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Lanzillotta C, Prestia F, Greco V, Iavarone F, Cordella F, Sette C, Forte E, Tramutola A, Lanzillotta S, Cassano T, Di Angelantonio S, Urbani A, Barone E, Perluigi M, Di Domenico F. Enhancing protein O-GlcNAcylation in down syndrome mice mitigates memory dysfunctions through the rescue of mitochondrial bioenergetics, stress responses and pathological markers. Redox biology 2025 85 40684658
Abstract:
Disturbances of the single sugar modification of proteins, O-GlcNAc, have been identified as a potential connection between disrupted brain metabolism and intellectual decay. In Alzheimer disease (AD), the reduced uptake of glucose in the brain results in aberrant O-GlcNAc cycling contributing to redox imbalance and neurodegeneration. Notably, alterations of O-GlcNAc homeostasis, associated with impaired O-GlcNAc transferase (OGT)/O-GlcNAcase (OGA) regulation, foster neuropathological mechanisms characterized by the presence of AD hallmarks in Down syndrome (DS) models. In the present study we examined the ability of Thiamet G (TMG), a well-known OGA inhibitor, in improving bio-energetic processes, inducing stress responses, reducing AD-related signatures and ameliorating cognition in a murine model of DS. Our data demonstrate that short-term intranasal administration of TMG restored OGA activity and normalized the global O-GlcNAc profile in mouse cortices. By a proteomic approach we identified protein components whose increased O-GlcNAc levels rescue, resulted to brain molecular and cognitive improvements. Remarkably, these included elements involved in energy production, neuronal architecture, antioxidant and stress response mechanisms. The ability of TMG in rescuing O-GlcNAc cycle and metabolic changes, associated with improved mitochondrial activity in cortical tissue, was further accompanied by changes in the O-GlcNAc/phospho ratio of APP and Tau. Functional improvements translated in enhanced recognition memory in Ts2Cje mice. Our study highlights the pivotal role of altered protein O-GlcNAcylation in DS neuropathology and establishes the molecular basis to envision the O-GlcNAc process as a promising therapeutic target to mitigate genetic- and metabolism-driven brain alterations linked to redox imbalance, mitochondrial failure and the development of AD features.
O-GlcNAc proteins:
APBA1, GDS1, DPYL2, STXB1, DLDH, DPYL4, REPS1, CTBP1, COR1A, GFAP, ALDOC, ALDOA, AATC, AATM, ENPL, NFL, NFM, PDIA1, TAU, KCC2A, NCAM1, ENOA, ENOG, HXK1, NFH, BIP, MAP4, KCRU, CTND1, DYN1, CAP1, TCPQ, NSF, PRS7, ALDH2, LMNA, SAHH, GDIA, KPYM, UBP5, ATPB, EF2, HNRPK, ABI2, LIS1, CH60, TBA4A, TBB4B, DLG3, TIAR, NHRF1, DPYL1, RGS14, TBB5, HNRL2, PLAK, ATPA, ANXA7, PPR21, FUBP2, CMPK2, GRIN1, C1TM, SRC8, TS101, PGCB, TCPW, DSG1A, FSCN1, PACN1, DLG4, SYN2, UBXN7, AT1A3, AT1A2, NEB2, 2AAA, TBB2A, PHF24, EFTU, PSD11, SAM50, MAON, CPNE3, SSDH, SEP11, MIC60, OGT1, PYGB, DNM1L, THIL, HNRPL, SHLB2, SNP47, FIBG, AT1A1, IRGQ, CSDE1, SYYC, PCY2, GMPPA, ARP3, RANB3, QCR1, SCOT1, TBB4A, EF1G, DPYL5, TBB3, LGI1, HABP4, AL9A1, GUAD, PDC6I, PYGM, E41L3, PACN2, P5CS, RASL1, PDPK1
Species: Mus musculus
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Zaro BW, Batt AR, Chuh KN, Navarro MX, Pratt MR. The Small Molecule 2-Azido-2-deoxy-glucose Is a Metabolic Chemical Reporter of O-GlcNAc Modifications in Mammalian Cells, Revealing an Unexpected Promiscuity of O-GlcNAc Transferase. ACS chemical biology 2017 12(3) 28135057
Abstract:
Glycans can be directly labeled using unnatural monosaccharide analogs, termed metabolic chemical reporters (MCRs). These compounds enable the secondary visualization and identification of glycoproteins by taking advantage of bioorthogonal reactions. Most widely used MCRs have azides or alkynes at the 2-N-acetyl position but are not selective for one class of glycoprotein over others. To address this limitation, we are exploring additional MCRs that have bioorthogonal functionality at other positions. Here, we report the characterization of 2-azido-2-deoxy-glucose (2AzGlc). We find that 2AzGlc selectively labels intracellular O-GlcNAc modifications, which further supports a somewhat unexpected, structural flexibility in this pathway. In contrast to the endogenous modification N-acetyl-glucosamine (GlcNAc), we find that 2AzGlc is not dynamically removed from protein substrates and that treatment with higher concentrations of per-acetylated 2AzGlc is toxic to cells. Finally, we demonstrate that this toxicity is an inherent property of the small-molecule, as removal of the 6-acetyl-group renders the corresponding reporter nontoxic but still results in protein labeling.
