n acetylgalactosaminyltransferases


Summary: Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

Top Publications

  1. Bennett E, Hassan H, Clausen H. cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. J Biol Chem. 1996;271:17006-12 pubmed
    ..Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3. ..
  2. Wandall H, Hassan H, Mirgorodskaya E, Kristensen A, Roepstorff P, Bennett E, et al. Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997;272:23503-14 pubmed
    ..The results demonstrate that individual GalNAc-transferases have distinct activities and the initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases. ..
  3. Brooks S, Carter T, Bennett E, Clausen H, Mandel U. Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer. Acta Histochem. 2007;109:273-84 pubmed
  4. Benet Pages A, Orlik P, Strom T, Lorenz Depiereux B. An FGF23 missense mutation causes familial tumoral calcinosis with hyperphosphatemia. Hum Mol Genet. 2005;14:385-90 pubmed
    ..These results suggest that the FGF23 function is decreased by absent or extremely reduced secretion of intact FGF23. We conclude that FGF23 mutations in hypophosphatemic rickets and FTC have opposite effects on phosphate homeostasis. ..
  5. Kato K, Jeanneau C, Tarp M, Benet Pages A, Lorenz Depiereux B, Bennett E, et al. Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation. J Biol Chem. 2006;281:18370-7 pubmed
    ..The study suggests a novel posttranslational regulatory model of FGF23 involving competing O-glycosylation and protease processing to produce intact FGF23. ..
  6. Dosaka Akita H, Kinoshita I, Yamazaki K, Izumi H, Itoh T, Katoh H, et al. N-acetylgalactosaminyl transferase-3 is a potential new marker for non-small cell lung cancers. Br J Cancer. 2002;87:751-5 pubmed
    ..04; P=0.03), and in pStage I nonsquamous cell carcinomas (hazards ratio, 2.70; P=0.03). These results suggest that GalNAc-T3 is a new marker of non-small cell lung cancers with specificity for histology and prognosis. ..
  7. Wang H, Tachibana K, Zhang Y, Iwasaki H, Kameyama A, Cheng L, et al. Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14. Biochem Biophys Res Commun. 2003;300:738-44 pubmed
    ..Our results provide evidence that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and suggest that pp-GalNAc-T14 may be involved in the O-glycosylation in kidney. ..
  8. Cheng L, Tachibana K, Iwasaki H, Kameyama A, Zhang Y, Kubota T, et al. Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15. FEBS Lett. 2004;566:17-24 pubmed
    ..These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity. ..
  9. Topaz O, Bergman R, Mandel U, Maor G, Goldberg R, Richard G, et al. Absence of intraepidermal glycosyltransferase ppGalNac-T3 expression in familial tumoral calcinosis. Am J Dermatopathol. 2005;27:211-5 pubmed
    ..Our data provide for the first time evidence for ppGalNAc-T3 deficiency in the skin of HFTC patients and suggest that immunostaining of skin biopsy samples for ppGal-Nac-T3 might be a useful tool for the diagnosis of HFTC. ..

More Information


  1. Berois N, Mazal D, Ubillos L, Trajtenberg F, Nicolas A, Sastre Garau X, et al. UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 as a new immunohistochemical breast cancer marker. J Histochem Cytochem. 2006;54:317-28 pubmed
    ..Considering that an abnormal O-glycosylation greatly contributes to the phenotype and biology of breast cancer cells, ppGalNAc-T6 expression could provide new insights about breast cancer glycobiology. ..
  2. Swerts K, de Moerloose B, Dhooge C, Vandesompele J, Hoyoux C, Beiske K, et al. Potential application of ELAVL4 real-time quantitative reverse transcription-PCR for detection of disseminated neuroblastoma cells. Clin Chem. 2006;52:438-45 pubmed
    ..However, combination of several molecular markers and screening techniques should be considered to ensure reliable detection of rare neuroblastoma cells. ..
  3. Campagnoli M, Pucci A, Garelli E, Carando A, Defilippi C, Lala R, et al. Familial tumoral calcinosis and testicular microlithiasis associated with a new mutation of GALNT3 in a white family. J Clin Pathol. 2006;59:440-2 pubmed
    ..Autoimmune diseases are present in several members of the family. Although immune disorders have been described in FTC, autoimmunity does not segregate with the GALNT3 mutation in this family. ..
