DOCSLIB.ORG

SUPPLEMENTARY DATA Data Supplement To

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

SUPPLEMENTARY DATA Data supplement to Perivascular adipose tissue controls insulin-stimulated perfusion, mitochondrial protein expression and glucose uptake in muscle through adipomuscular microvascular anastomoses Surname first author Turaihi Authors & Affiliations Turaihi, Alexander H MD1; Serné, Erik H, MD PhD2; Molthoff, Carla FM PhD3; Koning, Jasper J PhD4; Knol, Jaco PhD6; Niessen, Hans W MD PhD5; Goumans, Marie Jose TH PhD7; van Poelgeest, Erik M MD1; Yudkin, John S MD PhD8; Smulders, Yvo M MD PhD2; Connie R Jimenez, PhD6; van Hinsbergh, Victor WM PhD1; Eringa, Etto C PhD1 ©2020 American Diabetes Association. Published online at http://diabetes.diabetesjournals.org/lookup/suppl/doi:10.2337/db18-1066/-/DC1 SUPPLEMENTARY DATA Western immunoblotting Skeletal muscle samples were lysed up in 1D‐sample buffer (10% glycerol, 62.5 mmol/L Tris (pH 6.8), 2% w/v LDS, 2% w/v DTT) and protein concentration was determined using Pierce 660‐nm protein assay (Thermo scientific, Waltham, MA USA 02 451; 22 660) according to the manufacturer's instructions. Heat shock protein 90 immunoblotting was performed by application of samples (5 µg protein) on 4‐15% Criterion TGX gels (Biorad, Veenendaal, the Netherlands, 5 671 084) and semi‐dry blotting onto PVDF membranes (GE Healthcare‐Fisher, RPN1416F), incubated overnight with rat monoclonal HSP90 antibody (1:1000 dilution) after blocking with 5% milk in TBS‐T (137 mM NaCl, 20 mmol/L Tris pH 7.0 and 0.1% (v/v) Tween [Sigma‐Aldrich, P7949]). After 2 hours incubation with anti-rat, horse radish peroxidase-coupled secondary antibody (Thermo Fisher 62-9520), the blot was stained using ECL‐prime (Fisher scientific, 10 308 449) and analysed on an AI‐600 imaging system (GE Healthcare, Life Sciences). Four samples from each group were loaded on gel. Supplementary Table 1. Body weight and glucose infusion rate (GIR) in all groups. Body weight (g) Glucose infusion rate (µmol/Kg/min) Intact (Saline infusion) 20.8 ± 1.5 NA Intact (Insulin infusion) 22 ± 0.4 180.2 ± 19.8 PVAT Removed 21.2 ± 0.4 203.8 ± 21.4 Sham 22 ± 0.8 201.7 ± 21.4 PVAT Disconnected 21.8 ± 1.7 215.9 ± 50.8 ©2020 American Diabetes Association. Published online at http://diabetes.diabetesjournals.org/lookup/suppl/doi:10.2337/db18-1066/-/DC1 SUPPLEMENTARY DATA Supplementary Table 2. Proteins upregulated in muscles without PVAT compared to muscles with PVAT. Control Control No PVAT No PVAT Fold UniProt Symbol Protein Name P-value Mean SD Mean SD increase P27612 Plaa Phospholipase A-2-activating protein 0.0 0.0 1.9 1.2 >10 0.001 Q8BVZ5 Il33 Interleukin-33 0.0 0.0 1.2 1.1 >10 0.013 Q5XKN4 Jagn1 Protein jagunal homolog 1 0.0 0.0 0.8 0.8 >10 0.038 Q8BY89-2 Slc44a2 Choline transporter-like protein 2 0.3 0.5 1.7 1.4 6.7 0.035 Q9D154 Serpinb1a Leukocyte elastase inhibitor A 2.3 3.9 5.2 2.2 2.2 0.042 Q64727 Vcl Vinculin 7.6 2.5 15.2 6.1 2.0 0.020 P02469 Lamb1 