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Mgat5  -  mannoside acetylglucosaminyltransferase 5

Mus musculus

Synonyms: 4930471A21Rik, 5330407H02Rik, AI480971, Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A, Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase, ...
 
 
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Disease relevance of Mgat5

 

High impact information on Mgat5

 

Biological context of Mgat5

 

Anatomical context of Mgat5

  • Sequences of the mouse N-acetylglucosaminyltransferase V (Mgat5) mRNA and an mRNA expressed by an Mgat5-deficient cell line [2].
  • We generated Mgat5-deficient mice by gene targeting methods in embryonic stem cells, and observed a complex phenotype in adult mice including susceptibility to autoimmune disease, reduced cancer progression and a behavioral defect [10].
  • A common feature of cells in basal epithelia and in the cortical neural epithelium is the capacity to migrate, a cellular function which may require GlcNAc-TV-dependent glycoconjugates [11].
  • Leukoagglutinin (L-PHA)-reactive oligosaccharides co-localized with GlcNAc-TV transcripts in skin, kidney and intestine, but brain showed unexpectedly low overall staining punctuated by bright staining of the vascular endothelium [11].
  • 5. GlcNAc-TV transcripts were absent at E7, became expressed throughout E9.5 embryos, and then progressively restricted to regions of the developing central nervous system and to specialized epithelia of skin, intestine, kidney, endocrine tissues and respiratory tract [11].
 

Associations of Mgat5 with chemical compounds

 

Physical interactions of Mgat5

 

Regulatory relationships of Mgat5

  • Antibodies to the galectin-3 N-terminal oligomerization domain stimulate alpha5beta1 activation and recruitment to fibrillar adhesions in Mgat5(+/+) cells, an effect that is blocked by disrupting galectin-glycan binding [14].
  • These data suggest that a specific induction of GlcNAc-T V occurs after transfection with either the proto- or activated Ha-ras oncogenes, which is responsible for the increased beta 1-6 branching previously observed [15].
 

Other interactions of Mgat5

  • We previously demonstrated that beta1,6GlcNAc-branched complex-type (N-acetylglucosaminyltransferase V (Mgat5)) N-glycans on TCR are bound to galectins, an interaction that reduces TCR signaling by opposing agonist-induced TCR clustering at the immune synapse [1].
  • Similarly, CHO and MDAY-D2 mutants defective in GlcNAc-TV (i.e., Lec4 and KBL-1 respectively), which also reduces metastatic potential, showed increases in TIMP transcript levels [16].

References

  1. N-acetylglucosaminyltransferase V (Mgat5)-mediated N-glycosylation negatively regulates Th1 cytokine production by T cells. Morgan, R., Gao, G., Pawling, J., Dennis, J.W., Demetriou, M., Li, B. J. Immunol. (2004) [Pubmed]
  2. Sequences of the mouse N-acetylglucosaminyltransferase V (Mgat5) mRNA and an mRNA expressed by an Mgat5-deficient cell line. Alverez, K., Haswell, C., St Clair, M., Perng, G.S., Shorebah, M., Pierce, M., Fregien, N. Glycobiology (2002) [Pubmed]
  3. The her-2/neu oncogene stimulates the transcription of N-acetylglucosaminyltransferase V and expression of its cell surface oligosaccharide products. Chen, L., Zhang, W., Fregien, N., Pierce, M. Oncogene (1998) [Pubmed]
  4. Preparation of antisera to recombinant, soluble N-acetylglucosaminyltransferase V and its visualization in situ. Chen, L., Zhang, N., Adler, B., Browne, J., Freigen, N., Pierce, M. Glycoconj. J. (1995) [Pubmed]
  5. Glycoprotein glycosylation and cancer progression. Dennis, J.W., Granovsky, M., Warren, C.E. Biochim. Biophys. Acta (1999) [Pubmed]
  6. Knockdown of Mgat5 inhibits breast cancer cell growth with activation of CD4+ T cells and macrophages. Li, D., Li, Y., Wu, X., Li, Q., Yu, J., Gen, J., Zhang, X.L. J. Immunol. (2008) [Pubmed]
  7. Identification and characterization of a gene regulating enzymatic glycosylation which is induced by diabetes and hyperglycemia specifically in rat cardiac tissue. Nishio, Y., Warren, C.E., Buczek-Thomas, J.A., Rulfs, J., Koya, D., Aiello, L.P., Feener, E.P., Miller, T.B., Dennis, J.W., King, G.L. J. Clin. Invest. (1995) [Pubmed]
  8. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. Demetriou, M., Nabi, I.R., Coppolino, M., Dedhar, S., Dennis, J.W. J. Cell Biol. (1995) [Pubmed]
  9. Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Partridge, E.A., Le Roy, C., Di Guglielmo, G.M., Pawling, J., Cheung, P., Granovsky, M., Nabi, I.R., Wrana, J.L., Dennis, J.W. Science (2004) [Pubmed]
  10. UDP-N-acetylglucosamine:alpha-6-D-mannoside beta1,6 N-acetylglucosaminyltransferase V (Mgat5) deficient mice. Dennis, J.W., Pawling, J., Cheung, P., Partridge, E., Demetriou, M. Biochim. Biophys. Acta (2002) [Pubmed]
  11. GlcNAc-transferase V and core 2 GlcNAc-transferase expression in the developing mouse embryo. Granovsky, M., Fode, C., Warren, C.E., Campbell, R.M., Marth, J.D., Pierce, M., Fregien, N., Dennis, J.W. Glycobiology (1995) [Pubmed]
  12. Isolation, characterization and inactivation of the mouse Mgat3 gene: the bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction. Priatel, J.J., Sarkar, M., Schachter, H., Marth, J.D. Glycobiology (1997) [Pubmed]
  13. Minimal catalytic domain of N-acetylglucosaminyltransferase V. Korczak, B., Le, T., Elowe, S., Datti, A., Dennis, J.W. Glycobiology (2000) [Pubmed]
  14. Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Lagana, A., Goetz, J.G., Cheung, P., Raz, A., Dennis, J.W., Nabi, I.R. Mol. Cell. Biol. (2006) [Pubmed]
  15. Induction of N-acetylglucosaminyltransferase V by elevated expression of activated or proto-Ha-ras oncogenes. Lu, Y., Chaney, W. Mol. Cell. Biochem. (1993) [Pubmed]
  16. Inhibition of N-linked oligosaccharide processing in tumor cells is associated with enhanced tissue inhibitor of metalloproteinases (TIMP) gene expression. Korczak, B., Dennis, J.W. Int. J. Cancer (1993) [Pubmed]
 
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