O-GlcNAc proteins:
A2A5R8, A2A6U3, A2AF81, A2AG39, A2AIW9, A2AJ72, A2AJI1, A2AKV2, A2AL12, A2AMW0, A2AUR3, LAS1L, TRM1L, A5A4Y9, A6PWC3, B0QZF8, B1AU76, UPP, B7ZC19, B7ZP47, B8JJC1, D3YWF6, D3YWK1, D3YWS3, D3YYP4, E9PX53, E9Q066, I2BP2, E9Q4Q2, E9Q5L7, E9Q7W0, E9QP59, F8WGW3, G3UX26, G3UYZ0, G3UZ44, G3X972, H3BKW0, H7BWX9, GTPB1, AIP, ATOX1, HDAC1, GSH0, DHX15, IKBE, AKAP2, SLK, IMPCT, IF6, ACOT1, NMT1, DHB12, SRPK1, ZN326, KLC1, RPP30, IDHC, CASP8, GCR, TYSY, RIR1, S10AA, LEG1, G3P, TPIS, PRDX3, CBX3, TISD, CATA, IMDH2, NFKB1, MAP4, CEBPB, CDK4, FKBP4, HMGB2, KAP3, MP2K1, RANG, PTN11, FBRL, PTN12, FMR1, HMGCL, DYN1, CAP1, STAT1, STAT3, PURA, ALD2, SIPA1, PURA2, GSHR, FOSL2, FOSL1, GSTM5, PCY1A, VATA, HDGF, UBP10, RHOX5, HMGA2, CCHL, NUB1, FAF1, ZNRD2, TB182, PCBP1, ARL1, PFD3, TCTP, HMGB1, DYL1, UB2L3, HDAC2, ELAV1, 4EBP2, PYRG1, TCPB, SPTC2, PSME2, BOP1, WBP2, XDH, HMMR, E2AK2, CO6A1, FABP5, LARP7, CNN2, PP4R2, RM10, Q3TFP0, GUAA, FUBP2, TRADD, CTU2, Q3U4W8, SNX27, BABA1, EDC4, COBL1, SKAP2, ARH40, CSTOS, LRRF1, ZMAT1, Q45VK5, JIP4, MDC1, Q5SUW3, SRC8, SAMH1, KHDR1, SPB6, CAPR1, PAPS1, TS101, PA1B2, FNTA, IGBP1, FSCN1, FXR1, CBX5, RAI1, MELK, FOXC2, DBNL, CYTB, NDRG1, RALY, GPDM, RAB3I, F120A, NOP58, Q6DFZ1, TPM4, Q6NXL1, Q6NZD2, TNPO3, SMHD1, UGGG1, UBXN7, TXLNA, DC1L2, KI18B, JUPI2, LARP1, CAND2, ACAP2, HNRPQ, SPAG7, ATX2L, MAP6, ELP1, PJA2, PGRC2, KCMF1, Q80VB6, FA98B, WDTC1, CPPED, LPP, PEF1, IF4B, ATG4B, FTO, Q8BH80, PRUN1, AHSA1, RCC2, NCEH1, LSS, FBLN3, PPR18, SRRM2, MSRB3, PPME1, RL1D1, TBCD4, NHLC2, MAP1S, TLK1, CND2, RAE1L, SEP10, ZFP57, UBA6, UBA3, STON1, PPM1F, GNL3, PUR1, HMCS1, Q8K0C7, PDXK, ANGE2, LRC41, SDE2, DNM1L, ANLN, MATR3, CBR3, MEPCE, ERF3A, DC1L1, SPART, TDIF2, HEXI1, SNP47, UBP15, MAVS, UBXN4, ACSF2, MICU1, ZNG1, BACH, ISOC1, IPYR2, CSDE1, PIP30, GCSH, Q91X76, DUS3L, BAG2, KCC1A, TTC1, HNRLL, RIN1, PP6R3, MARC2, DBR1, ATAD3, PSIP1, NXF1, NONO, PLST, RRAGC, VMA5A, TARA, DDAH2, TADA1, GRPE1, ABD12, NU155, OGFR, NPM3, GLOD4, COPRS, DPOE4, MIEN1, TRAP1, VATG1, CHSP1, OCAD1, RANB3, MFR1L, NDUF7, TBC15, PPIL4, MPPB, CYBP, ZCHC8, CD37L, MMS19, ARPIN, HNRPM, NXP20, SPF27, TOE1, Q9D4G5, ATAD1, CF226, IPYR, ORN, CNN3, KAP0, PLIN3, AKAP8, EIF3F, IFG15, LIMA1, NEK7, RTN3, STK3, NUP50, SYSM, HSPB8, BAG3, CUL3, RABX5, CAF1A, DREB, TOM40, DNJC7, NFU1, FBX6, NUBP1, DEST, TEBP, ACOT9, NFKB2, KAD2, SKP1, PDC6I, VAPA, CARM1, RAD9A, IF2G, SAE2, TRIP6, MBD2, HNRPF
Species: Mus musculus
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