Behavioural characterization of mannoside acetylglucosaminyltransferase 5 (Mgat5) deficient mice.

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Mgat5 (mannoside acetylglucosaminyltransferase 5)-modified N-glycans, formed in the medial Golgi, promote structural heterogeneity in glycoproteins that regulate cellular interactions by binding to galectins. To study the role of these specific carbohydrates in the Central Nervous System (CNS) in an in vivo model, Mgat5 knockout (Mgat5-/-) mice were tested in a battery of tests consisting of different behavioural paradigms. Mgat5-/- mice were normal in physical exam, startle reactivity, sensori-motor gating, motor activity and spatial learning but showed a mild gender-dependent difference in anxiety level. Male and female Mgat5-/- mice showed a robust decrease in immobility time in the forced swim test and the tail suspension test. After the chronic mild stress test, Mgat5-/- mice decreased their immobility further, which implies they are resistant to depression-like phenotype. Our results suggest a role of complex carbohydrates in the pathogenesis of depression.

The Physical Object
Pagination90 leaves.
ID Numbers
Open LibraryOL19552010M
ISBN 139780494214466

A-1,3-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza (ECN-acetilglukozaminiltransferaza I, N-glikozil-oligosaharid-glikoprotein N-acetilglukozaminiltransferaza I, uridin difosfoacetilglukozamin-alfa-1,3-manozilglikoprotein beta-1,2-N-acetilglukozaminiltransferaza, UDP-N-acetilglukozaminil:alfa-1,3-D-manozid-beta-1,2-N-acetilglukozaminiltransferaza I, UDP-N BRENDA: BRENDA entry.

UDP-N-acetylglucosamine:αd-mannoside β-1,6-N-acetylglucosaminyltransferase V (GlcNAcT-V) has been purified from cell extracts of the human hepatoma cell line, Hep3B, with % purified enzymes had molecular masses of about 67 and 65 kDa on denaturated and natural conditions, respectively.

The values of pI was The GlcNAcT-V, when resolved by Cited by: 9.

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Oppenheimer, C.L.; Hill, R.L.: Purification and characterization of a rabbit liver α1→ 3 mannoside β1→2 N-acetylglucosaminyltransferase. Here we characterize one of these genes, TbGT11, and show that it encodes a Golgi apparatus resident UDP-GlcNAc:α3-d-mannoside β1–2-N-acetylglucosaminyltransferase I activity (TbGnTI).

The bloodstream-form TbGT11 null mutant exhibited significantly modified protein N -glycans but normal growth in vitro and infectivity to by: N-Acetylglucosaminyltransferase II (GNTII), which catalyzes the transfer of N-acetylglucosamine to N-glycans, plays an essential role in the biosynthesis of branched and complex-type characteristics of the GNTIIs from various species have been identified, but not all features have been revealed because some insects have GNTII redundancies due to the possession of splicing : Hiroyuki Kajiura, Yugo Nakamura, Mari Nishimura, Takao Ohashi, Ryo Misaki, Kazuhito Fujiyama.

The enzymatic activity was maintained after a min incubation at pHs –, but it was mostly abolished at pHs and The optimal pH of the enzyme was approximatelyand its activity decreased to less than 15% of the maximum at pHs lower than and higher than Tan J, D’Agostaro GAF, Bendiak B, Reck F, Sarkar M, Squire JA, Leong P, Schachter H () The human UDP-N-acetylglucosamine: alphaD-mannoside-betα-1,2-N-acetylglucosaminyltransferase II gene (MGAT2)—cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein.

Purification and characterization of rabbit liver UDP-N-acetylglucosamine:αD-mannoside β-1,2-N-acetylglucosaminyltransferase I. J Biol Chem – PubMed Google Scholar Opat AS, Puthalakath H, Burke J, Gleeson PA () Genetic defect in N -acetylgluco-saminyltransferase I gene of a ricin-resistant baby hamster kidney mutant.

Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. Spoljašnje veze. Alpha-1,3-mannosyl-glycoprotein+2-beta-N-acetylglucosaminyltransferase на US National Library of Medicine Medical Subject Headings Ова страница је последњи пут.

N-Acetylglucosaminyltransferase I (GnT-I), which catalyzes the transfer of an N-acetylglucosamine residue from UDP-N-acetylglucosamine to the α1,3-linked mannose on Man 5 GlcNAc 2 (M5), is a critical enzyme for the synthesis of high-mannose-type to complex-type glycan structures in N-linked glycan developed a large-scale preparation system for recombinant human.

A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc:α-D-mannoside β 1,6 N-acetylglucosaminyltransferase. Biol. Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (ECN-acetylglucosaminyltransferase I, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I, uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-acetylglucosaminyltransferase, UDP-N-acetylglucosaminyl:alpha-1,3-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase.

1. Introduction. Many studies show that alterations in N-linked oligosaccharides of tumor cells are associated with tumorigenesis, progression and metastasis.N-linked β(1,6)-N-acetylglucosamine (GlcNAc) synthesized by N-acetylglucosaminyltransferase Va (GnT-Va or Mgat5) is one of the more common glycans up-regulated during malignant transformation.

Previous reports have suggested that changes in oligosaccharide structures, especially β1–6 branching in N‐glycans, which are biosynthesized by UDP‐N‐acetylglucosamine:α mannoside β1,6 N‐acetylglucos. Manozil-oligosaharid 1,6-alfa-manozidaza (ECmanozidaza II, ekso-1,6-alfa-manozidaza, alfa-D-manozidaza II, alfa-manozidaza II, alfa,6-manozidaza, GlcNAc transferaza I-zavisna alfa1,3(alfa1,6)manozidaza, Golgi alfa-manozidaza II, ManII, 1,3(1,6)-alfa-D-manozidaza, 1,3-(1,6-)manozil-oligosaharid alfa-D-manohidrolaza) je enzim sa sistematskim imenom (1->3)-(1->6).