Laminin subunit beta-1 5.5 2.6 9.7 2.8 1.8 0.030 P01966 Hba-x Hemoglobin subunit zeta 5.6 1.2 13.0 5.8 2.3 0.014 P15327 Bpgm Bisphosphoglycerate mutase 2.6 1.3 5.6 0.8 2.1 0.035 P01942 Hba-a1 Hemoglobin subunit alpha 86.6 20.2 136.1 38.0 1.6 0.015 Q61316 Hspa4 Heat shock protein 70 kDa 4 1.5 1.8 4.5 2.3 2.9 0.029 P11499 Hsp90ab1 Heat shock protein HSP 90-beta 56.5 6.2 77.3 13.6 1.4 0.008 Q80XI4 Pip4k2b Phosphatidylinositol 5-phosphate 4-kinase type-2 beta 0.0 0.0 0.8 0.8 >10 0.038 P35283 Rab12 Ras-related protein Rab-12 0.3 0.6 1.7 0.4 6.2 0.026 P16332 Mut Methylmalonyl-CoA mutase, mitochondrial 0.3 0.5 2.4 1.7 9.5 0.010 Q9D8S9 Bola1 BolA-like protein 1 0.8 1.0 2.7 1.5 3.5 0.035 Q6PB66 Lrpprc Leucine-rich PPR motif-containing protein, mitochondrial 3.4 3.3 7.2 3.1 2.1 0.047 Q99LY9 Ndufs5 NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 6.8 4.0 13.5 5.1 2.0 0.029 Q9Z1P6 Ndufa7 NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 18.3 8.1 29.8 5.6 1.6 0.015 Q9CQZ5 Ndufa6 NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 10.5 2.9 15.5 3.1 1.5 0.046 Q9CQC7 Ndufb4 NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 14.2 2.2 20.2 4.3 1.4 0.035 O88441 Mtx2 Metaxin-2 0.5 0.6 2.6 1.4 5.1 0.013 Q8K0D5 Gfm1 Elongation factor G, mitochondrial 0.0 0.0 1.5 1.0 >10 0.004 Q99KK7 Dpp3 Dipeptidyl peptidase 3 0.0 0.0 1.5 0.9 >10 0.003 P46460 Nsf Vesicle-fusing ATPase 0.0 0.0 1.9 1.1 >10 0.002 Q9ESX5 Dkc1 H/ACA ribonucleoprotein complex subunit 4 0.0 0.0 1.0 0.7 >10 0.020 P57759 Erp29 Endoplasmic reticulum resident protein 29 0.0 0.0 0.9 1.0 >10 0.023 Q99JT9 Adi1 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 0.0 0.0 0.8 0.4 >10 0.037 P62908 Rps3 40S ribosomal protein S3 1.8 1.0 4.6 2.2 2.5 0.029 P58252 Eef2 Elongation factor 2 24.8 2.6 36.4 1.9 1.5 0.002 ©2020 American Diabetes Association. Published online at http://diabetes.diabetesjournals.org/lookup/suppl/doi:10.2337/db18-1066/-/DC1 SUPPLEMENTARY DATA Q8BL97-3 Srsf7 Serine/arginine-rich splicing factor 7 0.0 0.0 0.8 0.4 >10 0.037 D3Z4S3 Ptrhd1 Putative peptidyl-tRNA hydrolase PTRHD1 0.0 0.0 1.1 0.4 >10 0.011 Q9DCS2 Mettl26 Methyltransferase-like 26 0.0 0.0 0.9 1.0 >10 0.023 Q9D024-2 Ccdc47 Coiled-coil domain-containing protein 47 0.0 0.0 1.0 1.0 >10 0.023 P68254 Ywhaq 14-3-3 protein theta 0.3 0.5 1.7 1.0 6.6 0.027 Q60972 Rbbp4 Histone-binding protein RBBP4 0.3 0.5 1.5 0.9 5.9 0.043 Q3UHX2 Pdap1 28 kDa heat- and acid-stable phosphoprotein 1.1 0.0 3.6 1.5 3.4 0.013 P08074 Cbr2 Carbonyl reductase [NADPH] 2 1.0 2.1 3.4 2.7 3.3 0.049 O08529 Capn2 Calpain-2 catalytic subunit 2.1 2.4 5.5 2.5 2.7 0.032 P56812 Pdcd5 Programmed cell death protein 5 2.2 1.6 5.7 1.2 2.7 0.007 P28653 Bgn Biglycan 3.3 4.0 8.5 4.0 2.5 0.031 Q8BVI4 Qdpr Dihydropteridine reductase 5.2 3.7 11.4 3.9 2.2 0.019 Q9DAK9 Phpt1 14 kDa phosphohistidine phosphatase 7.0 3.7 11.7 1.9 1.7 0.030 Q9R062 Gyg Glycogenin-1 9.0 2.4 14.2 1.8 1.6 0.026 Q99PT1 Arhgdia Rho GDP-dissociation inhibitor 1 9.5 1.6 14.7 2.9 1.6 0.029 ©2020 