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beta 1 4 n acetylgalactosaminyltransferase 2

beta 1 4 n acetylgalactosaminyltransferase 2

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beta 1 4 n acetylgalactosaminyltransferase 2
B4GALNT1 - Beta-1,4 N-acetylgalactosaminyltransferase 1 , B4GALNT2 - Beta-1,4 N-acetylgalactosaminyltransferase 2 , Beta-1,4 N-Acetylgalactosaminyltransferase 1,2 (B4GAL NT1 , Beta-1,4 N-Acetylgalactosaminyltransferase 1,2 (B4GALNT1,2 , B4GALNT2 beta-1,4-N-acetyl-galactosaminyltransferase 2 , Beta-1,4 N-acetylgalactosaminyltransferase 2 (Q8NHY0 , , , .
We use cookies to make interactions with our website easy and meaningful, to better understand the use of our services, and to tailor advertising. For further information, including about cookie settings, please read our Cookie Policy . By continuing to use this site, you consent to the use of cookies.Got itWe value your privacyWe use cookies to offer you a better experience, personalize content, tailor advertising, provide social media features, and better understand the use of our services.To learn more or modify/prevent the use of cookies, see our Cookie Policy and Privacy Policy.Accept CookiestopSee all ›3 ReferencesDownload citationShare Request full-textChapterfrom book Handbook of glycosyltransferases and related genes, second edition (pp.417-428)Beta-1,4 N-Acetylgalactosaminyltransferase 1,2 (B4GALNT1,2)Chapter · January 2014 with 11 ReadsDOI: 10.1007/978-4-431-54240-7_34Cite this publicationKoichi Furukawa47.18Nagoya UniversityY. Ohmi+ 2Yuki Ohkawa29.57Osaka International Cancer InstituteYoshio Yamauchi28.67The University of TokyoShow more authorsHideAbstractUDP-GalNAc: GM3 beta-1,4 N-acetylgalactosaminyltransferase (B4GALNT1) catalyzes the transfer of N-acetylgalactosamine from UDP-GalNAc to ganglioside GM3 (Nagata et al. 1992) as shown in Fig. 39.1. The product is GM2. However, this gene product could synthesize not only GM2 but also GD2 and asialo-GM2 (GA2) (Yamashiro et al. 1995) as previously predicted (Pohlentz et al. 1988). These structures are molecules locating at the starting point for the synthesis of mature gangliosides enriched in the nervous tissues such as brain and peripheral nerve tissues. Thus, these complex gangliosides were all deleted in the knockout mice of B4GALNT1 (Takamiya et al. 1996). In addition to the first cDNA clones responsible for the synthesis of GM2 and GD2, a similar enzyme with high homology was identified (Smith and Lowe 1994; Montiel et al. 2003). Thereafter, GM2/GD2/GA2 gene was designated B4GALNT1, and the latter has been called as B4GALNT2. Structures of acceptor substrates are very similar to each other (GM3 vs. sialylparagloboside), but the substrate specificities of them are clearly distinct, i.e., B4GALNT2 catalyzes the synthesis of Sda antigen (or Cad antigen), GalNAcβ1,4(α2,3NeuAc)Galβ1,4GlcNAc-R (Yamashiro et al. 1995). Following the cloning of mouse cDNA (Smith and Lowe 1994), human cDNA was isolated (Montiel et al. 2003). In human cDNAs of B4GALNT2, presence of two isoforms with different length in N-terminus (cytoplasmic region) was reported, while the implication of them has not been clarified (Montiel et al. 2003).Do you want to read the rest of this chapter?Request full-text Citations (0)References (3)This research hasn't been cited in any other publications.Biosynthesis of GlycolipidsChapterDec 2007ViewGangliosides play pivotal roles in the regulation of complement systems and in the maintenance of integrity in nerve tissuesArticleFull-text availableDec 2009Proc Natl Acad Sci Unit States AmGangliosides are considered to be essential in the maintenance and repair of nervous tissues; however, the mechanisms for neurodegeneration caused by ganglioside defects are unknown. We examined gene expression profiles in double knockout (DKO) mice of GM2/GD2 synthase and GD3 synthase genes and showed that the majority of complement genes and their receptors were up-regulated in cerebellum in DKO mice. Inflammatory reactions were demonstrated in those tissues by measuring up-regulated inflammatory cytokines, indicating the presence of complement activation and inflammation as reported in Alzheimer's disease. Immunoblotting of fractionated membrane extracts by sucrose density gradient revealed that complement-regulatory molecules such as decay-accelerating factor and CD59 were dispersed from glycolipid-enriched microdomain/rafts in DKO cerebellum. Immunohistostaining of these molecules showed disordered membrane localization. These results suggested that dysfunction of complement-regulatory molecules may be due to abnormal glycolipid-enriched microdomain/rafts that triggered complement activation, subsequent inflammation, and neurodegeneration in DKO mice. Generation of the triple KO mice lacking complement activity in addition to the two glycosyltransferases suggested that complement activation is involved in the inflammatory reactions and neurodegeneration caused by the ganglioside deficiency.ViewShow abstractSuppression by ganglioside GD1A of migration capability, adhesion to vitronectin and metastatic potential of highly metastatic FBJ-LL cellsArticleDec 1999INT J CANCERGanglioside GD1a, which is highly expressed in poorly metastatic FBJ-S1 cells, has been shown to inhibit the serum-induced migration capability of highly metastatic FBJ-LL cells. In the present