HUGO ID Detailed Result 9353


HUGO ID 9353
Symbol PRDX2
Name peroxiredoxin 2
#Occurrence 112
#Paper 2

 


PMID Match String Actual String Score Flanking text Edited by Edit
12909279PrPPrP1.1from copper bound to peptide A_amp_#x3b2 and to the protein PrP respectively has been provided 11 and 47 
12909279PrPPrP1.1would not be surprising to learn that copper-bound A_amp_#x3b2 and PrP are also able to induce the formation of the noxious 
14648077PRX2Prx23.91 (SOD1) SOD1 and a redox system including peroxiredoxin2 (Prx2, Prx2 thioredoxin peroxidase and glutathione peroxidase1 (GPx1): GPx1 SOD1 converts superoxide 
14648077PRX2Prx23.9(H H 2 O and oxygen (O O 2 by Prx2 and GPx1 that directly regulate the redox system 
14648077PRX2Prx23.9biological significance of the interaction of the redox system (Prx2/GPx1) Prx2 GPx1 with SOD1 in SOD1-mutated motor neurons in vivo we 
14648077PRX2Prx23.9neurons in vivo we produced an affinity-purified rabbit antibody against Prx2 and investigated the immunohistochemical localization of Prx2 and GPx1 in 
14648077PRX2Prx23.9rabbit antibody against Prx2 and investigated the immunohistochemical localization of Prx2 and GPx1 in neuronal Lewy body-like hyaline inclusions (LBHIs) LBHIs 
14648077PRX2Prx23.9SOD1-mutated FALS patients and transgenic rats showed identical immunoreactivities for Prx2 and GPx1 the reaction product deposits with the antibodies against 
14648077PRX2Prx23.9and GPx1 the reaction product deposits with the antibodies against Prx2 and GPx1 were localized in the LBHIs 
14648077PRX2Prx23.9addition the localizations of the immunoreactivities for SOD1 and Prx2/GPx1 Prx2 GPx1 were similar in the inclusions the co-aggregation of Prx2/GPx1 
14648077PRX2Prx23.9GPx1 were similar in the inclusions the co-aggregation of Prx2/GPx1 Prx2 GPx1 with SOD1 in neuronal LBHIs in mutant SOD1-related FALS 
14648077PRX2Prx23.9Based on the fact that Prx2/GPx1 Prx2 GPx1 directly regulates the redox system such co-aggregation of Prx2/GPx1 
14648077PRX2Prx23.9GPx1 directly regulates the redox system such co-aggregation of Prx2/GPx1 Prx2 GPx1 with SOD1 in neuronal LBHIs may lead to the 
14648077PRX2Prx23.9Peroxiredoxin2 (Prx2) Prx2 is a novel organ-specific antioxidative enzyme that is mainly expressed 
14648077PRX2Prx23.9Prx2 requires thioredoxin reductase (TR) TR as a secondary enzyme as 
14648077PRX2Prx23.9as cofactors to function at high efficiency the activity of Prx2 in the thioredoxin/TR/NADPH thioredoxin TR NADPH system is over five 
14648077PRX2Prx23.9NADPH system is over five times higher than that of Prx2 by itself 5 
14648077PRX2Prx23.9In this milieu Prx2 is also called thioredoxin peroxidase 1 (thioredoxin-dependent thioredoxin-dependent peroxide reductase 
14648077PRX2Prx23.9to controlling the intracellular content of H 2 O 2 Prx2 directly regulates the redox signals of the thioredoxin/TR/NADPH thioredoxin TR 
14648077PRX2Prx23.9Like Prx2 GPx1 needs glutathione reductase (GR) GR as a secondary enzyme 
14648077PRX2Prx23.9Therefore Prx2 and GPx1 directly control the redox system 
14648077PRX2Prx23.9motor neurons induce mutant and wild-type SOD1 as well as Prx2 and GPx1 
14648077PRX2Prx23.9Considering that Prx2 and GPx1 interact not only with wild-type SOD1 but also 
14648077PRX2Prx23.9SOD1 but also with mutant SOD1 the interaction of Prx2/GPx1 Prx2 GPx1 with SOD1 has been suggested to contribute to mutant 
14648077PRX2Prx23.9been suggested to contribute to mutant SOD1 aggregation toxicity Prx2/GPx1 Prx2 GPx1 possibly aggregate as LBHIs in SOD1-mutated motor neurons 
14648077PRX2Prx23.9Furthermore the aggregation of Prx2/GPx1 Prx2 GPx1 might affect the intracytoplasmic redox regulation and amplify mutant 
14648077PRX2Prx23.9To clarify the biological significance of the interaction of Prx2/GPx1 Prx2 GPx1 (redox redox system with SOD1 in SOD1-mutated motor neurons 