American Diabetes Association. Published online at http://diabetes.diabetesjournals.org/lookup/suppl/doi:10.2337/db18-1066/-/DC1 SUPPLEMENTARY DATA Supplementary Table 3. Proteins downregulated in muscles without PVAT compared to muscles with PVAT. Control Control No PVAT No PVAT Fold UniProt Symbol Protein Name P-value Mean SD Mean SD Decrease P50136 Bckdha 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial 1.6 1.3 0.0 0.0 >10 0.004 Q9CRA7 Atp5s ATP synthase subunit s, mitochondrial 1.0 0.8 0.0 0.0 >10 0.009 Q8BYM8 Cars2 Probable cysteine--tRNA ligase, mitochondrial 0.8 1.0 0.0 0.0 >10 0.032 Q8VD26-3 Tmem143 Transmembrane protein 143 0.8 1.0 0.0 0.0 >10 0.033 Q91WU5 As3mt Arsenite methyltransferase 0.8 1.0 0.0 0.0 >10 0.033 Q9DC61 Pmpca Mitochondrial-processing peptidase subunit alpha 2.1 0.8 0.6 0.5 3.6 0.043 P56379 Atp5mpl 6.8 kDa mitochondrial proteolipid 11.8 4.2 5.4 1.7 2.2 0.004 Q3ULD5 Mccc2 Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial 10.2 3.5 4.8 1.0 2.1 0.005 Q8R404 2410015M20Rik Protein QIL1 7.8 3.7 3.8 0.8 2.0 0.018 P43023 Cox6a2 Cytochrome c oxidase subunit 6A2, mitochondrial 7.3 3.3 3.9 1.4 1.9 0.033 P99028 Uqcrh Cytochrome b-c1 complex subunit 6, mitochondrial 8.7 1.5 4.6 1.5 1.9 0.018 P56135 Atp5j2 ATP synthase subunit f, mitochondrial 25.0 4.7 15.0 2.5 1.7 0.002 Q7TMF3 Ndufa12 NADH dehydrogenase alpha subcomplex subunit 12 30.1 3.3 19.2 1.3 1.6 0.002 Q8BFR5 Tufm Elongation factor Tu, mitochondrial 25.3 4.3 18.7 3.4 1.4 0.041 Q06185 Atp5k ATP synthase subunit e, mitochondrial 27.9 4.8 20.6 3.6 1.4 0.031 Q9CPQ8 Atp5l ATP synthase subunit g, mitochondrial 21.4 1.5 14.2 2.2 1.5 0.012 P56391 Cox6b1 Cytochrome c oxidase subunit 6B1 29.3 1.8 22.2 1.5 1.3 0.042 Q9D855 Uqcrb Cytochrome b-c1 complex subunit 7 64.8 7.1 50.4 6.3 1.3 0.008 P62897 Cycs Cytochrome c, somatic 94.9 17.0 75.8 7.5 1.3 0.024 Q9DCX2 Atp5h ATP synthase subunit d, mitochondrial 48.7 9.4 39.5 2.5 1.2 0.042 Q9CPQ1 Cox6c Cytochrome c oxidase subunit 6C 76.8 6.2 63.7 5.0 1.2 0.022 Q9R0Y5 Ak1 Adenylate kinase isoenzyme 1 111.2 9.1 89.5 11.5 1.2 0.007 P19536 Cox5b Cytochrome c oxidase subunit 5B, mitochondrial 71.6 11.4 60.5 4.2 1.2 0.048 O88653 Lamtor3 Regulator complex protein LAMTOR3 0.8 0.5 0.0 0.0 >10 0.023 Q9Z2P8 Vamp5 Vesicle-associated membrane protein 5 2.4 1.0 0.6 0.9 4.2 0.022 Q91WS0 Cisd1 CDGSH iron-sulfur domain-containing protein 1 41.8 9.9 29.9 3.0 1.4 0.011 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit P62874 Gnb1 1.0 1.4 0.0 0.0 >10 0.037 beta-1 Q9Z0Y1 Dctn3 Dynactin subunit 3 1.6 1.3 0.2 0.4 8.0 0.027 O08539-2 Bin1 Myc box-dependent-interacting protein 1 42.0 4.0 33.5 2.6 1.3 0.045 P40142 Tkt Transketolase 8.2 2.9 4.0 1.8 2.1 0.017 P14824 Anxa6 Annexin A6 91.5 9.2 73.6 12.7 1.2 0.025 P47199 Cryz Quinone oxidoreductase 1.9 1.0 0.2 0.4 10.2 0.009 ©2020 American Diabetes Association.
Recommended publications
  • Table 1. Identified Proteins with Expression Significantly Altered in the Hippocampus of Rats of Exposed Group (Pb) Vs

