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Yu SB, Wang H, Sanchez RG, Carlson NM, Nguyen K, Zhang A, Papich ZD, Abushawish AA, Whiddon Z, Matysik W, Zhang J, Whisenant TC, Ghassemian M, Koberstein JN, Stewart ML, Myers SA, Pekkurnaz G. Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity. Developmental cell 2024 38843836
Abstract:
Neuronal activity is an energy-intensive process that is largely sustained by instantaneous fuel utilization and ATP synthesis. However, how neurons couple ATP synthesis rate to fuel availability is largely unknown. Here, we demonstrate that the metabolic sensor enzyme O-linked N-acetyl glucosamine (O-GlcNAc) transferase regulates neuronal activity-driven mitochondrial bioenergetics in hippocampal and cortical neurons. We show that neuronal activity upregulates O-GlcNAcylation in mitochondria. Mitochondrial O-GlcNAcylation is promoted by activity-driven glucose consumption, which allows neurons to compensate for high energy expenditure based on fuel availability. To determine the proteins that are responsible for these adjustments, we mapped the mitochondrial O-GlcNAcome of neurons. Finally, we determine that neurons fail to meet activity-driven metabolic demand when O-GlcNAcylation dynamics are prevented. Our findings suggest that O-GlcNAcylation provides a fuel-dependent feedforward control mechanism in neurons to optimize mitochondrial performance based on neuronal activity. This mechanism thereby couples neuronal metabolism to mitochondrial bioenergetics and plays a key role in sustaining energy homeostasis.
O-GlcNAc proteins:
A0A096MIX2, A0A0G2JUA5, IQEC1, A0A0G2JUI5, A0A0G2JUT7, A0A0G2JVC2, A0A0G2JVU1, A0A0G2JVW3, A0A0G2JVZ6, A0A0G2JW69, A0A0G2JWG6, A0A0G2JWK6, A0A0G2JXD0, A0A0G2JXD6, A0A0G2JXE4, TRI46, A0A0G2JXZ9, A0A0G2JY48, A0A0G2JY73, A0A0G2JYE0, A0A0G2JYI7, A0A0G2JYU3, A0A0G2JZ52, A0A0G2JZ94, A0A0G2JZA1, A0A0G2JZA7, A0A0G2JZB7, A0A0G2JZH9, A0A0G2JZX5, A0A0G2K0W3, ABCA3, A0A0G2K2B5, A0A0G2K2Y2, A0A0G2K315, A0A0G2K3H2, A0A0G2K459, A0A0G2K490, A0A0G2K548, A0A0G2K5E4, A0A0G2K5L1, GHC1, A0A0G2K618, A0A0G2K654, A0A0G2K6F2, A0A0G2K6T9, A0A0G2K719, A0A0G2K782, A0A0G2K7L2, A0A0G2K7P9, A0A0G2K847, A0A0G2K8I5, A0A0G2K8S6, A0A0G2K929, A0A0G2K999, A0A0G2K9J0, A0A0G2KAE2, A0A0G2KBB9, A0A0H2UHM7, A0A0U1RS25, A0A140TAA1, NUMBL, PBIP1, A5I9F0, ROA2, H2AJ, B0BN30, B0BNK1, LRFN3, B0K026, FLRT3, B1H2A6, B1WC18, ACAD9, BRSK1, B2GUY8, B2GV74, PTPRE, B2RYB1, B2RYC9, B2RYD7, CTL2, B5DEJ9, TTC17, B5DEZ8, SNPH, B5DFC3, D3Z981, D3Z9D0, D3Z9L0, D3ZA31, ATPK, D3ZAG0, LRRT3, D3ZB81, D3ZBM3, D3ZC55, D3ZC56, D3ZC81, D3ZCT7, D3ZD23, D3ZD73, D3ZDX5, D3ZE26, D3ZEH1, SIDT2, D3ZEI4, D3ZEK5, D3ZES7, D3ZFQ8, D3ZFT1, D3ZG43, D3ZH14, D3ZH36, D3ZH41, D3ZHA1, D3ZHG3, D3ZHL1, MACF1, D3ZK41, D3ZKV7, D3ZLE2, D3ZMJ7, D3ZN27, HCFC1, D3ZN99, D3ZPJ0, D3ZPN0, PLXA3, D3ZQ57, TRIM2, D3ZQM3, D3ZQN7, D3ZRH1, D3ZRN3, D3ZSY8, D3