Contents
Academic literature on the topic 'Regē'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Regē.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Regē"
1
RECHSTEINER, Martin, Claudio REALINI, and Vicença USTRELL. "The proteasome activator 11 S REG (PA28) and Class I antigen presentation." Biochemical Journal 345, no. 1 (1999): 1–15. http://dx.doi.org/10.1042/bj3450001.
Full textAbstract:
There are two immune responses in vertebrates: humoral immunity is mediated by circulating antibodies, whereas cytotoxic T lymphocytes (CTL) confer cellular immunity. CTL lyse infected cells upon recognition of cell-surface MHC Class I molecules complexed with foreign peptides. The displayed peptides are produced in the cytosol by degradation of host proteins or proteins from intracellular pathogens that might be present. Proteasomes are cylindrical multisubunit proteases that generate many of the peptides eventually transferred to the cell surface for immune surveillance. In mammalian proteasomes, six active sites face a central chamber. As this chamber is sealed off from the enzyme's surface, there must be mechanisms to promote entry of substrates. Two protein complexes have been found to bind the ends of the proteasome and activate it. One of the activators is the 19 S regulatory complex of the 26 S proteasome; the other activator is ‘11 S REG’ [Dubiel, Pratt, Ferrell and Rechsteiner (1992) J. Biol. Chem. 267, 22369-22377] or ‘PA28’ [Ma, Slaughter and DeMartino (1992) J. Biol. Chem. 267, 10515-10523]. During the past 7 years, our understanding of the structure of REG molecules has increased significantly, but much less is known about their biological functions. There are three REG subunits, namely α, β and γ. Recombinant REGα forms a ring-shaped heptamer of known crystal structure. 11 S REG is a heteroheptamer of α and β subunits. REGγ is also presumably a heptameric ring, and it is found in the nuclei of the nematode work Caenorhabditis elegans and higher organisms, where it may couple proteasomes to other nuclear components. REGα and REGβ, which are abundant in vertebrate immune tissues, are located mostly in the cytoplasm. Synthesis of REG α and β subunits is induced by interferon-γ, and this has led to the prevalent hypothesis that REG α/β hetero-oligomers play an important role in Class I antigen presentation. In the present review we focus on the structural properties of REG molecules and on the evidence that REGα/β functions in the Class I immune response.
2
Elsen, Sylvie, Lee R. Swem, Danielle L. Swem, and Carl E. Bauer. "RegB/RegA, a Highly Conserved Redox-Responding Global Two-Component Regulatory System." Microbiology and Molecular Biology Reviews 68, no. 2 (2004): 263–79. http://dx.doi.org/10.1128/mmbr.68.2.263-279.2004.
Full textAbstract:
SUMMARY The Reg regulon from Rhodobacter capsulatus and Rhodobacter sphaeroides encodes proteins involved in numerous energy-generating and energy-utilizing processes such as photosynthesis, carbon fixation, nitrogen fixation, hydrogen utilization, aerobic and anaerobic respiration, denitrification, electron transport, and aerotaxis. The redox signal that is detected by the membrane-bound sensor kinase, RegB, appears to originate from the aerobic respiratory chain, given that mutations in cytochrome c oxidase result in constitutive RegB autophosphorylation. Regulation of RegB autophosphorylation also involves a redox-active cysteine that is present in the cytosolic region of RegB. Both phosphorylated and unphosphorylated forms of the cognate response regulator RegA are capable of activating or repressing a variety of genes in the regulon. Highly conserved homologues of RegB and RegA have been found in a wide number of photosynthetic and nonphotosynthetic bacteria, with evidence suggesting that RegB/RegA plays a fundamental role in the transcription of redox-regulated genes in many bacterial species.
3
Masuda, Shinji, Yumi Matsumoto, Kenji V. P. Nagashima, et al. "Structural and Functional Analyses of Photosynthetic Regulatory Genes regA and regBfrom Rhodovulum sulfidophilum, Roseobacter denitrificans, and Rhodobacter capsulatus." Journal of Bacteriology 181, no. 14 (1999): 4205–15. http://dx.doi.org/10.1128/jb.181.14.4205-4215.1999.