    Table 1. Identified Proteins with Expression Significantly Altered in the Hippocampus of Rats of Exposed Group (Pb) Vs

    Table 1. Identified proteins with expression significantly altered in the hippocampus of rats of exposed group (Pb) vs. Control. Fold Change Accession Id a Protein Description Score Pb P35213 14-3-3 protein beta/alpha 85420 −0.835 P62260 14-3-3 protein epsilon 96570 −0.878 P68511 14-3-3 protein eta 85420 −0.844 P68255 14-3-3 protein theta 85420 −0.835 P63102 14-3-3 protein zeta/delta 105051 −0.803 P13233 2',3'-cyclic-nucleotide 3'-phosphodiesterase 151400 1.405 P68035 Actin, alpha cardiac muscle 1 442584 −0.942 P68136 Actin, alpha skeletal muscle 441060 −0.970 P62738 Actin, aortic smooth muscle 438270 −0.970 P60711 Actin, cytoplasmic 1 630104 −0.942 P63259 Actin, cytoplasmic 2 630104 −0.942 P63269 Actin, gamma-enteric smooth muscle 438270 −0.951 Q05962 ADP/ATP translocase 1 60100 −0.554 Q09073 ADP/ATP translocase 2 49102 −0.482 P84079 ADP-ribosylation factor 1 34675 −0.644 P84082 ADP-ribosylation factor 2 22412 −0.644 P61206 ADP-ribosylation factor 3 34675 −0.619 P61751 ADP-ribosylation factor 4 22412 −0.670 P84083 ADP-ribosylation factor 5 22412 −0.625 P04764 Alpha-enolase 46219 −0.951 P23565 Alpha-internexin 9478 1.062 P37377 Alpha-synuclein 89619 −0.771 P13221 Aspartate aminotransferase, cytoplasmic 23661 1.083 P00507 Aspartate aminotransferase, mitochondrial 46049 1.116 P10719 ATP synthase subunit beta, mitochondrial 232442 −0.835 P85969 Beta-soluble NSF attachment protein 9638 1.419 Q63754 Beta-synuclein 66842 −0.779 P11275 Calcium/calmodulin-dependent protein kinase type II subunit alpha 181954 1.105 P08413 Calcium/calmodulin-dependent protein kinase type II subunit beta 80840 1.127 P15791 Calcium/calmodulin-dependent protein kinase type II subunit delta 62682 1.105 Int.
  • The Role of Methemoglobin and Carboxyhemoglobin in COVID-19: a Review

    The Role of Methemoglobin and Carboxyhemoglobin in COVID-19: a Review

    Journal of Clinical Medicine Review The Role of Methemoglobin and Carboxyhemoglobin in COVID-19: A Review Felix Scholkmann 1,2,*, Tanja Restin 2, Marco Ferrari 3 and Valentina Quaresima 3 1 Biomedical Optics Research Laboratory, Department of Neonatology, University Hospital Zurich, University of Zurich, 8091 Zurich, Switzerland 2 Newborn Research Zurich, Department of Neonatology, University Hospital Zurich, University of Zurich, 8091 Zurich, Switzerland; [email protected] 3 Department of Life, Health and Environmental Sciences, University of L’Aquila, 67100 L’Aquila, Italy; [email protected] (M.F.); [email protected] (V.Q.) * Correspondence: [email protected]; Tel.: +41-4-4255-9326 Abstract: Following the outbreak of a novel coronavirus (SARS-CoV-2) associated with pneumonia in China (Corona Virus Disease 2019, COVID-19) at the end of 2019, the world is currently facing a global pandemic of infections with SARS-CoV-2 and cases of COVID-19. Since severely ill patients often show elevated methemoglobin (MetHb) and carboxyhemoglobin (COHb) concentrations in their blood as a marker of disease severity, we aimed to summarize the currently available published study results (case reports and cross-sectional studies) on MetHb and COHb concentrations in the blood of COVID-19 patients. To this end, a systematic literature research was performed. For the case of MetHb, seven publications were identified (five case reports and two cross-sectional studies), and for the case of COHb, three studies were found (two cross-sectional studies and one case report). The findings reported in the publications show that an increase in MetHb and COHb can happen in COVID-19 patients, especially in critically ill ones, and that MetHb and COHb can increase to dangerously high levels during the course of the disease in some patients.
  • Mitochondrial Cytochrome C Oxidase As a Target Site for Daunomycin in K-562 Cells and Heart Tissue1

    Mitochondrial Cytochrome C Oxidase As a Target Site for Daunomycin in K-562 Cells and Heart Tissue1

