Reference - Detail
| RRC ID | 41712 |
|---|---|
| Author | Zhang Y, Iwasaki H, Wang H, Kudo T, Kalka TB, Hennet T, Kubota T, Cheng L, Inaba N, Gotoh M, Togayachi A, Guo J, Hisatomi H, Nakajima K, Nishihara S, Nakamura M, Marth JD, Narimatsu H. |
| Title | 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. |
| Journal | J Biol Chem |
| Abstract |
To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons. |
| Volume | 278(1) |
| Pages | 573-84 |
| Published | 2003-1-3 |
| DOI | 10.1074/jbc.M203094200 |
| PII | S0021-9258(19)31307-9 |
| PMID | 12407114 |
| MeSH | Amino Acid Sequence Animals Antigens, Tumor-Associated, Carbohydrate / immunology Antigens, Tumor-Associated, Carbohydrate / metabolism* Astrocytes / cytology Astrocytes / metabolism Base Sequence Cells, Cultured Cerebellar Cortex / cytology Cerebellar Cortex / metabolism Chromatography, High Pressure Liquid Cloning, Molecular Glycopeptides / metabolism Glycosylation Humans Membrane Glycoproteins / metabolism Mice Mice, Knockout Molecular Sequence Data Mucin 5AC Mucins / metabolism N-Acetylgalactosaminyltransferases / genetics N-Acetylgalactosaminyltransferases / metabolism* Neurons / cytology Neurons / physiology* Polypeptide N-acetylgalactosaminyltransferase Proteoglycans / metabolism Recombinant Proteins / genetics Recombinant Proteins / metabolism Sequence Alignment Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Substrate Specificity Syndecan-3 Tissue Distribution |
| IF | 4.238 |
| Times Cited | 96 |
| WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
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| The most frequently cited source | Wikipedia |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Human and Animal Cells | KG-1-C(RCB02700 |