Full textAbstract:
ABSTRACT Genes coding for putative RegA, RegB, and SenC homologues were identified and characterized in the purple nonsulfur photosynthetic bacteria Rhodovulum sulfidophilum and Roseobacter denitrificans, species that demonstrate weak or no oxygen repression of photosystem synthesis. This additional sequence information was then used to perform a comparative analysis with previously sequenced RegA, RegB, and SenC homologues obtained fromRhodobacter capsulatus and Rhodobacter sphaeroides. These are photosynthetic bacteria that exhibit a high level of oxygen repression of photosystem synthesis controlled by the RegA-RegB two-component regulatory system. The response regulator, RegA, exhibits a remarkable 78.7 to 84.2% overall sequence identity, with total conservation within a putative helix-turn-helix DNA-binding motif. The RegB sensor kinase homologues also exhibit a high level of sequence conservation (55.9 to 61.5%) although these additional species give significantly different responses to oxygen. ARhodovulum sulfidophilum mutant lacking regA orregB was constructed. These mutants produced smaller amounts of photopigments under aerobic and anaerobic conditions, indicating that the RegA-RegB regulon controls photosynthetic gene expression in this bacterium as it does as in Rhodobacterspecies. Rhodobacter capsulatus regA- orregB-deficient mutants recovered the synthesis of a photosynthetic apparatus that still retained regulation by oxygen tension when complemented with reg genes fromRhodovulum sulfidophilum and Roseobacter denitrificans. These results suggest that differential expression of photosynthetic genes in response to aerobic and anaerobic growth conditions is not the result of altered redox sensing by the sensor kinase protein, RegB.
4
Realini, Claudio, Christopher C. Jensen, Zhi-guo Zhang та ін. "Characterization of Recombinant REGα, REGβ, and REGγ Proteasome Activators". Journal of Biological Chemistry 272, № 41 (1997): 25483–92. http://dx.doi.org/10.1074/jbc.272.41.25483.
Full text
5
Elsen, Sylvie, Wanda Dischert, Annette Colbeau, and Carl E. Bauer. "Expression of Uptake Hydrogenase and Molybdenum Nitrogenase in Rhodobacter capsulatus Is Coregulated by the RegB-RegA Two-Component Regulatory System." Journal of Bacteriology 182, no. 10 (2000): 2831–37. http://dx.doi.org/10.1128/jb.182.10.2831-2837.2000.
Full textAbstract:
ABSTRACT Purple photosynthetic bacteria are capable of generating cellular energy from several sources, including photosynthesis, respiration, and H2 oxidation. Under nutrient-limiting conditions, cellular energy can be used to assimilate carbon and nitrogen. This study provides the first evidence of a molecular link for the coregulation of nitrogenase and hydrogenase biosynthesis in an anoxygenic photosynthetic bacterium. We demonstrated that molybdenum nitrogenase biosynthesis is under the control of the RegB-RegA two-component regulatory system in Rhodobacter capsulatus. Footprint analyses and in vivo transcription studies showed that RegA indirectly activates nitrogenase synthesis by binding to and activating the expression of nifA2, which encodes one of the two functional copies of the nif-specific transcriptional activator, NifA. Expression of nifA2 but notnifA1 is reduced in the reg mutants up to eightfold under derepressing conditions and is also reduced under repressing conditions. Thus, although NtrC is absolutely required fornifA2 expression, RegA acts as a coactivator ofnifA2. We also demonstrated that in regmutants, [NiFe]hydrogenase synthesis and activity are increased up to sixfold. RegA binds to the promoter of the hydrogenase gene operon and therefore directly represses its expression. Thus, the RegB-RegA system controls such diverse processes as energy-generating photosynthesis and H2 oxidation, as well as the energy-demanding processes of N2 fixation and CO2 assimilation.
6
Wang, Hong, Marko Vatamaniuk, Zeping Zhao, and Xin Gen Lei. "Altering Two Major Redox Enzymes Affected Expression and Function of Murine REG Family Proteins." Current Developments in Nutrition 4, Supplement_2 (2020): 1850. http://dx.doi.org/10.1093/cdn/nzaa067_077.