    [CANCER RESEARCH 53. 1072-1078. March I. 1993] Mitochondrial Cytochrome c Oxidase as a Target Site for Daunomycin in K-562 Cells and Heart Tissue1 Lefkothea C. Papadopoulou and Asterios S. Tsiftsoglou2 iMhoratory of Pharmacology, Department of Pharmaceutical Sciences. Aristotle University' of Thesstiloniki. Thesstiloniki 540 (Ì6,Greece ABSTRACT cells like ADR (20); (/;) DAU interacts selectively with mitochondrial COX; these interactions appear to be specific in nature and may occur Daunomycin and other structurally related anthracyclines can cause in part via the prosthetic group of heme located in two of the several myelosuppression and cardiomyopathy. We explored the possible mecha- nism(s) by which daunomycin (DAU) interacts with target sites in neo- subunits of this enzyme; (c) DAU and ADR inhibited COX activity in plastic hemopoietic cells and heart tissue. We observed that | 'lli(. i|l) VI a dose-dependent fashion that was prevented by exogenously added interacts selectively with mitochondria! hemoproteins isolated from K-562 hemin. In light of these observations, we propose that mitochondrial cells and rat and bovine heart and forms relatively stable protein com COX may serve as a target site for DAU and presumably other plexes. Isolation, purification, and Chromatographie analysis of the mito anthracyclines on highly proliferating neoplastic cells and heart tissue. chondria! components complexed with [JH(G)]DAU revealed that one of the major components involved is cytochrome c oxidase (COX). Both DAU and ADR caused a dose-dependent inhibition of COX activity in vitro, an MATERIALS AND METHODS event prevented by exogenous hemin. The interaction of DAL with COX Chemicals and Biologicals. Hemin was purchased from Eastman Kodak appears to occur via more than one site, one of which at least appears to (Rochester.
  • Diabetes-Induced Mitochondrial Dysfunction in the Retina

    Diabetes-Induced Mitochondrial Dysfunction in the Retina

    Diabetes-Induced Mitochondrial Dysfunction in the Retina Renu A. Kowluru and Saiyeda Noor Abbas 4–9 PURPOSE. Oxidative stress is increased in the retina in diabetes, tase are downregulated. We have reported that the long- and antioxidants inhibit activation of caspase-3 and the devel- term administration of antioxidants inhibits the development opment of retinopathy. The purpose of this study was to of retinopathy in diabetic rats and in galactose-fed rats (another investigate the effect of diabetes on the release of cytochrome model of diabetic retinopathy),3 suggesting an important role c from mitochondria and translocation of Bax into mitochon- for oxidative stress in the development of retinopathy in dia- dria in the rat retina and in the isolated retinal capillary cells. betes. Oxidative stress is involved directly in the upregulation ETHODS of vascular endothelial growth factor in the retina during early M . Mitochondria and cytosol fractions were prepared 10 from retina of rats with streptozotocin-induced diabetes and diabetes. Recent studies from our laboratory have shown that from the isolated retinal endothelial cells and pericytes incu- oxidative stress plays an important role, not only in the devel- opment of retinopathy in diabetes, but also in the resistance of bated in 5 or 20 mM glucose medium for up to 10 days in the 11 presence of superoxide dismutase (SOD) or a synthetic mi- retinopathy to arrest after good glycemic control is initiated. metic of SOD (MnTBAP). The release of cytochrome c into the Capillary cells and neurons are lost in the retina before other histopathology is detectable, and apoptosis has been cytosol and translocation of the proapoptotic protein Bax into 12–15 the mitochondria were determined by the Western blot tech- implicated as one of the mechanism(s).
  • Iron Deficiency in the Rat: Effects on Neutrophil Activation and Metabolism

    Iron Deficiency in the Rat: Effects on Neutrophil Activation and Metabolism

    THEOPHYLLINE AND BRAIN 549 A dietary protein deficiency can affect the susceptibility to the metabolism in children with protein-calorie malnutrition. Am. J. Clin. Nutr., 28: 977 (1975). toxicity of drugs or other agents such as pesticides and herbicides 8. Nakamoto. T. and Miller. S. A.: Effect of vrotein-energy malnutrition on the (2). At the present time, there are no such studies relative to growth df mandible aid long bone in newborn miie and female rats. J. theophylline, although the usage of theophylline is now quite Nutr., 107: 983 (1977). common in the neonatal intensive care environment. Many 9. Nebron, R. M., Resnick, M. D., and Halstmm, W. J.: Developmental outcome of premature infants treated with theophylline. Dev. Pharmacol. Ther., 1: infants therein who are now receiving theophylline therapeuti- 274 ( 1980). cally are being dosed on a body weight basis without considera- 10. Newberne, P. M., Gross, R. L., and Roe, D. A,: Dmg, toxin, nutrient interac- tion of the nutritional status. Our data suggest that, in the animal tions. World Rev. Nutr. Diet., 29: 130 (1978). model, the administration of theophylline in the presence of a 1 I. Pastorova, B., Sova, O., and Burda, J.: Incorporation of I4C-thymidine into liver and brain DNA of protein-deficient rats. Physiol. Bohemoslov., 27: 69 compromised nutritional status may have effects not now appar- (1978). ent. We add our concern to that expressed by others (16) that 12. Prasad, A. S., Dumouchell, E., Kovich, D., and Oberleas, D.: A simple methylxanthine administration may have previously unsus- fluorometric method for the determination of RNA and DNA in tissue.
  • Concentration of NADH-Cytochrome B5 Reductase in Erythrocytes of Normal and Methemoglobinemic Individuals Measured with a Quantitative Radioimmunoblotting Assay