ZT20, D3ZT36, D3ZT47, D3ZTG3, D3ZTL0, D3ZTW6, D3ZU13, D3ZUJ8, D3ZUM4, D3ZUY8, D3ZW09, D3ZW15, D3ZW19, D3ZWP6, D3ZWQ0, D3ZXQ2, D3ZXX3, D3ZYD7, D3ZYM4, D3ZYR4, D3ZYS7, D3ZZK3, D3ZZU4, D4A062, D4A0A1, D4A1G8, LRFN5, D4A2H4, D4A2I9, D4A2Q3, D4A3H5, D4A3L3, D4A3N4, D4A435, D4A507, D4A517, D4A567, D4A5F1, D4A5I4, D4A5X7, D4A604, D4A628, D4A644, LRRT1, D4A6G2, D4A6H8, MGLYR, D4A6T9, D4A732, D4A758, D4A7M0, D4A7Y4, D4A831, D4A833, D4A885, D4A8N1, D4A9F4, D4A9U6, D4AA63, D4AA77, D4ABA9, D4ABI7, LRFN4, D4ACK1, PCD16, D4AD89, D4ADS4, D4ADU2, D4AE63, D4AEB3, E9PT51, E9PT53, E9PT92, E9PTA4, E9PTR4, F1LM47, F1LMW0, F1LNL3, F1LP13, F1LPD7, F1LPJ1, F1LPV0, F1LR12, F1LS01, F1LT36, F1LUC0, F1LUT4, F1LUZ4, F1LV44, F1LVL5, S2512, F1LXC7, F1LXD6, F1LYJ8, FARP1, F1LZ38, F1LZB7, F1M049, F1M1E4, F1M2D4, F1M2E9, F1M2K6, F1M3H3, F1M3J7, F1M3P6, F1M3T8, F1M4B6, F1M4J1, F1M5G8, F1M6P8, F1M853, F1M8K0, F1M949, F1MA42, F1MA97, F1MAK3, F1MAP4, F1MAS4, F7EL93, F7EYB9, F7F3I7, G3V667, G3V6K6, G3V6N7, G3V6U3, G3V728, G3V765, G3V7D4, G3V7K5, G3V7N0, G3V7V3, G3V824, G3V881, G3V886, G3V8D0, LRP1, PGLT1, M0R4G0, M0R557, RN157, M0R5P8, M0R5T4, M0R6E0, M0R715, M0R757, M0R7B4, M0R868, M0R9U3, M0RAP5, M0RB22, M0RC17, M0RDA4, MARK1, MARK2, SYT11, DCLK1, CD166, CTND2, NRP2, ACSL4, NPTXR, ENTP2, C1QBP, DNJA2, PICAL, SEM6B, TRIM3, ANK3, CELR3, SLIT1, SLIT3, VKGC, PACS1, BSN, GABR2, PTN23, AGRL1, AGRL2, CATB, OX2G, ROA1, ENOA, G3P, GNAI2, AT1A1, AT1A2, AT1A3, BIP, GDN, RPN1, AT1B1, CPSM, SYPH, KCC2B, SYN1, MAP1S, LRFN1, LRC4B, ATPB, KCC2A, CLH1, AT2B1, AT2B2, AT2A2, KCC2G, SUCA, RS14, NCAM1, AT1B2, PRIO, LAMP1, INSR, MTAP2, MAP1B, GBRB1, KCC2D, H14, ATPA, S25A3, SPTN1, ABCD3, LAMP2, RL9, RL35, THIL, GSK3B, RL27A, AP2A2, GBRG2, CSK21, GRIA1, GRIA2, GRIA3, GRIA4, AT5F1, NFL, GNAZ, RLA0, GBRA5, GBRA3, CNR1, PPAL, PGFRA, EDNRB, SYT1, PERI, AINX, GBRA2, RL17, RS5, IGF1R, CATD, AKAP5, EAA1, RPN2, VPP1, AGRIN, KAPCA, RS2, DCTN1, TCPA, SC6A9, BDH, RS9, SERPH, ITPR1, PLEC, PFKAL, VIME, ATP5H, GRM2, GRM3, GRM4, GRM5, EAA2, S6A11, EZRI, TXTP, CPT1A, QCR2, HS90B, MAP1A, GRM7, ATPG, NMDZ1, DYHC1, MPC2, ANPRC, GRIK2, GRIK3, DPP6, GFAP, PFKAM, PFKAP, SYT5, DPYL2, NPTX1, S1PR1, GRP75, ITB1, RS3A, AP1B1, MOT1, P4HA1, CACB1, CA2D1, GBB2, AT12A, EPHA5, NCAN, PGCB, OGT1, IDHP, GNAO, ACTB, ARF3, STXB1, HNRPK, 1433G, RS7, PP1B, RS16, 1433E, RS23, RS13, RS11, EF1A1, RS4X, RL23A, RS6, H4, GBRA1, RAN, RL23, RS24, RS3, RL32, RL11, AP2B1, RS27A, RL40, HSP7C, CYH2, DNJA1, GBRB3, GBRB2, ACTC, TBA1A, NEUA, TBB5, APC, MFGM, NUP54, FOLH1, IF2G, RL24, ENPP5, AP2M1, H33, RMXRL, STIM1, TBB2A, MDGA1, EFTU, PURA, MET, CNTN5, NPTN, GPAT1, NEO1, LCAP, KC1A, NFASC, NRCAM, M2OM, SHPS1, CD47, CNTP1, S27A1, DHB4, CSPG4, NMDE2, CAC1B, SV2A, PTPRA, NTRK3, TENR, L1CAM, ADT1, KC1D, ATPO, TGFB2, NRX3A, CAC1E, ADT2, MYPT1, ADA10, K2C8, Q14U74, KINH, Q32KJ5, MIC60, ATAD3, TBB2B, LONP2, AMZ2, LRFN2, Q498C9, DJC10, CARM