N-Acetylglucosaminyltransferase I (EC ) initiates the conversion of high-mannose asparagine-linked glycans to complex asparagine-linked glycans in plant as well as in animal cells. This Golgi enzyme is missing in the cgl mutant of Arabidopsis thaliana, and the mutant cells are unable to synthesize complex glycans.

A beta N-acetylglucosaminyltransferase (GnT-V) [EC ] which catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to alpha-Dmannoside has been purified up to.

Nishikawa Y, Pegg W, Paulsen H, Schachter H. Control of glycoprotein synthesis. Purification and characterization of rabbit liver UDP-N-acetylglucosamine:alphaD-mannoside beta-1,2-N-acetylglucosaminyltransferase I.

Details Behavioural characterization of mannoside acetylglucosaminyltransferase 5 (Mgat5) deficient mice. FB2

J Biol Chem. Jun 15; (17)– Laemmli UK. Shoreibah MG, Hindsgaul O, Pierce M. Purification and characterization of rat kidney UDP-N-acetylglucosamine: alphaD-mannoside beta-1,6-N-acetylglucosaminyltransferase. J Biol Chem.

Feb 15; (5)– N-glycan, a fundamental and versatile protein modification in mammals, plays critical roles in various physiological and pathological events including cancer progression. The formation of N-glycan branches catalyzed by specific N-acetylglucosaminyltransferases [GnT-III, GnT-IVs, GnT-V, GnT-IX (Vb)] and a fucosyltransferase, Fut8, provides functionally diverse N-glycosylated proteins.

UDP-galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) form heterologous complexes in the Golgi occurs in close proximity to mannosyl (α-1,6-)-glycoprotein β-1,6-N-acetylglucosaminyltransferase (Mgat5).In this study we analyzed whether NGT and both splice variants of UGT (UGT1 and UGT2) are able to interact with four different mannoside.

UDP-N-acetylglucosamine:alphaD-mannoside beta-1,2-N-acetylglucosaminyltransferase I is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows typical features of a type II transmembrane protein.

The protein is believed to be essential for normal embryogenesis. Brockhausen I, Hull E, Hindsgaul O, Schachter H, Shah RN, Michnick SW, Carver JP () Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc beta (GlcNAc beta ) Man alpha-R (GlcNAc to Man) betaN-acetylglucosaminyltransferase VI.J Biol Chem – PubMed Google Scholar.

Douglas, R.H.; Ballou, C.E.: Purification of an α-N-acetylglucosaminyltransferase from the yeast Kluyveromyces lactis and a study of mutants defective in this enzyme activity.

Biochemistry, 21, – () PubMed CrossRef Google Scholar. The human UDP-N-Acetylglucosamine:alphad-Mannoside-beta-1,2-N-Acetylglucosaminyltransferase II Gene (MGAT2).

Cloning of Genomic DNA, Localization to Chromosome 14q21, Expression in Insect Cells and Purification of the Recombinant Protein. European Journal of Biochemistry(2), DOI: /jtbx. A key enzyme in regulating the maturation of N-linked glycans is UDP-N-acetylglucosamine:αd-mannoside β-1,2-N-acetylglucosaminyltransferase I (GlcNAc-TI, EC ).

Lec1 CHO cells lack GlcNAc-TI activity and synthesize only the oligomannosyl class of N-glycans. By contrast, Lec1A CHO mutants have weak GlcNAc-TI activity due to the reduced affinity of. The plasma α 1-antitrypsin (AT) of normal individuals has been reported to have four oligosaccharides per molecule; these oligosaccharides are all of the complex type, containing only three D-mannose (Man) residues per oligosaccharide as well as several residues of galactose, sialic acid, and N-acetyl-D-glucosamine (GlcNAc) (Chan, S.

K., Rees, D. C., Li, S.-C. &Li, Y.-T. () J.

Description Behavioural characterization of mannoside acetylglucosaminyltransferase 5 (Mgat5) deficient mice. FB2

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (ECN-acetylglucosaminyltransferase II, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II, acetylglucosaminyltransferase II, uridine diphosphoacetylglucosamine-mannoside alpha1->6-acetylglucosaminyltransferase, uridine.

α-Mannoside β-1,6-N-acetylglucosaminyltransferase V (MGAT5) is a mammalian glycosyltransferase involved in complex N-glycan formation, which strongly drives cancer when overexpressed. Despite intense interest, the catalytic mechanism of MGAT5 is not known in detail, precluding therapeutic exploitation.

We solved structures of MGAT5 complexed to glycosyl donor and acceptor ligands. Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta branch on the GlcNAcbetaManalpha arm of the core structure of N-linked glycans.

Essential for the production of tri- and tetra-antennary N-linked sugar chains. Request PDF | N-Acetylglucosaminyltransferase-II | The synthesis of complex N-glycans can be divided into three distinct stages. The first stage occurs primarily in the cytoplasm and rough.UDP‐GlcNAc:α‐6–D‐mannoside [GlcNAc to Manα1–6] β‐1,2‐N‐acetylglucosaminyltransferase II (GlcNAc‐T II, EC ) is a Golgi enzyme catalyzing an essential step in the conversion of oligo‐mannbse to complex N‐glycans.A ‐kb probe from a rat liver cDNA encoding GlcNAc‐T II was used to screen a human genomic DNA library in λEMBL3.Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.).

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