Full textAbstract:
Abstract Objectives We previously revealed a substantially-suppressed expression of regenerating islets-derived protein 2 (Reg2) in murine pancreatic islets by overexpression of glutathione peroxidase-1 (Gpx1-OE). Two experiments were conducted to determine: 1) how knockouts of Gpx1 and superoxide dismutase-1 (Sod1) alone and together (dKO) affected the expression profiles of the full Reg family genes in three tissues; and 2) how GPX1 and SOD1 activities regulated effects of REG2 on islet proliferation. Methods In Expt. 1, six groups of mice (Gpx1−/−, Gpx1-OE, and their wild-type, WT1; Sod1−/−, dKO, and their WT2) (male, 2–4 months old (n = 6 – 8) were fed an Se-adequate diet and killed to collect islets, liver, and intestine samples. In Expt. 2, islets isolated from the 6 groups of mice were cultured in RPMI 1640 medium and treated with recombinant REG2 and REG2 mutant proteins (1 μg/mL), GPX mimic (ebselen, 50 μM) and SOD mimic (CuDIP, 10 μM) for 48 h. The proliferation of islets was estimated using the bromodeoxyuridine (Sigma) assay. Results Compared with the WT1 mice, the Gpx1−/− mice had greater (P < 0.05) and the Gpx1-OE mice had lower (P < 0.05) mRNA levels of all 7 assayed Reg genes with a few exceptions of Reg3ẞ,Reg3δ, or Reg4 in the three tissues. Similar inductions of the 7 Reg mRNA levels were also seen in the islets of Sod1−/− and dKO mice over their controls. However, responses of these 7 genes in the liver and intestine of these two genotypes in comparison with the controls were less consistent. The incubation of islets with REG2, but not the REG2 mutant, inhibited islet proliferation in the Gpx1−/−, Sod1−/−, dKO, and Gpx1-OE groups, where no such effect was seen in the two WT groups. Co-incubations of islets with CuDIP and ebselen partially blocked the REG2 inhibitory effect on the islet proliferation. Conclusions Altering GPX1 and SOD1 expression and activity affected the Reg family gene expression in the islets, liver, and intestine of mice as well as the function of REG2 protein in the islets. Our results reveal a novel dependence of the REG family protein expression and function on cellular redox status. Funding Sources This research was supported in an NIH grant DK 53,018.
7
Li, Bing, Xiao Wang, and Jun-Li Liu. "Pancreatic acinar-specific overexpression of Reg2 gene offered no protection against either experimental diabetes or pancreatitis in mice." American Journal of Physiology-Gastrointestinal and Liver Physiology 299, no. 2 (2010): G413—G421. http://dx.doi.org/10.1152/ajpgi.00500.2009.
Full textAbstract:
Reg proteins are normally expressed in pancreatic acinar cells, and the level of several of these proteins was significantly induced upon damage to the endocrine or exocrine pancreas. It has been established that Reg1 and pancreatic islet neogenesis-associated protein [INGAP, Reg3δ] promote the growth or regeneration of the endocrine islet cells. Recent reports suggest that Reg2 is an autoantigen normally expressed in islet β-cells. Reg2 overexpression in vitro offered protection to insulinoma cells. Overexpressed Reg3α increased cyclin D1 and CDK4 levels and the rate of proliferation in insulinoma cells. Acinar-specific overexpression of INGAP increased β-cell mass and protected the animals from streptozotocin-induced diabetes. Moreover, Reg2 gene expression was induced during pancreatitis. We hypothesized that Reg2 is a secreted protein that promotes the growth, survival, and/or regeneration of pancreatic endocrine and exocrine cells. To test its effectiveness, we used elastase-1 promoter (Ela-Reg2) to develop an acinar cell-specific overexpression of the Reg2 gene. Western blot analysis, real-time PCR, and immunohistochemistry revealed barely detectable levels of endogenous Reg2 in the pancreas of normal wild-type mice and increased Reg2 levels in the pancreas of Ela-Reg2 mice that were similar to or higher than Reg2 levels induced in experimental diabetes or pancreatitis. Compared with wild-type littermates, growth, blood glucose and insulin levels, and glucose tolerance were normal in Ela-Reg2 mice; pancreatic histology revealed no change in endocrine or exocrine tissues. Acinar-specific overexpression of the Reg2 gene offered no protection against streptozotocin-induced β-cell damage and diabetes, in hyperglycemia and weight loss, and no advantage in restoring glucose homeostasis and islet function within 3 mo. Furthermore, serum amylase level and pancreatic histochemistry showed that Reg2 overexpression did not protect acinar cells against caerulein-induced acute pancreatitis. In contrast to INGAP or Reg3β, exocrine overexpression of Reg2 offered no protection to the endocrine or exocrine pancreas, indicating clear subtype specificities of the Reg family of proteins.
8
Du, Shouying, Jean-Louis K. Kouadio, and Carl E. Bauer. "Regulated Expression of a Highly Conserved Regulatory Gene Cluster Is Necessary for Controlling Photosynthesis Gene Expression in Response to Anaerobiosis in Rhodobacter capsulatus." Journal of Bacteriology 181, no. 14 (1999): 4334–41. http://dx.doi.org/10.1128/jb.181.14.4334-4341.1999.