14648077PRX2Prx23.9motor neurons in vivo we first produced an antibody against Prx2 and analyzed the characteristic expressions of both Prx2 and GPx1 
14648077PRX2Prx23.9antibody against Prx2 and analyzed the characteristic expressions of both Prx2 and GPx1 in neuronal LBHIs in SOD1-mutated motor neurons of 
14648077PRX2Prx23.9Preparation of polyclonal antibody against Prx2 A synthetic peptide corresponding to the C-terminal region of Prx2 
14648077PRX2Prx23.9Prx2 A synthetic peptide corresponding to the C-terminal region of Prx2 (amino amino acids 184_amp_#x2013 198 NH 2 -KPNVDDSKEYFSKHN-COOH with or 
14648077PRX2Prx23.9of the C-terminal region of the human rat or mouse Prx2 
14648077PRX2Prx23.9To prepare immunogen 6 mg synthesized Prx2 peptide was conjugated with 6 mg keyhole limpet hemocyanin (KLH) 
14648077PRX2Prx23.9an affinity column of immobilized KLH conjugated with the synthetic Prx2 peptide as described previously 16 
14648077PRX2Prx23.9Fig 1 Specificity of antibody against Prx2 
14648077PRX2Prx23.9The immunoreactivity of the antibody to HSA-conjugated Prx2 peptide ( solid circles and native HSA ( open circles 
14648077PRX2Prx23.9The anti-Prx2 antibody recognizes the HSA-conjugated Prx2 peptide but does not react with HAS ( Prx2 peroxiredoxin2 
14648077PRX2Prx23.9HSA-conjugated Prx2 peptide but does not react with HAS ( Prx2 peroxiredoxin2 ELISA enzyme-linked immunosorbent assay HAS human serum albumin 
14648077PRX2Prx23.9following primary antibodies were utilized an affinity-purified rabbit antibody against Prx2 (concentration: concentration 1 _amp_micro;g/ml), _amp_micro g ml a polyclonal antibody 
14648077PRX2Prx23.9had been preabsorbed with an excess amount of the synthetic Prx2 peptide 
14648077PRX2Prx23.9Results We successfully produced an affinity-purified rabbit antibody against Prx2 peptide (amino amino acids 184_amp_#x2013 198 although this amino acid 
14648077PRX2Prx23.9of the human rat mouse Chinese hamster or Bos Taurus Prx2 this peptide does not share homology with other members of 
14648077PRX2Prx23.9This anti-Prx2 antibody recognized the HSA-conjugated Prx2 peptide but did not react with HSA (Fig Fig 1 
14648077PRX2Prx23.9Prx2 immunoreactivity in normal spinal cords was identified in almost all 
14648077PRX2Prx2-immunostaining3.3In addition Prx2-immunostaining was found throughout the neuropil with considerably lower intensity (Fig 
14648077PRX2Prx23.9With respect to the intracellular localization of Prx2 immunostaining of the neuronal cytoplasm and proximal dendrites was specifically 
14648077PRX2Prx23.9that had been pretreated with an excess of the synthetic Prx2 produced no staining (Fig Fig 3 D 
14648077PRX2Prx23.9B C Immunostaining for GPx1 ( B and Prx2 ( C 
14648077PRX2Prx23.9GPx1 and Prx2 immunoreactivities are found diffusely in the neuropil with considerably less 
14648077PRX2Prx23.9No counterstaining ( HE hematoxylin and eosin GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2 
14648077PRX2Prx23.9Fig 3 Detection of Prx2 and GPx1 in the normal motor neurons of the human 
14648077PRX2Prx23.9C Immunostaining with the antibody to Prx2 
14648077PRX2Prx23.9in the spinal cord co-express both GPx1 ( B and Prx2 ( C although their staining intensities in neurons vary 
14648077PRX2Prx23.9with anti-Prx2 antibody pretreated with an excess of the synthetic Prx2 peptide 
14648077PRX2Prx23.9F Prx2 immunostaining of the neuronal cytoplasm and proximal dendrites is observed 
14648077PRX2Prx23.9No counterstaining ( HE hematoxylin and eosin GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2 
14648077PRX2Prx23.9_amp_micro m A neuropil staining pattern similar to that for Prx2 was observed with GPx1 weak GPx1 immunoreactivity was diffusely seen 
14648077PRX2Prx23.9The stainability and intensity of Prx2 and GPx1 in the normal anterior horn cells of the 
14648077PRX2Prx23.9the normal motor neurons in the spinal cords co-expressed both Prx2 and GPx1 (Fig Fig 3 A_amp_#x2013 C although the staining 