1, K2C6A, TBB3, MACOI, S39A6, RBMX, Q4V8H7, LRC8A, Q505J7, SYFA, S2551, ZFR, PGAM5, Q566E4, NOE2, NDUA9, ARHG2, PLD3, NONO, FA98A, RM16, CAPR1, DCLK2, PMGT2, NSDHL, ITM2C, LRC59, DRS7B, Q5RK08, Q5U2P5, Q5U302, LRC8D, KIF2B, Q5XIA6, ECSIT, TBA4A, Q5XIH3, EPDR1, TMX2, MGRN1, ECHB, NOE1, GSLG1, NMDE4, PTPRZ, SYT7, KC1G3, FPRP, Q62797, CNTN4, GGH, NLGN2, NLGN3, NELL2, DPYL1, DPYL3, ERBB4, SCNAA, CAMKV, Q63116, CNTN1, GRIK5, PHLB1, MYO9B, NRX1A, NRX2A, MAP6, NTRK2, HYOU1, S12A5, SFXN1, OST48, NDUS2, DDX1, TECR, ECHA, AT1A4, AT2B4, PTPRF, PTPRS, PACC1, FACR1, C2D1A, ENPL, NDUS1, S12A9, TBA3, SIR5, SIAT9, HEXB, Q6AY21, SCPDL, Q6AYI1, Q6AYM8, RTCB, ABD12, K1C15, K1C10, K2C4, K2C1B, K22E, K2C73, K2C1, TS101, PRC2A, ABHGA, PLAK, Q6P3V8, TCPG, MEST, K2C5, DAB2P, Q6P762, LYAG, DHB12, TBB4B, RL10, DPP10, GNA13, KIF5A, ROA3, RS27, PGAP1, PCDA4, ANR46, 4F2, PLPR3, PLPR4, SSRA, QCR8, R4RL2, T132A, SE1L1, MAST1, TFB1M, RB6I2, SFXN5, CA2D3, AGAP2, NICA, SGPL1, Q8CJE3, BRNP2, ERC2, AGRG1, L2GL1, LGI1, Q8R490, TIP, FAT3, AFAP1, MARK3, CCG8, KHDR1, BRNP1, TFR1, ATRN, CLAP2, RTN4R, Q99PS2, PABP1, XYLT1, SO1C1, KDIS, TPP1, CSPG2, DCX, PSD1, ABCA2, CBPD, SFXN3, WNK1, RIMS1, RIMS2, CHD8, HNRPD, HCN4, HCN3, HCN2, HCN1, PCLO, TAOK2, SYGP1, NRP1, SRCN1, MEGF8, CELR2, S22AN, PDZD2, CXAR, TEN2, PODXL, CTNB1, SHAN1, KIF2A, SLIT2, NEGR1, GABR1, FADS2, TMM33, AGRL3, RPGF4, FLOT1, MYO9A, CADH2, HOME1, DHCR7
Species: Rattus norvegicus
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Sacoman JL, Dagda RY, Burnham-Marusich AR, Dagda RK, Berninsone PM. Mitochondrial O-GlcNAc Transferase (mOGT) Regulates Mitochondrial Structure, Function, and Survival in HeLa Cells. The Journal of biological chemistry 2017 292(11) 28100784
Abstract:
O-Linked N-acetylglucosamine transferase (OGT) catalyzes O-GlcNAcylation of target proteins and regulates numerous biological processes. OGT is encoded by a single gene that yields nucleocytosolic and mitochondrial isoforms. To date, the role of the mitochondrial isoform of OGT (mOGT) remains largely unknown. Using high throughput proteomics, we identified 84 candidate mitochondrial glycoproteins, of which 44 are novel. Notably, two of the candidate glycoproteins identified (cytochrome oxidase 2 (COX2) and NADH:ubiquinone oxidoreductase core subunit 4 (MT-ND4)) are encoded by mitochondrial DNA. Using siRNA in HeLa cells, we found that reducing endogenous mOGT expression leads to alterations in mitochondrial structure and function, including Drp1-dependent mitochondrial fragmentation, reduction in mitochondrial membrane potential, and a significant loss of mitochondrial content in the absence of mitochondrial ROS. These defects are associated with a compensatory increase in oxidative phosphorylation per mitochondrion. mOGT is also critical for cell survival; siRNA-mediated knockdown of endogenous mOGT protected cells against