  4. Wang J, Ban M, Zou G, Cao H, Lin T, Kennedy B, et al. Polygenic determinants of severe hypertriglyceridemia. Hum Mol Genet. 2008;17:2894-9 pubmed publisher
    ..At the extremes of a quantitative trait, such as severe HTG, are found the cumulative contributions of both multiple rare alleles with large genetic effects and common alleles with small effects. ..
  5. Hagen F, Van Wuyckhuyse B, Tabak L. Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase. J Biol Chem. 1993;268:18960-5 pubmed
    ..Alternatively, there may be additional factors required to enhance the glycosylation of serine residues in vivo. ..
  6. Brockhausen I, Dowler T, Paulsen H. Site directed processing: role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2. Biochim Biophys Acta. 2009;1790:1244-57 pubmed publisher
    ..Knowledge of site directed processing enhances our understanding of the control of O-glycosylation in normal cells and in disease. ..
  7. Wandall H, Irazoqui F, Tarp M, Bennett E, Mandel U, Takeuchi H, et al. The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation. Glycobiology. 2007;17:374-87 pubmed
    ..The results suggest that GalNAc-transferase lectins serve to modulate the kinetic properties of the enzymes in the late stages of the initiation process of O-glycosylation to accomplish dense or complete O-glycan occupancy. ..
  8. Inoue T, Eguchi T, Oda Y, Nishiyama K, Fujii K, Izumi H, et al. Expression of GalNAc-T3 and its relationships with clinicopathological factors in 61 extrahepatic bile duct carcinomas analyzed using stepwise sections - special reference to its association with lymph node metastases-. Mod Pathol. 2007;20:267-76 pubmed
    ..Clinically, preoperative evaluation of GalNAc-T3 expression is considered to be useful for decisions regarding operative procedures. ..
  9. Tenno M, Ohtsubo K, Hagen F, Ditto D, Zarbock A, Schaerli P, et al. Initiation of protein O glycosylation by the polypeptide GalNAcT-1 in vascular biology and humoral immunity. Mol Cell Biol. 2007;27:8783-96 pubmed
    ..These findings reveal that the initiation of protein O glycosylation by ppGalNAcT-1 provides a distinctive repertoire of advantageous functions that support vascular responses and humoral immunity. ..
  10. Ten Hagen K, Tran D, Gerken T, Stein D, Zhang Z. Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster. J Biol Chem. 2003;278:35039-48 pubmed
    ..The characterization reported here provides additional insight into the use of this model system to dissect the biological role of this enzyme family in vivo during both fly and mammalian development. ..
  11. Storrie B, White J, Rottger S, Stelzer E, Suganuma T, Nilsson T. Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J Cell Biol. 1998;143:1505-21 pubmed
    ..In conclusion, we have shown that Golgi-resident glycosylation enzymes recycle through the ER and that this novel pathway is the likely explanation for the nocodazole-induced Golgi scattering observed in interphase cells. ..
  12. Gerken T, Zhang J, Levine J, Elhammer A. Mucin core O-glycosylation is modulated by neighboring residue glycosylation status. Kinetic modeling of the site-specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases . J Biol Chem. 2002;277:49850-62 pubmed
  13. Kingsley P, Hagen K, Maltby K, Zara J, Tabak L. Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development. Glycobiology. 2000;10:1317-23 pubmed
    ..5 maxilla and mandible underlying the dental lamina. The unique spatiotemporal expression of the different ppGaNTase family members during development suggests unique roles for each of these gene products. ..
  14. Sato T, Gotoh M, Kiyohara K, Akashima T, Iwasaki H, Kameyama A, et al. Differential roles of two N-acetylgalactosaminyltransferases, CSGalNAcT-1, and a novel enzyme, CSGalNAcT-2. Initiation and elongation in synthesis of chondroitin sulfate. J Biol Chem. 2003;278:3063-71 pubmed
    ..Quantitative real-time PCR analysis revealed that CSGalNAcT-2 transcripts were highly expressed in the small intestine, leukocytes, and spleen, however, both CSGalNAcTs were ubiquitously expressed in various tissues. ..
  15. Ten Hagen K, Tran D. A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster. J Biol Chem. 2002;277:22616-22 pubmed
    ..This study provides the first direct evidence for the involvement of a member of this conserved multigene family in eukaryotic development and viability. ..