14648077PRX2Prx23.9Most neuronal LBHIs were also immunoreactive for Prx2 although the intensity of Prx2 immunoreactivity in the LBHIs varied 
14648077PRX2Prx23.9LBHIs were also immunoreactive for Prx2 although the intensity of Prx2 immunoreactivity in the LBHIs varied (Figs Figs 4 C F 
14648077PRX2Prx23.9rats (H46R H46R and G93A showed a similar immunoreactivity for Prx2 
14648077PRX2Prx23.9The Prx2 immunolocalization in many intracytoplasmic and intraneuritic LBHIs was similar to 
14648077PRX2Prx23.9halo-type LBHIs the reaction product deposits of the antibody against Prx2 were generally restricted to the periphery (Fig Fig 4 C 
14648077PRX2Prx23.9In ill-defined LBHIs Prx2 immunostaining was distributed throughout each inclusion 
14648077PRX2Prx23.9In some inclusions however expression of Prx2 was observed in only part of the inclusion (Fig Fig 
14648077PRX2Prx23.9immunostaining in the neuronal LBHIs similar stainability and immunolocalization to Prx2 were confirmed in the core and halo types as well 
14648077PRX2Prx23.9Like Prx2 the immunolocalization of GPx1 was similar to that of SOD1 
14648077PRX2Prx23.9C Immunoreactivity for Prx2 
14648077PRX2Prx23.9Co-localization of the three proteins SOD1 GPx1 and Prx2 in the LBHI is evident 
14648077PRX2Prx23.9Immunostaining for SOD1 ( D GPx1 ( E and Prx2 ( F 
14648077PRX2Prx23.9Similar stainability and immunolocalization of SOD1 GPx1 and Prx2 in the LBHI are observed ( LBHI Lewy body-like hyaline 
14648077PRX2Prx23.9amyotrophic lateral sclerosis SOD1 superoxide dismutase 1 GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2 
14648077PRX2Prx23.9Immunostaining for SOD1 ( A GPx1 ( B and Prx2 ( C 
14648077PRX2Prx23.9Immunostaining for SOD1 ( D GPx1 ( E and Prx2 ( F 
14648077PRX2Prx23.9Immunostaining GPx1 ( E and Prx2 ( F are observed in only part of the SOD1-positive 
14648077PRX2Prx23.9amyotrophic lateral sclerosis SOD1 superoxide dismutase 1 GPx1 glutathione peroxidase1 Prx2 peroxiredoxin2 
14648077PRX2Prx23.9H46R mutation immunostained with antibodies against SOD1 ( A and Prx2 ( B 
14648077PRX2Prx23.9LBHIs in the neuropil are positive for both SOD1 and Prx2 ( arrows ( SOD1 superoxide dismutase1 LBHI Lewy body-like hyaline 
14648077PRX2Prx23.9arrows ( SOD1 superoxide dismutase1 LBHI Lewy body-like hyaline inclusion Prx2 peroxiredoxin2 
14648077PRX2Prx23.9_amp_micro m Noticeably the co-localization of the three proteins SOD1 Prx2 and GPx1 in neuronal LBHIs in SOD1-mutated FALS patients and 
14648077PRX2Prx23.9LBHIs the precise intra-inclusional immunolocalizations of the three proteins differed Prx2 (Fig Fig 5 D F and GPx1 (Fig Fig 5 
14648077PRX2Prx23.9Discussion Under normal physiological conditions Prx2 and GPx1 immunoreactivities in the spinal cord anterior horns in 
14648077PRX2Prx23.933 intranuclear localization in some neurons is also observed in Prx2 immunostaining 
14648077PRX2Prx23.9Considering that endogenous Prx2 and GPx1 within the neuronal cytoplasm are extremely effective regulators 
14648077PRX2Prx23.9almost all of the normal spinal motor neurons co-expressed both Prx2 and GPx1 confirms that these motor neurons maintain themselves using 
14648077PRX2Prx23.9that these motor neurons maintain themselves using the intracellular Prx2/GPx1 Prx2 GPx1 system that is the redox system 
14648077PRX2Prx23.9Intense co-expression of SOD1 Prx2 and GPx1 in neuronal LBHIs in both diseases was evident 
14648077PRX2Prx23.9mutant/wild-type mutant wild-type SOD1 as an antioxidant system and Prx2/GPx1 Prx2 GPx1 as a redox system 
14648077PRX2Prx23.9In this in vivo milieu where mutant SOD1 exists Prx2 and GPx1 would aberrantly interact with the mutant SOD1 which 
14648077PRX2Prx23.9the facts that there are neuronal LBHIs positive for SOD1 Prx2 and GPx1 in the milieu where mutant SOD1 exists but 
