presence of some antioxidants

1996 ◽  
Vol 8 (6) ◽  
pp. 1013 ◽  
Author(s):  
WM Maxwell ◽  
T Stojanov
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Intrauterine Insemination ◽  
Fertilization Rates ◽  
Liquid Storage ◽  
Semen Storage ◽  
Acrosome Integrity ◽  
Improvement In Survival ◽  
Fresh Semen

The antioxidants superoxide dismutase (SOD), catalase (CAT), cytochrome c (CHc) and glutathione peroxidase (GP) were added at various concentrations to Tris-glucose-yolk diluent (TGY), and their effects on motility, acrosome integrity and fertility of ram spermatozoa were assessed after extension and liquid storage. All the antioxidants improved the motility and acrosome integrity of spermatozoa, and a combination of SOD and CAT had an additive effect on the survival of spermatozoa stored at 5 degrees C but not at 25 degrees C. There was a linear improvement in survival of spermatozoa with increasing dose of antioxidants except for CAT for which doses higher than 200 U mL-1 were toxic. The proportion of oocytes fertilized in vitro declined with time of semen storage (P < 0.001), and was better for semen diluted with TGY containing SOD or CAT than TGY without antioxidants when stored for 7 days (116/246, 47% v. 25/79, 32%; P < 0.05) but not for 14 days (23/174, 13% v. 8/66, 12%). Fertilization rates were unaffected by the presence or absence in the diluent of CHc or GP. The proportions of ewes with fertilized ova and of recovered ova fertilized were better after insemination with semen diluted in TGY containing SOD and CAT than TGY without antioxidants when stored for 14 days (9/18, 50% and 20/40, 50% v. 2/13, 15% and 5/32, 16%; P < 0.05) but not for 7 days (9/20, 45% and 16/48, 33% v. 8/16, 50% and 24/41, 59%). Pregnancy rates were better after intrauterine insemination of ewes with fresh semen than stored semen (11/18, 61% v. 21/75, 28%; P < 0.01), and with semen stored in TGY containing SOD and CAT than in TGY without antioxidants (15/37, 41% v. 6/38, 16%; P < 0.05).

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