    Concentration of NADH-Cytochrome B5 Reductase in Erythrocytes of Normal and Methemoglobinemic Individuals Measured with a Quantitative Radioimmunoblotting Assay

    Concentration of NADH-cytochrome b5 reductase in erythrocytes of normal and methemoglobinemic individuals measured with a quantitative radioimmunoblotting assay. N Borgese, … , G Pietrini, S Gaetani J Clin Invest. 1987;80(5):1296-1302. https://doi.org/10.1172/JCI113205. Research Article The activity of NADH-cytochrome b5 reductase (NADH-methemoglobin reductase) is generally reduced in red cells of patients with recessive hereditary methemoglobinemia. To determine whether this lower activity is due to reduced concentration of an enzyme with normal catalytic properties or to reduced activity of an enzyme present at normal concentration, we measured erythrocyte reductase concentrations with a quantitative radioimmunoblotting method, using affinity-purified polyclonal antibodies against rat liver microsomal reductase as probe. In five patients with the "mild" form of recessive hereditary methemoglobinemia, in which the activity of erythrocyte reductase was 4-13% of controls, concentrations of the enzyme, measured as antigen, were also reduced to 7-20% of the control values. The concentration of membrane-bound reductase antigen, measured in the ghost fraction, was similarly reduced. Thus, in these patients, the reductase deficit is caused mainly by a reduction in NADH-cytochrome b5 reductase concentration, although altered catalytic properties of the enzyme may also contribute to the reduced enzyme activity. Find the latest version: https://jci.me/113205/pdf Concentration of NADH-Cytochrome b5 Reductase in Erythrocytes of Normal and Methemoglobinemic
  • Chain of Human Neutrophil Cytochrome B CHARLES A

    Chain of Human Neutrophil Cytochrome B CHARLES A

    Proc. Nati. Acad. Sci. USA Vol. 85, pp. 3319-3323, May 1988 Biochemistry Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b CHARLES A. PARKOS*, MARY C. DINAUERt, LESLIE E. WALKER*, RODGER A. ALLEN*, ALGIRDAS J. JESAITIS*, AND STUART H. ORKINtt *Department of Immunology, Research Institute of the Scripps Clinic, La Jolla, CA 92037; tDivision of Hematology-Oncology, Children's Hospital, and Dana-Farber Cancer Institute, Department of Pediatrics, Harvard Medical School, Boston, MA 02115; and tHoward Hughes Medical Institute, Children's Hospital, Boston, MA 02115 Communicated by Harvey F. Lodish, January 14, 1988 ABSTRACT Cytochrome b comprising 91-kDa and 22- Cytochrome b purified from neutrophil membranes ap- kDa subunits is a critical component of the membrane-bound pears to be a heterodimer of a glycosylated 91-kDa heavy oxidase of phagocytes that generates superoxide. This impor- chain and a nonglycosylated 22-kDa light chain (10-12). The tant microbicidal system is impaired in inherited disorders 91-kDa subunit is encoded by a gene designated CGD, known as chronic granulomatous disease (CGD). Previously we residing at chromosomal position Xp2l, which originally was determined the sequence of the larger subunit from the cDNA identified on the basis of genetic linkage without reference to of the CGD gene, the X chromosome locus affected in "X- a specific protein product (8). Antisera generated to either a linked" CGD. To complete the primary structure of the synthetic peptide predicted from the cDNA or to a fusion cytochrome b and to assess expression of the smaller subunit, protein produced in E.
  • Table S1. Identified Proteins with Exclusive Expression in Cerebellum of Rats of Control, 10Mg F/L and 50Mg F/L Groups

    Table S1. Identified Proteins with Exclusive Expression in Cerebellum of Rats of Control, 10Mg F/L and 50Mg F/L Groups