toxicity mediated by rotenone, a complex I inhibitor. Conversely, reduced expression of both nucleocytoplasmic (ncOGT) and mitochondrial (mOGT) OGT isoforms is associated with increased mitochondrial respiration and elevated glycolysis, suggesting that ncOGT is a negative regulator of cellular bioenergetics. Last, we determined that mOGT is probably involved in the glycosylation of a restricted set of mitochondrial targets. We identified four proteins implicated in mitochondrial biogenesis and metabolism regulation as candidate substrates of mOGT, including leucine-rich PPR-containing protein and mitochondrial aconitate hydratase. Our findings suggest that mOGT is catalytically active in vivo and supports mitochondrial structure, health, and survival, whereas ncOGT predominantly regulates cellular bioenergetics.
O-GlcNAc proteins:
A6QQ83, B1WBY5, D4A1Y5, E1BJA2, C1QBP, O62828, HCD2, IDH3B, AKAP1, NDUAC, CY1, QCR7, DHE3, COX41, COX5A, COX5B, THTR, ATPB, ADT1, NU4M, ATPD, ATPG, HXK1, CX6A2, KAD2, NNTM, IVD, MPCP, AATM, CX7A2, GLSK, QCR8, AT5F1, ATP5H, ATPO, ABCD3, ATPA, NB5R3, QCR2, SDHA, QCR1, 3HIDH, CPT1A, NDUAA, PRDX2, NDUS7, NDUB4, ODPB, VDAC2, COX2, FIS1, M2OM, NDUA4, NDUB7, NDUA2, NDUB8, NDUBA, NDUB5, NDUC2, IDHP, NDUA7, COQ5, LETM1, ATPK, CISY, Q2NL19, COQ9, MDHM, ATAD3, SDHB, STML2, HSDL2, LONM, NDUA9, TOM20, AMPL, Q7TQ85, NDUBB, HINT2, NDUAD, SFXN3
Species: Bos taurus, Homo sapiens, Rattus norvegicus
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Ma J, Banerjee P, Whelan SA, Liu T, Wei AC, Ramirez-Correa G, McComb ME, Costello CE, O'Rourke B, Murphy A, Hart GW. Comparative Proteomics Reveals Dysregulated Mitochondrial O-GlcNAcylation in Diabetic Hearts. Journal of proteome research 2016 15(7) 27213235
Abstract:
O-linked β-N-acetylglucosamine (O-GlcNAc), a post-translational modification on serine and threonine residues of many proteins, plays crucial regulatory roles in diverse biological events. As a nutrient sensor, O-GlcNAc modification (O-GlcNAcylation) on nuclear and cytoplasmic proteins underlies the pathology of diabetic complications including cardiomyopathy. However, mitochondrial O-GlcNAcylation, especially in response to chronic hyperglycemia in diabetes, has been poorly explored. We performed a comparative O-GlcNAc profiling of mitochondria from control and streptozotocin (STZ)-induced diabetic rat hearts by using an improved β-elimination/Michael addition with isotopic DTT reagents (BEMAD) followed by tandem mass spectrometric analysis. In total, 86 mitochondrial proteins, involved in diverse pathways, were O-GlcNAcylated. Among them, many proteins have site-specific alterations in O-GlcNAcylation in response to diabetes, which suggests that protein O-GlcNAcylation is a novel layer of regulation mediating adaptive changes in mitochondrial metabolism during the progression of diabetic cardiomyopathy.