study, the capacity of FBJ-S1 cells to adhere to vitronectin was found to be about half that of FBJ-LL cells. Pre-treatment of FBJ-LL cells with GD1a decreased this capacity by 30% that of the control, whereas GM1-pre-treatment caused only a 10% decrease, indicating that GD1a specifically inhibits FBJ-LL cell adhesion to vitronectin. Since FBJ-LL cells contain almost no GD1a, transfectants capable of expressing GD1a to varying degrees were produced in this study by transfection of FBJ-LL cells with GM2/GD2-synthase cDNA. Decrease in the serum-induced migration capacity of these transfectants was accompanied by an increment in GD1a expression. Adhesion of the transfectants to vitronectin decreased by 30% as compared with mock-transfected cells. Within 4 to 5 weeks after GD1a-expressing transfectant and mock-transfected cells were transplanted into mice, metastatic nodules were observed in liver, lung, kidney and adrenal glands of mock-transplanted mice, but not in those with GD1a-expressing transfectants, indicating that GD1a suppresses the metastasis of FBJ-osteosarcoma cells, possibly by inhibiting cell migration and cell adhesion. The involvement of the ganglioside in the suppression of metastasis is clearly demonstrated in the present study.ViewShow abstractJoin ResearchGate to find the people and research you need to help your work.15+ million members118+ million publications700k+ research projectsJoin for freeRecommendationsDiscover more publications, questions and projects in Nerve TissueProjecthistological characterization of degenerated nerve fibers in the galnglioside-knockout mice[...]View projectProjectNeuronal gangliosides as targets for antibody-mediated motor nerve degeneration[...]View projectArticleWisp2/CCN5 up-regulated in the central nervous system of GM3-only mice facilitates neurite formation...June 2011 · Biochemical and Biophysical Research Communications Yuki Ohkawa Yuhsuke OhmiO. Tajima[...] Koichi FurukawaWisp2/CCN5 belongs to CCN family proteins which are involved in cell proliferation, angiogenesis, tumorigenesis and wound healing. Although a number of studies on the roles of Wisp2/CCN5 in cancers have been reported, no study on the expression and function of Wisp2/CCN5 in the central nervous system has been reported. In this study, we focused on Wisp2/CCN5 that was up-regulated in nervous ... [Show full abstract] tissues in GM3-only mice. Over-expression of Wisp2/CCN5 enhanced neurite outgrowth potently after serum withdrawal with increased phosphorylation levels of Akt and ERKs. When cells were cultured with recombinant Wisp2/CCN5 proteins, more and longer neurites were formed than in the controls. Thus, we demonstrated for the first time that Wisp2/CCN5 facilitates neurite formation in a mouse neuroblastoma cell line, Neuro2a. Akt phosphorylation induced by recombinant Wisp2/CCN5 was suppressed after knockdown of integrin β1. Moreover, Wisp2/CCN5-over-expressing cells were resistant to apoptosis induced by H(2)O(2). These results suggested that secreted Wisp2/CCN5 induces Akt and ERK phosphorylation via integrins, and consequently facilitates neurite formation and conferred resistance to apoptosis. Up-regulation of Wisp2/CCN5 in GM3-only mice should be, therefore, a reaction to protect nervous tissues from neurodegeneration caused by ganglioside deficiency.Read moreArticleGangliosides: Synthesis and Function in Nervous TissuesOctober 2015Keiko Furukawa Yuhsuke Ohmi Yuki Ohkawa[...]O. TajimaGangliosides, sialic acid-containing glycosphingolipids, have been considered to be involved in the development and functions of the nervous system. Recent progress in the genetic analysis of gangliosides in cultured cells and experimental animals revealed their roles in the maintenance of integrity of nervous tissues and neuroregeneration. The fact that ganglioside-deficient mice exhibited ... [Show full abstract] milder abnormalities than expected suggests that compensatory actions of remaining glycolipids might be present, and complex knockout of multiple glycosyltransferase genes might be useful to clarify essential roles of gangliosides.Read moreArticleGangliosides are essential in the protection of inflammation and neurodegeneration via maintenance o...March 2011 · Journal of Neurochemistry Yuhsuke OhmiO. Tajima Yuki Ohkawa[...] Koichi FurukawaJ. Neurochem. (2011) 116, 926–935.. Disease description A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs.. Involved in the synthesis of the Sd(a) antigen (Sia-alpha2,3-[GalNAc-beta1,4]Gal-beta1,4-GlcNAc), a carbohydrate determinant expressed on erythrocytes, the colonic mucosa and other tissues..
Abstract. UDP-GalNAc: GM3 beta-1,4 N-acetylgalactosaminyltransferase (B4GALNT1) catalyzes the transfer of N-acetylgalactosamine from UDP-GalNAc to ganglioside GM3 . UDP-GalNAc: GM3 beta-1,4 N-acetylgalactosaminyltransferase (B4GALNT1) catalyzes the transfer of N-acetylgalactosamine from UDP-GalNAc to ganglioside GM3 (Nagata et al . Gene ID: 124872, updated on 6-Dec-2016. Summary. B4GALNT2 catalyzes the last step in the biosynthesis of the human Sd(a) antigen through the addition of an N-acetylgalactosamine residue via a beta-1,4 linkage to a subterminal galactose residue substituted with an alpha-2,3-linked sialic acid.. InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.. . .
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