    Table S1. Identified proteins with exclusive expression in cerebellum of rats of control, 10mg F/L and 50mg F/L groups. Accession PLGS Protein Name Group IDa Score Q3TXS7 26S proteasome non-ATPase regulatory subunit 1 435 Control Q9CQX8 28S ribosomal protein S36_ mitochondrial 197 Control P52760 2-iminobutanoate/2-iminopropanoate deaminase 315 Control Q60597 2-oxoglutarate dehydrogenase_ mitochondrial 67 Control P24815 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 84 Control Q99L13 3-hydroxyisobutyrate dehydrogenase_ mitochondrial 114 Control P61922 4-aminobutyrate aminotransferase_ mitochondrial 470 Control P10852 4F2 cell-surface antigen heavy chain 220 Control Q8K010 5-oxoprolinase 197 Control P47955 60S acidic ribosomal protein P1 190 Control P70266 6-phosphofructo-2-kinase/fructose-2_6-bisphosphatase 1 113 Control Q8QZT1 Acetyl-CoA acetyltransferase_ mitochondrial 402 Control Q9R0Y5 Adenylate kinase isoenzyme 1 623 Control Q80TS3 Adhesion G protein-coupled receptor L3 59 Control B7ZCC9 Adhesion G-protein coupled receptor G4 139 Control Q6P5E6 ADP-ribosylation factor-binding protein GGA2 45 Control E9Q394 A-kinase anchor protein 13 60 Control Q80Y20 Alkylated DNA repair protein alkB homolog 8 111 Control P07758 Alpha-1-antitrypsin 1-1 78 Control P22599 Alpha-1-antitrypsin 1-2 78 Control Q00896 Alpha-1-antitrypsin 1-3 78 Control Q00897 Alpha-1-antitrypsin 1-4 78 Control P57780 Alpha-actinin-4 58 Control Q9QYC0 Alpha-adducin 270 Control Q9DB05 Alpha-soluble NSF attachment protein 156 Control Q6PAM1 Alpha-taxilin 161
  • Comparative Study of the Primary Structures of Cytochrome B5 from Four Species* Akira Tsugitat, Midori Kobayashi, Seiji Tani, Sukei Kyo, M

    Comparative Study of the Primary Structures of Cytochrome B5 from Four Species* Akira Tsugitat, Midori Kobayashi, Seiji Tani, Sukei Kyo, M

    Proceedings ofthe National Academy ofSciences Vol. 67, No. 1, pp. 442-447, September 1970 Comparative Study of the Primary Structures of Cytochrome b5 from Four Species* Akira Tsugitat, Midori Kobayashi, Seiji Tani, Sukei Kyo, M. A. Rashidt, Yukuo Yoshida, Toshimasa Kajihara, and Bunji Hagihara LABORATORY OF MOLECULAR GENETICS AND DEPARTMENT OF BIOCHEMISTRY, OSAKA UNIVERSITY MEDICAL SCHOOL, OSAKA, JAPAN Communicated by Britton Chance, April 1, 1970 Abstract. The primary structures of human, bovine, and chicken cytochrome bN have been determined and compared with that of the previously studied rabbit protein. One peptide containing 31 amino acid residues and another con- taining 10 were found common to all four species. The substitutions of amino acids between species could be accounted for mainly by single base exchange, with a few exceptional double base exchanges for the chicken. Results for bovine cytochrome b5 differ significantly from those previously reported for calf cyto- chrome N5. Cytochrome b5 is a hemoprotein with a role in the microsomal electron- transport system. The prosthetic group of the protein is a protoheme identical with that of hemoglobin and myoglobin.' The main interest of the work to be described resides in the relationship between the function and structure of cytochrome b5, hemoglobin, and myoglobin. Primary and tertiary structures of hemoglobin and myoglobin, together with details of their functional roles, have been reported.2-5 In contrast, little is known about cytochrome b5 except for the primary structures of two cytochromes b5.6-8 This communication describes and compares the primary structures of human, bovine, rabbit, and chicken hepatic cytochrome b5.
  • Myoglobin-Mediated Oxygen Delivery to Mitochondria of Isolated Cardiac Myocytes (Electron Transport/Heart Cells/Cytochrome Oxidase) BEATRICE A

    Myoglobin-Mediated Oxygen Delivery to Mitochondria of Isolated Cardiac Myocytes (Electron Transport/Heart Cells/Cytochrome Oxidase) BEATRICE A

    Proc. Nati. Acad. Sci. USA Vol. 84, pp. 7503-7507, November 1987 Biochemistry Myoglobin-mediated oxygen delivery to mitochondria of isolated cardiac myocytes (electron transport/heart cells/cytochrome oxidase) BEATRICE A. WITTENBERG* AND JONATHAN B. WITTENBERG Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461 Communicated by Berta Scharrer, July 20, 1987 (receivedfor review May 5, 1987) ABSTRACT Myoglobin-mediated oxygen delivery to in- Cytochrome oxidase, half-oxidized when ambient oxygen tracellular mitochondria is demonstrated in cardiac myocytes partial pressure (Po2) is 0.07 torr (1 torr = 133 Pa) (16), in the isolated from the hearts of mature rats. Myocytes are held at circumstance described here experiences oxygen pressures high ambient oxygen pressure, 40-340 torr (5-45 kPa); 20- to 200-fold the pressure required to maintain the normal, sarcoplasmic myoglobin is fully oxygenated. In this condition largely oxidized, state seen in resting myocytes (16). Carbon oxygen availability does not limit respiratory rate; myoglobin- monoxide in this circumstance blocks oxygenation of facilitated diffusion contributes no additional oxygen flux and, sarcoplasmic myoglobin selectively without perturbing the since oxygen consumption is measured in steady states, the optical spectrum of intracellular cytochrome oxidase. We storage function of myoglobin vanishes. Carbon monoxide, conclude that cardiac mitochondria accept two additive introduced stepwise, displaces oxygen from intracellular simultaneous flows of oxygen: the well-known flow of dis- oxymyoglobin without altering the optical spectrum of the solved oxygen to cytochrome oxidase and a flow of largely oxidized intracellular mitochondria. A large part, myoglobin-bound oxygen to a mitochondrial terminus. The about one-third, of the steady-state oxygen uptake is abolished myoglobin-mediated oxygen flow supports ATP generation by carbon monoxide blockade of myoglobin oxygenation.
  • Interfacial Electrochemistry of Cytochrome C and Myoglobin