  16. Miyahara N, Shoda J, Kawamoto T, Furukawa M, Ueda T, Todoroki T, et al. Expression of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetylgalactosaminyltransferase isozyme 3 in the subserosal layer correlates with postsurgical survival of pathological tumor stage 2 carcinoma of the gallbladder. Clin Cancer Res. 2004;10:2090-9 pubmed
    ..This phenotype may serve as a unique biological feature associated with the malignant behavior. ..
  17. Ten Hagen K, Bedi G, Tetaert D, Kingsley P, Hagen F, Balys M, et al. Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9. J Biol Chem. 2001;276:17395-404 pubmed
    ..These findings lend further support to the existence of a hierarchical network of differential enzymatic activity within the diversely regulated ppGaNTase family, which may play a role in the various processes governing development. ..
  18. Zhang Y, Iwasaki H, Wang H, Kudo T, Kalka T, Hennet T, et al. Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen. J Biol Chem. 2003;278:573-84 pubmed
    ..pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons. ..
  19. Mohlke K, Purkayastha A, Westrick R, Smith P, Petryniak B, Lowe J, et al. Mvwf, a dominant modifier of murine von Willebrand factor, results from altered lineage-specific expression of a glycosyltransferase. Cell. 1999;96:111-20 pubmed
    ..These findings identify alterations in glycosyltransferase function as a potential general mechanism for the genetic modification of plasma protein levels. ..
  20. Specktor P, Cooper J, Indelman M, Sprecher E. Hyperphosphatemic familial tumoral calcinosis caused by a mutation in GALNT3 in a European kindred. J Hum Genet. 2006;51:487-90 pubmed
    ..The present results expand the spectrum of known mutations in GALNT3 and demonstrate the existence of HFTC-causing mutations in this gene outside the Middle Eastern and African-American populations. ..
  21. Landers K, Burger M, Tebay M, Purdie D, Scells B, Samaratunga H, et al. Use of multiple biomarkers for a molecular diagnosis of prostate cancer. Int J Cancer. 2005;114:950-6 pubmed
    ..Supplemental material for this article can be found on the International Journal of Cancer website at http://www.interscience.wiley.com/jpages/0020-7136/suppmat/index.html.) ..
  22. Gerken T, Tep C, Rarick J. Role of peptide sequence and neighboring residue glycosylation on the substrate specificity of the uridine 5'-diphosphate-alpha-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyl transferases T1 and T2: kinetic modeling of the porcine and canin. Biochemistry. 2004;43:9888-900 pubmed
  23. Topaz O, Shurman D, Bergman R, Indelman M, Ratajczak P, Mizrachi M, et al. Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat Genet. 2004;36:579-81 pubmed
    ..Sequence analysis of GALNT3 identified biallelic deleterious mutations in all individuals with FTC, suggesting that defective post-translational modification underlies the disease. ..
  24. Kitagawa H, Izumikawa T, Uyama T, Sugahara K. Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. J Biol Chem. 2003;278:23666-71 pubmed
    ..Thus, the ChPF is required for chondroitin polymerizing activity of mammalian ChSy. ..
  25. Stolz A, Haines N, Pich A, Irvine K, Hokke C, Deelder A, et al. Distinct contributions of beta 4GalNAcTA and beta 4GalNAcTB to Drosophila glycosphingolipid biosynthesis. Glycoconj J. 2008;25:167-75 pubmed
  26. Kawar Z, van Die I, Cummings R. Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans. J Biol Chem. 2002;277:34924-32 pubmed
    ..The identification and availability of this novel enzyme should enhance our understanding of the structure and function of LDN-containing glycoconjugates. ..
  27. Elhammer A, Kezdy F, Kurosaka A. The acceptor specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycoconj J. 1999;16:171-80 pubmed
    ..Results from substrate binding studies suggest that GalNAc-T catalyzed transfer proceeds via an ordered sequential mechanism. ..
  28. Bennett E, Hassan H, Mandel U, Hollingsworth M, Akisawa N, Ikematsu Y, et al. Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J Biol Chem. 1999;274:25362-70 pubmed
    ..The results demonstrate the existence of genetic redundancy of a polypeptide GalNAc-transferase that does not provide full functional redundancy. ..
  29. Takamiya K, Yamamoto A, Yamashiro S, Shin M, Okada M, Fukumoto S, et al. Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but exhibit only subtle defects in their nervous system. Proc Natl Acad Sci U S A. 1996;93:10662-7 pubmed
    ..The higher levels of GM3 and GD3 expressed in the brains of these mutant mice may be able to compensate for the lack of complex gangliosides. ..