Full textAbstract:
ABSTRACT We utilized primer extension analysis to demonstrate that the divergently transcribed regB and senC-regA-hvrAtranscripts contain stable 5′ ends 43 nucleotides apart within theregB-senC intergenic region. DNA sequence analysis indicates that this region contains two divergent promoters with overlapping ς70 type −35 and −10 promoter recognition sequences. In vivo analysis of expression patterns ofregB::lacZ andsenC-regA-hvrA::lacZ reporter gene fusions demonstrates that the regB andsenC-regA-hvrA transcripts are both negatively regulated by the phosphorylated form of the global response regulator RegA. DNase I protection assays with a constitutively active variant of RegA indicate that RegA binds between regB and senCoverlapping −10 and −35 promoter recognition sequences. Two mutations were also isolated in a regB-deficient background that increased expression of the senC-regA-hvrA operon 10- and 5-fold, respectively. As a consequence of increased RegA expression, these mutants exhibited elevated aerobic and anaerobic photosynthesis (puf) gene expression, even in the absence of the sensor kinase RegB. These results indicate that autoregulation by RegA is a factor contributing to the maintenance of an optimal low level of RegA expression that allows responsiveness to activation by phosphorylation.
9
Frederick, D. L., and K. Tatchell. "The REG2 gene of Saccharomyces cerevisiae encodes a type 1 protein phosphatase-binding protein that functions with Reg1p and the Snf1 protein kinase to regulate growth." Molecular and Cellular Biology 16, no. 6 (1996): 2922–31. http://dx.doi.org/10.1128/mcb.16.6.2922.
Full textAbstract:
The GLC7 gene of Saccharomyces cerevisiae encodes the catalytic subunit of type 1 protein phosphatase (PP1) and is essential for cell growth. We have isolated a previously uncharacterized gene, REG2, on the basis of its ability to interact with Glc7p in the two-hybrid system. Reg2p interacts with Glc7p in vivo, and epitope-tagged derivatives of Reg2p and Glc7p coimmunoprecipitate from cell extracts. The predicted protein product of the REG2 gene is similar to Reg1p, a protein believed to direct PP1 activity in the glucose repression pathway. Mutants with a deletion of reg1 display a mild slow-growth defect, while reg2 mutants exhibit a wild-type phenotype. However, mutants with deletions of both reg1 and reg2 exhibit a severe growth defect. Overexpression of REG2 complements the slow-growth defect of a reg1 mutant but does not complement defects in glycogen accumulation or glucose repression, two traits also associated with a reg1 deletion. These results indicate that REG1 has a unique role in the glucose repression pathway but acts together with REG2 to regulate some as yet uncharacterized function important for growth. The growth defect of a reg1 reg2 double mutant is alleviated by a loss-of-function mutation in the SNF1-encoded protein kinase. The snf1 mutation also suppresses the glucose repression defects of reg1. Together, our data are consistent with a model in which Reg1p and Reg2p control the activity of PP1 toward substrates that are phosphorylated by the Snf1p kinase.
10
Singh, Bhagirath, Thomas Hill, Olga Krougly, et al. "Role of IL-22 in tissue regeneration in autoimmunity (P5164)." Journal of Immunology 190, no. 1_Supplement (2013): 195.11. http://dx.doi.org/10.4049/jimmunol.190.supp.195.11.
Full textAbstract:
Abstract The various cell types in our bodies are constantly regenerating but at a different rate. In autoimmune diseases cells once destroyed can regenerate. However, immune system once activated continues to target and destroy these cells. Thus, tissue regeneration remains a challenge in these diseases. Cytokines play a major role in immune regulation, inflammation, tissue injury and autoimmunity. We have shown that immunostimulation by mycobacterial adjuvants such as BCG vaccine as well as complete Freund’s adjuvant (CFA) can prevent the autoimmune process and can stimulate tissue regeneration. These adjuvants induce regulatory Th17 (Treg17) cells and stimulate expression of Regenerative (Reg) genes such as Reg1 and Reg2 in pancreatic islets. Th17 cells also produce Interleukin-22 (IL-22) that has been shown to stimulate This is probably mediated through STAT3/ERK signaling. Reg gene expression. Blocking of IL-22 prevented the expression of Reg genes in vivo. In this study we explored the cell types that express Reg genes following IL-22 treatment by using RT-PCR analysis and by histological staining. Our hypothesis is that the Reg gene expression drives the islet regeneration following tissue injury by autoimmunity in type 1 diabetes. These approaches offer alternatives to tissue transplantation in autoimmunity.