    Interfacial Electrochemistry of Cytochrome C and Myoglobin

    Virginia Commonwealth University VCU Scholars Compass Theses and Dissertations Graduate School 1982 Interfacial Electrochemistry of Cytochrome c and Myoglobin Edmond F. Bowden Follow this and additional works at: https://scholarscompass.vcu.edu/etd Part of the Chemistry Commons © The Author Downloaded from https://scholarscompass.vcu.edu/etd/4371 This Dissertation is brought to you for free and open access by the Graduate School at VCU Scholars Compass. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of VCU Scholars Compass. For more information, please contact [email protected]. COLLEGE OF HUMANITIES AND SCIENCES VIRGINIA COMMONWEALTH UNIVERSITY This is to certify that the dissertation prepared by Edmond F. Bowden entitled "Interfacial Electrochemistry of Cytochrome £.and Myoglobin" has been approved by his committee as satisfactory completion of the dissertation requirement for the degree of Doctor of Philosophy. School Dean Date INTERFACIAL ELECTROCHEMISTRY OF CYTOCHROME C AND MYOGLOBIN A thesis submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy at Virginia Commonwealth University. by Edmond F. Bowden Director: Dr. Fred M. Hawkridge Professor of Chemistry Virginia Commonwealth University Richmond, Virginia May, 1982 Virginia Commonwealth Um�Ubrary ii ACKNOWLEDGEMENTS I offer my sincere thanks to the following people: Fred M. Hawkridge, without whom the whole show would not have been possible. Fred's guidance, trust, and intense interest as well as his leadership by example have provided inspiration for this work and for my future aspirations. Ronald and Nettie Bowden, my parents, who have continued to pro­ vide guidance and emotional and material support for my endeavors.
  • Liver Mitochondrial DNA Damage and Genetic Variability of Cytochrome B - a Key Component of the Respirasome - Drive the Severity of Fatty Liver Disease

    Liver Mitochondrial DNA Damage and Genetic Variability of Cytochrome B - a Key Component of the Respirasome - Drive the Severity of Fatty Liver Disease

    DR. SILVIA SOOKOIAN (Orcid ID : 0000-0001-5929-5470) Article type : Original This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differencesAccepted Article between this version and the Version of Record. Please cite this article as doi: 10.1111/JOIM.13147 This article is protected by copyright. All rights reserved Liver mitochondrial DNA damage and genetic variability of Cytochrome b - a key component of the respirasome - drive the severity of fatty liver disease Short title: NASH and respirasome Carlos J Pirola *, Martin Garaycoechea, Diego Flichman, Gustavo O Castaño and Silvia Sookoian *. 1 University of Buenos Aires, School of Medicine, Institute of Medical Research A Lanari, Ciudad Autónoma de Buenos Aires, Argentina (CJP, SS). 2 National Scientific and Technical Research Council (CONICET)−University of Buenos Aires, Institute of Medical Research (IDIM), Department of Molecular Genetics and Biology of Complex Diseases, Ciudad Autónoma de Buenos Aires, Argentina (CJP). 3 Department of Surgery, Hospital de Alta Complejidad en Red “El Cruce”, Florencio Varela, Buenos Aires, Argentina (MG). 4 Department of Virology, School of Pharmacy and Biochemistry, University of Buenos Aires, Ciudad Autónoma de Buenos Aires, Argentina (DF). 5 Liver Unit, Medicine and Surgery Department, Hospital Abel Zubizarreta, Ciudad Autónoma de Buenos Aires, Argentina (GOC). 6 National Scientific and Technical Research Council (CONICET)−University of Buenos Aires, Institute of Medical Research (IDIM), Department of Clinical and Molecular Hepatology, Ciudad Autónoma de Buenos Aires, Argentina (SS). * Co-corresponding authorship Grant support: This study was partially supported by grants PICT 2015-0551 and PICT 2016- 0135 (Agencia Nacional de Promoción Científica y Tecnológica, FONCyT).