  30. White T, Bennett E, Takio K, Sørensen T, Bonding N, Clausen H. Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995;270:24156-65 pubmed
    ..The data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members. ..
  31. Fritz T, Hurley J, Trinh L, Shiloach J, Tabak L. The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1. Proc Natl Acad Sci U S A. 2004;101:15307-12 pubmed
  32. Hanisch F, Reis C, Clausen H, Paulsen H. Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides. Glycobiology. 2001;11:731-40 pubmed
    ..These findings are in accord with the inhibition of rGalNAc-T2 and -T4 by fully GalNAc-substituted MUC1 repeat peptide and support a glycosylation-dependent activity induction or enhancement of both enzymes. ..
  33. Gu C, Oyama T, Osaki T, Li J, Takenoyama M, Izumi H, et al. Low expression of polypeptide GalNAc N-acetylgalactosaminyl transferase-3 in lung adenocarcinoma: impact on poor prognosis and early recurrence. Br J Cancer. 2004;90:436-42 pubmed
    ..019, rr=3.05, respectively). The low expression of GalNAc-T3 may be a useful marker for predicting poor prognosis and early recurrence in completely resected lung carcinoma patients, particularly patients with stage I diseases. ..
  34. Shibao K, Izumi H, Nakayama Y, Ohta R, Nagata N, Nomoto M, et al. Expression of UDP-N-acetyl-alpha-D-galactosamine-polypeptide galNAc N-acetylgalactosaminyl transferase-3 in relation to differentiation and prognosis in patients with colorectal carcinoma. Cancer. 2002;94:1939-46 pubmed
    ..GalNAc-T3 expression is a novel and useful indicator of tumor differentiation, disease aggressiveness, and prognosis in patients with colorectal carcinoma. ..
  35. Hang H, Bertozzi C. The chemistry and biology of mucin-type O-linked glycosylation. Bioorg Med Chem. 2005;13:5021-34 pubmed
    ..The review discusses the significance of mucin-type O-linked glycosylation initiated by the polypeptide N-acetylgalactosaminyltransferases in biology and development of chemical tools to study these enzymes and their substrates. ..
  36. Okajima T, Nakamura Y, Uchikawa M, Haslam D, Numata S, Urano T, et al. Expression cloning of human globoside synthase cDNAs. Identification of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta 1,3-N-acetylgalactosaminyltransferase. J Biol Chem. 2000;275:40498-503 pubmed
    ..The globoside synthase gene was expressed in many tissues, such as heart, brain, testis, etc. We propose the designation beta3GalNAc-T1 for the cloned globoside synthase gene. ..
  37. Zhang L, Zhang Y, Hagen K. A mucin-type O-glycosyltransferase modulates cell adhesion during Drosophila development. J Biol Chem. 2008;283:34076-86 pubmed publisher
    ..This study provides the first evidence for the role of O-glycosylation in a developmentally regulated, integrin-mediated, cell adhesion event and reveals a novel player in wing blade formation during Drosophila development. ..
  38. Tian E, Ten Hagen K. Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj J. 2009;26:325-34 pubmed publisher
    ..Gaining an understanding of mucin-type O-glycans in these diverse systems will elucidate crucial conserved processes underlying many aspects of development and homeostasis. ..
  39. Tarp M, Clausen H. Mucin-type O-glycosylation and its potential use in drug and vaccine development. Biochim Biophys Acta. 2008;1780:546-63 pubmed
    ..The present review will highlight some of the potential applications of site-directed O-glycosylation. ..
  40. Guo J, Zhang Y, Cheng L, Iwasaki H, Wang H, Kubota T, et al. Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12. FEBS Lett. 2002;524:211-8 pubmed
    ..Since mucins are glycoproteins mainly produced in the digestive organs, our results suggest that pp-GalNAc-T12 plays an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. ..
  41. Barbieri A, Filopanti M, Bua G, Beck Peccoz P. Two novel nonsense mutations in GALNT3 gene are responsible for familial tumoral calcinosis. J Hum Genet. 2007;52:464-8 pubmed
    ..This is the first report describing the simultaneous presence of two different stop codons in the coding sequence of the GALNT3 gene. ..
  42. Gerken T, Raman J, Fritz T, Jamison O. Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates. J Biol Chem. 2006;281:32403-16 pubmed
    ..Such information will be invaluable for identifying isoform-specific peptide acceptors, creating isoform-specific substrates, and predicting O-glycosylation sites. ..