O-GlcNAc proteins:
A9UMV9, B0BNE6, SCOT1, B2RYS2, B5DEL8, D3ZUX5, D4A0T0, D4A565, F1LM47, M0R6F2, HCD2, AATM, MDHM, COX1, SODM, ODP2, ACADM, KCRS, ATPB, DHE3, COX41, CX6C2, ODBA, IVD, THIM, ETFA, ECHM, PCCA, ACADL, ACADS, ATPA, S25A3, THIL, ACSL1, NDUV2, AT5F1, ATP5J, SDHB, ODPA, 3HIDH, ATP5I, QCR2, ODPB, CH60, PHB1, CX6B1, VDAC2, EFTU, M2OM, MMSA, ADT1, ATPO, MIC60, ACSF2, NDUAA, COQ8A, Q5BJZ3, NDUA9, T126A, ODO1, PHB2, ECHB, ECH1, CPT1B, NDUS2, ECHA, NDUS1, ETFB, IDH3B, QCR1, SAM50, DLDH, ATP5L, CACP, SDHA, IDH3A, ACON, NDUF4, HCDH, PRDX3, VDAC1
Species: Rattus norvegicus
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Ma J, Liu T, Wei AC, Banerjee P, O'Rourke B, Hart GW. O-GlcNAcomic Profiling Identifies Widespread O-Linked β-N-Acetylglucosamine Modification (O-GlcNAcylation) in Oxidative Phosphorylation System Regulating Cardiac Mitochondrial Function. The Journal of biological chemistry 2015 290(49) 26446791
Abstract:
Dynamic cycling of O-linked β-N-acetylglucosamine (O-GlcNAc) on nucleocytoplasmic proteins serves as a nutrient sensor to regulate numerous biological processes. However, mitochondrial protein O-GlcNAcylation and its effects on function are largely unexplored. In this study, we performed a comparative analysis of the proteome and O-GlcNAcome of cardiac mitochondria from rats acutely (12 h) treated without or with thiamet-G (TMG), a potent and specific inhibitor of O-GlcNAcase. We then determined the functional consequences in mitochondria isolated from the two groups. O-GlcNAcomic profiling finds that over 88 mitochondrial proteins are O-GlcNAcylated, with the oxidative phosphorylation system as a major target. Moreover, in comparison with controls, cardiac mitochondria from TMG-treated rats did not exhibit altered protein abundance but showed overall elevated O-GlcNAcylation of many proteins. However, O-GlcNAc was unexpectedly down-regulated at certain sites of specific proteins. Concomitantly, TMG treatment resulted in significantly increased mitochondrial oxygen consumption rates, ATP production rates, and enhanced threshold for permeability transition pore opening by Ca(2+). Our data reveal widespread and dynamic mitochondrial protein O-GlcNAcylation, serving as a regulator to their function.
