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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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Hédou J, Bastide B, Page A, Michalski JC, Morelle W. Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle. Proteomics 2009 9(8) 19322778
Abstract:
O-linked beta-N-acetylglucosamine (O-GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy and light chains and actin) were identified as O-GlcNAc modified. Moreover, it was demonstrated that O-GlcNAc moieties involved in contractile protein interactions could modulate Ca(2+) activation parameters of contraction. In order to better understand how O-GlcNAc can modulate the contractile activity of muscle fibers, we decided to identify the sites of O-GlcNAc modification in purified contractile protein homogenates. Using an MS-based method that relies on mild beta-elimination followed by Michael addition of DTT (BEMAD), we determined the localization of one O-GlcNAc site in the subdomain four of actin and four O-GlcNAc sites in the light meromyosin region of myosin heavy chains (MHC). According to previous reports concerning the role of these regions, our data suggest that O-GlcNAc sites might modulate the actin-tropomyosin interaction, and be involved in MHC polymerization or interactions between MHC and other contractile proteins. Thus, the results suggest that this PTM might be involved in protein-protein interactions but could also modulate the contractile properties of skeletal muscle.
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Khidekel N, Ficarro SB, Clark PM, Bryan MC, Swaney DL, Rexach JE, Sun YE, Coon JJ, Peters EC, Hsieh-Wilson LC. Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics. Nature chemical biology 2007 3(6) 17496889
Abstract:
The addition of the monosaccharide beta-N-acetyl-D-glucosamine to proteins (O-GlcNAc glycosylation) is an intracellular, post-translational modification that shares features with phosphorylation. Understanding the cellular mechanisms and signaling pathways that regulate O-GlcNAc glycosylation has been challenging because of the difficulty of detecting and quantifying the modification. Here, we describe a new strategy for monitoring the dynamics of O-GlcNAc glycosylation using quantitative mass spectrometry-based proteomics. Our method, which we have termed quantitative isotopic and chemoenzymatic tagging (QUIC-Tag), combines selective, chemoenzymatic tagging of O-GlcNAc proteins with an efficient isotopic labeling strategy. Using the method, we detect changes in O-GlcNAc glycosylation on several proteins involved in the regulation of transcription and mRNA translocation. We also provide the first evidence that O-GlcNAc glycosylation is dynamically modulated by excitatory stimulation of the brain in vivo. Finally, we use electron-transfer dissociation mass spectrometry to identify exact sites of O-GlcNAc modification. Together, our studies suggest that O-GlcNAc glycosylation occurs reversibly in neurons and, akin to phosphorylation, may have important roles in mediating the communication between neurons.
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Cole RN, Hart GW. Cytosolic O-glycosylation is abundant in nerve terminals. Journal of neurochemistry 2001 79(5) 11739622
Abstract:
Phosphorylation plays a key role in regulating growth cone migration and protein trafficking in nerve terminals. Here we show that nerve terminal proteins contain another abundant post-translational modification: beta-N-acetylglucosamine linked to hydroxyls of serines or threonines (O-GlcNAc(1)). O-GlcNAc modifications are essential for embryogenesis and mounting evidence suggests that O-GlcNAc is a regulatory modification that affects many phosphorylated proteins. We show that the activity and expression of O-GlcNAc transferase (OGT) and N-acetyl-beta-D-glucosaminidase (O-GlcNAcase), the two enzymes regulating O-GlcNAc modifications, are present in nerve terminal structures (synaptosomes) and are particularily abundant in the cytosol of synaptosomes. Numerous synaptosome proteins are highly modified with O-GlcNAc. Although most of these proteins are present in low abundance, we identified by proteomic analysis three neuron-specific O-GlcNAc modified proteins: collapsin response mediator protein-2 (CRMP-2), ubiquitin carboxyl hydrolase-L1 (UCH-L1) and beta-synuclein. CRMP-2, which is involved in growth cone collapse, is a major O-GlcNAc modified protein in synaptosomes. All three proteins are implicated in regulatory cascades that mediate intracellular signaling or neurodegenerative diseases. We propose that O-GlcNAc modifications in the nerve terminal help regulate the functions of these and other synaptosome proteins, and that O-GlcNAc may play a role in neurodegenerative disease.
O-GlcNAc proteins:
DPYL2, UCHL1, SYUB
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