  43. White K, Lorenz B, Evans W, Meitinger T, Strom T, Econs M. Molecular cloning of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate autosomal dominant hypophosphatemic rickets (ADHR) gene. Gene. 2000;246:347-56 pubmed
    ..In summary, these studies identified the human GalNAc-T8 gene, as well as multiple genomic polymorphisms that will be useful for further understanding the structure-function relations of the ppGaNTases. ..
  44. Sato T, Gotoh M, Kiyohara K, Kameyama A, Kubota T, Kikuchi N, et al. Molecular cloning and characterization of a novel human beta 1,4-N-acetylgalactosaminyltransferase, beta 4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, galNAc beta 1-4GlcNAc. J Biol Chem. 2003;278:47534-44 pubmed
    ..These results suggest that beta 4GalNAc-T3 could transfer GalNAc residues, producing N,N'-diacetylgalactosediamine structures at least in N-glycans and probably in both N- and O-glycans. ..
  45. Tian E, Ten Hagen K. O-linked glycan expression during Drosophila development. Glycobiology. 2007;17:820-7 pubmed
    ..This information will aid us in identifying the in vivo substrates of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltranferases, in a continuing effort to define the biological role of O-linked glycoproteins during development. ..
  46. Cheng L, Tachibana K, Zhang Y, Guo J, Kahori Tachibana K, Kameyama A, et al. Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10. FEBS Lett. 2002;531:115-21 pubmed
    ..In a polypeptide GalNAc-transfer assay, recombinant pp-GalNAc-T10 transferred GalNAc onto a panel of mucin-derived peptide substrates. Furthermore, pp-GalNAc-T10 demonstrated strong transferase activity with glycopeptide substrates. ..
  47. Yamashita T, Wu Y, Sandhoff R, Werth N, Mizukami H, Ellis J, et al. Interruption of ganglioside synthesis produces central nervous system degeneration and altered axon-glial interactions. Proc Natl Acad Sci U S A. 2005;102:2725-30 pubmed
    ..These results indicate that ganglioside synthesis is essential for the development of a stable CNS, possibly by means of the promotion of interactions between axon and glia. ..
  48. Montiel M, Krzewinski Recchi M, Delannoy P, Harduin Lepers A. Molecular cloning, gene organization and expression of the human UDP-GalNAc:Neu5Acalpha2-3Galbeta-R beta1,4-N-acetylgalactosaminyltransferase responsible for the biosynthesis of the blood group Sda/Cad antigen: evidence for an unusual extended cytopl. Biochem J. 2003;373:369-79 pubmed
  49. Sakai K, Kimata K, Sato T, Gotoh M, Narimatsu H, Shinomiya K, et al. Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical role in chondroitin sulfate synthesis in cartilage. J Biol Chem. 2007;282:4152-61 pubmed
    ..Our studies may lead to a new therapeutic intervention, ameliorating the outcome of cartilage degenerative diseases. ..
  50. Bennett E, Hassan H, Mandel U, Mirgorodskaya E, Roepstorff P, Burchell J, et al. Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. J Biol Chem. 1998;273:30472-81 pubmed
  51. Ichikawa S, Sorenson A, Austin A, Mackenzie D, Fritz T, Moh A, et al. Ablation of the Galnt3 gene leads to low-circulating intact fibroblast growth factor 23 (Fgf23) concentrations and hyperphosphatemia despite increased Fgf23 expression. Endocrinology. 2009;150:2543-50 pubmed publisher
    ..Our findings indicate that Galnt3-deficient mice have a biochemical phenotype of tumoral calcinosis and provide in vivo evidence that Galnt3 plays an essential role in proper secretion of Fgf23 in mice. ..
  52. Uyama T, Kitagawa H, Tanaka J, Tamura J, Ogawa T, Sugahara K. Molecular cloning and expression of a second chondroitin N-acetylgalactosaminyltransferase involved in the initiation and elongation of chondroitin/dermatan sulfate. J Biol Chem. 2003;278:3072-8 pubmed
  53. Toba S, Tenno M, Konishi M, Mikami T, Itoh N, Kurosaka A. Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9). Biochim Biophys Acta. 2000;1493:264-8 pubmed
    ..Northern blot analysis revealed the mRNA expression of the enzyme to be confined to the brain. The brain-specific expression of GalNAc-T9 suggested that this isozyme catalyzes O-glycosylation in the brain. ..