14648077PRX2Prx23.9physiological conditions our study demonstrates an aberrant interaction of Prx2/GPx1 Prx2 GPx1 with mutant SOD1 the aggregation of which results in 
14648077PRX2Prx23.9In addition intra-inclusional co-aggregation of Prx2/GPx1 Prx2 GPx1 with mutant SOD1 causes the intracytoplasmic reduction of Prx2/GPx1, 
14648077PRX2Prx23.9GPx1 with mutant SOD1 causes the intracytoplasmic reduction of Prx2/GPx1, Prx2 GPx1 thereby reducing the availability of the redox system 
14648077PRX2Prx23.9with the aberrant interaction of cytotoxic mutant SOD1 with Prx2/GPx1 Prx2 GPx1 directly regulating a redox system our finding leads us 
14648077PRX2Prx23.9leads us to speculate that not only co-aggregation of Prx2/GPx1 Prx2 GPx1 and SOD1 into LBHIs but also intracytoplasmic reduction of 
14648077PRX2Prx23.9and SOD1 into LBHIs but also intracytoplasmic reduction of Prx2/GPx1 Prx2 GPx1 in both diseases may partly contribute to the breakdown 
14648077PRX2Prx23.9remains to be determined whether this aberrant interaction of Prx2/GPx1 Prx2 GPx1 with mutant SOD1 is a direct or an indirect 
14648077PRX2Prx23.9on the pathogenesis of SOD1-mutated FALS disease itself or whether Prx2 and GPx1 play a primary or a secondary role to 
14648077PRX2Prx23.9to emphasize that the aberrant interaction and co-aggregation of Prx2/GPx1 Prx2 GPx1 and SOD1 (probably probably Prx2/GPx1 Prx2 GPx1 and mutant 
14648077PRX2Prx23.9co-aggregation of Prx2/GPx1 Prx2 GPx1 and SOD1 (probably probably Prx2/GPx1 Prx2 GPx1 and mutant SOD1 in FALS patients with SOD1 gene 
14648077peroxiredoxin 2peroxiredoxin21.0to protect themselves from these ross the cells have developed both an antioxidant system containing superoxide dismutase 1 sod1 and a redox system including peroxiredoxin2 prx2 thioredoxin peroxidase and glutathione peroxidase1 gpx1 : sod1 converts superoxide radicals into hydrogen peroxide h 2 o 2 and h 2 o 2 is then converted into harmless water h 2 o and oxygen o 2  
14648077peroxiredoxin 2peroxiredoxin 21.0keywords peroxiredoxin 2 glutathione peroxidase 1 redox system superoxide dismutase 1 familial amyotrophic lateral sclerosis  
14648077peroxiredoxin 2peroxiredoxin21.0peroxiredoxin2 prx2 is a novel organ specific antioxidative enzyme that is mainly expressed in mammalian brain [ 23 ].  
14648077thioredoxin-dependent peroxide reductase 1thioredoxin dependent peroxide reductase 11.0in this milieu prx2 is also called thioredoxin peroxidase 1 thioredoxin dependent peroxide reductase 1 or thiol specific antioxidant [ 4 5 6 ].  
14648077thioredoxin peroxidase 1thioredoxin peroxidase 11.0in this milieu prx2 is also called thioredoxin peroxidase 1 thioredoxin dependent peroxide reductase 1 or thiol specific antioxidant [ 4 5 6 ].  
14648077peroxiredoxin 2peroxiredoxin21.0the anti prx2 antibody recognizes the hsa conjugated prx2 peptide but does not react with has prx2 peroxiredoxin2 elisa enzyme linked immunosorbent assay has human serum albumin  
14648077peroxiredoxin 2peroxiredoxin21.0no counterstaining he hematoxylin and eosin gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .  
14648077peroxiredoxin 2peroxiredoxin21.0b _amp_#x2013; f no counterstaining he hematoxylin and eosin gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .  
14648077peroxiredoxin 2peroxiredoxin21.0lization of sod1 gpx1 and prx2 in the lbhi are observed lbhi lewy body like hyaline inclusion fals familial amyotrophic lateral sclerosis sod1 superoxide dismutase 1 gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .  
14648077peroxiredoxin 2peroxiredoxin21.0hese three proteins differ from each other in this lbhi lbhi lewy body like hyaline inclusion fals familial amyotrophic lateral sclerosis sod1 superoxide dismutase 1 gpx1 glutathione peroxidase1 prx2 peroxiredoxin2 .  
14648077peroxiredoxin 2peroxiredoxin21.0round and sausage like lbhis in the neuropil are positive for both sod1 and prx2 arrows sod1 superoxide dismutase1 lbhi lewy body like hyaline inclusion prx2 peroxiredoxin2 .