O-GlcNAc proteins:
A9UMV9, B0BNC0, B2RYW3, B2RYX1, B5DEL8, D3ZUX5, D4A7L4, D4A898, F1LM47, F1LXA0, O70253, AATM, MDHM, NU4M, SODM, ODP2, ATPB, DHE3, COX5A, ALDH2, CX6C2, THIM, ETFA, ECHM, PCCA, ACADL, ACADS, ATPA, ACSL1, CPT2, NDUV2, ATP5J, SDHB, 3HIDH, ATP5E, ATP5I, ATP5H, CX7A2, ATPD, ACADV, ODPB, IDHP, CH60, EFTU, M2OM, MMSA, ADT1, ATPO, MIC60, Q3V5X8, ACSF2, Q4FZZ4, TGT, NDUAA, Q5BJZ3, NDUA9, ODO1, ECHB, NDUS2, ECHA, PDK2, NDUS1, Q66HF3, ETFB, QCR1, DLDH, Q6PCU0, ATP5L, CACP, QCR8, CISY, SDHA, ACON, PRDX3, VDAC1
Species: Rattus norvegicus
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Johnsen VL, Belke DD, Hughey CC, Hittel DS, Hepple RT, Koch LG, Britton SL, Shearer J. Enhanced cardiac protein glycosylation (O-GlcNAc) of selected mitochondrial proteins in rats artificially selected for low running capacity. Physiological genomics 2013 45(1) 23132757
Abstract:
O-linked β-N-acetyl glucosamine (O-GlcNAc) is a posttranslational modification consisting of a single N-acetylglucosamine moiety attached by an O-β-glycosidic linkage to serine and threonine residues of both nuclear and cytosolic proteins. Analogous to phosphorylation, the modification is reversible and dynamic, changing in response to stress, nutrients, hormones, and exercise. Aims of this study were to examine differences in O-GlcNAc protein modification in the cardiac tissue of rats artificially selected for low (LCR) or high (HCR) running capacity. Hyperinsulinemic-euglycemic clamps in conscious animals assessed insulin sensitivity while 2-[(14)C] deoxyglucose tracked both whole body and tissue-specific glucose disposal. Immunoblots of cardiac muscle examined global O-GlcNAc modification, enzymes that control its regulation (OGT, OGA), and specific proteins involved in mitochondrial oxidative phosphorylation. LCR rats were insulin resistant disposing of 65% less glucose than HCR. Global tissue O-GlcNAc, OGT, OGA, and citrate synthase were similar between groups. Analysis of cardiac proteins revealed enhanced O-GlcNAcylation of mitochondrial Complex I, Complex IV, VDAC, and SERCA in LCR compared with HCR. These results are the first to establish an increase in specific protein O-GlcNAcylation in LCR animals that may contribute to progressive mitochondrial dysfunction and the pathogenesis of insulin resistance observed in the LCR phenotype.
O-GlcNAc proteins:
COX1, AT2A2, NDUA9, VDAC1
Species: Rattus norvegicus
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Hu Y, Suarez J, Fricovsky E, Wang H, Scott BT, Trauger SA, Han W, Hu Y, Oyeleye MO, Dillmann WH. Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. The Journal of biological chemistry 2009 284(1) 19004814
Abstract:
Increased nuclear protein O-linked beta-N-acetylglucosamine glycosylation (O-GlcNAcylation) mediated by high glucose treatment or the hyperglycemia of diabetes mellitus contributes to cardiac myocyte dysfunction. However, whether mitochondrial proteins in cardiac myocytes are also submitted to O-GlcNAcylation or excessive O-GlcNAcylation alters mitochondrial function is unknown. In this study, we determined if mitochondrial proteins are O-GlcNAcylated and explored if increased O-GlcNAcylation is linked to high glucose-induced mitochondrial dysfunction in neonatal rat cardiomyocytes. By immunoprecipitation, we found that several mitochondrial proteins, which are members of complexes of the respiratory chain, like subunit NDUFA9 of complex I, subunits core 1 and core 2 of complex III, and the mitochondrial DNA-encoded subunit I of complex IV (COX I) are O-GlcNAcylated. By mass spectrometry, we identified that serine 156 on NDUFA9 is O-GlcNAcylated. High glucose treatment (30 mm glucose) increases mitochondrial protein O-GlcNAcylation, including those of COX I and NDUFA9 which are reduced by expression of O-GlcNAcase (GCA). Increased mitochondrial O-GlcNAcylation is associated with impaired activity of complex I, III, and IV in addition to lower mitochondrial calcium and cellular ATP content. When the excessive O-GlcNAc modification is reduced by GCA expression, mitochondrial function improves; the activity of complex I, III, and IV increases to normal and mitochondrial calcium and cellular ATP content are returned to control levels. From these results we conclude that specific mitochondrial proteins of cardiac myocytes are O-GlcNAcylated and that exposure to high glucose increases mitochondrial protein O-GlcNAcylation, which in turn contributes to impaired mitochondrial function.
O-GlcNAc proteins:
COX1, NDUA9, QCR1
Species: Rattus norvegicus
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