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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

GALNT2  -  polypeptide N-acetylgalactosaminyltransfer...

Homo sapiens

Synonyms: GalNAc-T2, Polypeptide GalNAc transferase 2, Polypeptide N-acetylgalactosaminyltransferase 2, Protein-UDP acetylgalactosaminyltransferase 2, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, ...
 
 
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Disease relevance of GALNT2

 

High impact information on GALNT2

  • To mark the Golgi in HeLa cells, we stably expressed the Golgi stack enzyme N-acetylgalactosaminyltransferase-2 (GalNAc-T2) fused to the green fluorescent protein (GFP) or to an 11-amino acid epitope, VSV-G (VSV), and the trans/TGN enzyme beta1,4-galactosyltransferase (GalT) fused to GFP [2].
  • Two of the GalNAc-transferases, GalNAc-T1 and GalNAc-T2, were expressed constitutively and at low levels in most or all cell lines examined [3].
  • Other pp-GalNAc-Ts exhibited different substrate specificities from pp-GalNAc-T2; however, their activities were extremely weak [4].
  • These results strongly suggested that pp-GalNAc-T2 is an essential enzyme for initiation of O-linked glycosylation of the IgA1 hinge region [4].
  • GalNAc-T1 and -T3 showed strict donor substrate specificities for UDP-GalNAc, whereas GalNAc-T2 also utilized UDP-Gal with one peptide acceptor substrate [5].
 

Anatomical context of GALNT2

  • RESULTS: Immunohistochemical studies revealed the presence of GalNAc-T2, -T3, and -T4 isoforms within the stratified epithelium of the cornea and the conjunctiva [6].
 

Associations of GALNT2 with chemical compounds

  • Evidence from in vitro glycosylation with polypeptide N-acetylgalactosaminyltransferases GalNAc-T1 and GalNAc-T2 in concert with mass spectrometric analyses of in vivo glycosylated MUC1 probes from transiently transfected HEK293 cells indicated reduced glycosylation densities of repeats with three concerted replacements: AHGVTSAPESRPAPGSTAPA [7].
 

Other interactions of GALNT2

  • GalNAc-T1 distributes evenly across the Golgi stack whereas GalNAc-T2 and -T3 reside preferentially on the trans side and in the medial part of the Golgi stack, respectively [8].
  • The GalNAc-T4 isoenzyme was found in the apical cell layers, whereas GalNAc-T2 was found in the supranuclear region of the basal cell layers of both cornea and conjunctiva [6].
  • In all samples, apical GalNAc-T2 was absent, and GalNAc-T6 was entirely absent [6].

References

  1. Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. Mandel, U., Hassan, H., Therkildsen, M.H., Rygaard, J., Jakobsen, M.H., Juhl, B.R., Dabelsteen, E., Clausen, H. Glycobiology (1999) [Pubmed]
  2. Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. Storrie, B., White, J., Röttger, S., Stelzer, E.H., Suganuma, T., Nilsson, T. J. Cell Biol. (1998) [Pubmed]
  3. Expression of three UDP-N-acetyl-alpha-D-galactosamine:polypeptide GalNAc N-acetylgalactosaminyltransferases in adenocarcinoma cell lines. Sutherlin, M.E., Nishimori, I., Caffrey, T., Bennett, E.P., Hassan, H., Mandel, U., Mack, D., Iwamura, T., Clausen, H., Hollingsworth, M.A. Cancer Res. (1997) [Pubmed]
  4. Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. Iwasaki, H., Zhang, Y., Tachibana, K., Gotoh, M., Kikuchi, N., Kwon, Y.D., Togayachi, A., Kudo, T., Kubota, T., Narimatsu, H. J. Biol. Chem. (2003) [Pubmed]
  5. Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. Wandall, H.H., Hassan, H., Mirgorodskaya, E., Kristensen, A.K., Roepstorff, P., Bennett, E.P., Nielsen, P.A., Hollingsworth, M.A., Burchell, J., Taylor-Papadimitriou, J., Clausen, H. J. Biol. Chem. (1997) [Pubmed]
  6. The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization. Argüeso, P., Tisdale, A., Mandel, U., Letko, E., Foster, C.S., Gipson, I.K. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  7. Sequence-variant repeats of MUC1 show higher conformational flexibility, are less densely O-glycosylated and induce differential B lymphocyte responses. von Mensdorff-Pouilly, S., Kinarsky, L., Engelmann, K., Baldus, S.E., Verheijen, R.H., Hollingsworth, M.A., Pisarev, V., Sherman, S., Hanisch, F.G. Glycobiology (2005) [Pubmed]
  8. Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. Röttger, S., White, J., Wandall, H.H., Olivo, J.C., Stark, A., Bennett, E.P., Whitehouse, C., Berger, E.G., Clausen, H., Nilsson, T. J. Cell. Sci. (1998) [Pubmed]
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