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Denis M, Dupas T, Persello A, Dontaine J, Bultot L, Betus C, Pelé T, Dhot J, Erraud A, Maillard A, Montnach J, Leroux AA, Bigot-Corbel E, Vertommen D, Rivière M, Lebreton J, Tessier A, Waard M, Bertrand L, Rozec B, Lauzier B. An O-GlcNAcylomic Approach Reveals ACLY as a Potential Target in Sepsis in the Young Rat. International journal of molecular sciences 2021 22(17) 34502162
Abstract:
Sepsis in the young population, which is particularly at risk, is rarely studied. O-GlcNAcylation is a post-translational modification involved in cell survival, stress response and metabolic regulation. O-GlcNAc stimulation is beneficial in adult septic rats. This modification is physiologically higher in the young rat, potentially limiting the therapeutic potential of O-GlcNAc stimulation in young septic rats. The aim is to evaluate whether O-GlcNAc stimulation can improve sepsis outcome in young rats. Endotoxemic challenge was induced in 28-day-old rats by lipopolysaccharide injection (E. Coli O111:B4, 20 mg·kg-1) and compared to control rats (NaCl 0.9%). One hour after lipopolysaccharide injection, rats were randomly assigned to no therapy, fluidotherapy (NaCl 0.9%, 10 mL·kg-1) ± NButGT (10 mg·kg-1) to increase O-GlcNAcylation levels. Physiological parameters and plasmatic markers were evaluated 2h later. Finally, untargeted mass spectrometry was performed to map cardiac O-GlcNAcylated proteins. Lipopolysaccharide injection induced shock with a decrease in mean arterial pressure and alteration of biological parameters (p < 0.05). NButGT, contrary to fluidotherapy, was associated with an improvement of arterial pressure (p < 0.05). ATP citrate lyase was identified among the O-GlcNAcylated proteins. In conclusion, O-GlcNAc stimulation improves outcomes in young septic rats. Interestingly, identified O-GlcNAcylated proteins are mainly involved in cellular metabolism.
O-GlcNAc proteins:
A0A096MJ01, A0A096MK30, A0A096MKD4, A0A096P6L8, A0A0G2JSH9, A0A0G2JSP8, A0A0G2JSR0, A0A0G2JSU7, A0A0G2JSW3, A0A0G2JTG7, A0A0G2JTP6, A0A0G2JUT0, A0A0G2JV65, A0A0G2JVG3, A0A0G2JVH4, A0A0G2JW41, A0A0G2JW94, A0A0G2JWK2, A0A0G2JWS2, A0A0G2JYK0, A0A0G2JZF0, A0A0G2K0F5, A0A0G2K3K2, A0A0G2K3Z9, A0A0G2K401, A0A0G2K477, A0A0G2K5I9, A0A0G2K5P5, A0A0G2K654, A0A0G2K719, A0A0G2K7F7, A0A0G2K8H0, A0A0G2K9P4, A0A0G2K9Q9, A0A0G2KAK2, A0A0G2KB63, A0A0H2UHM5, A0A0H2UHQ9, A0A0H2UHZ6, A0A0H2UI36, A0A0U1RRV7, ROA2, B0BNG3, CAH1, SCOT1, B2RYW3, C0JPT7, D3ZCV0, D3ZG43, D3ZIC4, D3ZQM0, D3ZUB0, D3ZZ68, D3ZZN3, D4A0T0, D4A5E5, D4A6Q4, SYNP2, D4A7X7, D4A8X8, D4AA63, D4ACC2, F1LM30, F1LM47, F1LMP9, F1LMV6, F1LP05, F1LP30, F1LSC3, F1LX07, F1LZW6, F1M3H8, F1M820, F1M865, F1M944, F1M953, F1MAA7, F1MAF7, G3V6E1, G3V6H0, G3V6H5, G3V6P7, G3V6S0, G3V6T7, G3V6Y6, G3V7C6, G3V7J0, G3V826, G3V885, G3V8B0, G3V8L3, G3V8V3, G3V9A3, G3V9U2, M0R5J4, M0R735, M0R757, M0R7S5, M0R9L0, PRDX6, C1QBP, HSPB2, ACOT2, HCD2, PARK7, MDHC, AATM, HBA, FIBG, GPX1, ROA1, MDHM, LDHA, PDIA1, G3P, GSTP1, ALDOA, EF2, AT1A1, BIP, RPN1, ODP2, MLRV, KCRS, HS71A, ATPB, CLH1, AT2A2, DMD, ALDH2, KPYM, AL1A7, ETFA, A1I3, CAH3, FIBB, ECHM, ACADL, PGAM2, MYL3, PGK1, ACLY, THIL, ACSL1, CPT2, CSK21, NDUV2, AT5F1, NDKB, NB5R3, IGG2A, IGG2B, LAC2, UCRI, SDHB, TNNI3, CRYAB, PPIB, PGAM1, RPN2, CAH2, TCPA, VIME, PEBP1, ATP5H, EZRI, QCR2, HS90B, 1433B, ATPG, CRIP2, RSSA, CAV1, LDHB, HSPB1, COF1, TERA, DPYL2, TPIS, DESM, ODPB, TNNT2, AL1A1, ES1, IDHP, MYPC, PSA6, ARF3, 1433G, 1433E, EF1A2, H4, RAN, RS3, AP2B1, RL40, HSP7C, CH60, PHB, ACTC, 1433T, TBA1A, 1433F, TBB5, NUP54, VDAC2, HS90A, EFTU, PNPH, HSPB6, PTBP1, H2B1, MUG1, ATPO, ANXA2, ADT2, K2C8, PRRC1, NIT2, Q498N4, ACSF2, H2A3, K2C6A, Q4G079, AGFG1, Q4PP99, Q4V8E1, EHD2, Q52KS1, NDUAA, Q5BJZ3, Q5D059, Q5M9H2, Q5RJN0, Q5RJR9, UBA1, Q5XFV4, LPP, Q5XI38, GDIR1, ODO1, TBA4A, Q5XIH3, ECHB, PDLI5, A1M, CPT1B, NDUS2, ECHA, ENPL, NDUS1, Q66HF3, MAVS, AMPL, ETFB, QCR1, K1C42, Q6IFU9, K1C14, K1C15, K1C13, K1C10, K2C75, K2C1, HNRPU, Q6IMZ3, TS101, RAB1A, PLAK, K2C5, DLDH, SYWC, TBA1B, Q6P9Y4, Q6PDV6, CNDP2, ROA3, CACP, DEST, Q7TQ70, CISY, Q91XN6, SDHA, IDH3A, ACON, AIFM1, MYG, TGM2, HCDH, VDAC1, SC31A
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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.
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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.
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Cieniewski-Bernard C, Bastide B, Lefebvre T, Lemoine J, Mounier Y, Michalski JC. Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry. Molecular & cellular proteomics : MCP 2004 3(6) 14985449
Abstract:
O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation. O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose. Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach. Fourteen proteins were identified as being O-GlcNAc modified. These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain). A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction. These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
O-GlcNAc proteins:
KCRM, ALDOA, MDHM, G3P, SPA3N, CAH3, ENOB, CRYAB, DKC1, MK08, P85A, 2A5B
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