Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15
- PMID: 15147861
- DOI: 10.1016/j.febslet.2004.03.108
Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15
Abstract
We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity.
Similar articles
-
Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10).J Mol Biol. 2006 Jun 9;359(3):708-27. doi: 10.1016/j.jmb.2006.03.061. Epub 2006 Apr 19. J Mol Biol. 2006. PMID: 16650853
-
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 Apr;17(4):374-87. doi: 10.1093/glycob/cwl082. Epub 2007 Jan 10. Glycobiology. 2007. PMID: 17215257
-
O-glycosylation in Toxoplasma gondii: identification and analysis of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases.Int J Parasitol. 2004 Mar 9;34(3):309-22. doi: 10.1016/j.ijpara.2003.11.016. Int J Parasitol. 2004. PMID: 15003492
-
All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases.Glycobiology. 2003 Jan;13(1):1R-16R. doi: 10.1093/glycob/cwg007. Epub 2002 Nov 1. Glycobiology. 2003. PMID: 12634319 Review.
-
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase- 6 (pp-GalNAc-T6): Role in Cancer and Prospects as a Drug Target.Curr Cancer Drug Targets. 2017;17(1):53-61. doi: 10.2174/1568009616666160922102641. Curr Cancer Drug Targets. 2017. PMID: 27659430 Review.
Cited by
-
Engineering of N. benthamiana L. plants for production of N-acetylgalactosamine-glycosylated proteins--towards development of a plant-based platform for production of protein therapeutics with mucin type O-glycosylation.BMC Biotechnol. 2010 Aug 24;10:62. doi: 10.1186/1472-6750-10-62. BMC Biotechnol. 2010. PMID: 20735851 Free PMC article.
-
Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs.Glycobiology. 2008 Nov;18(11):861-70. doi: 10.1093/glycob/cwn073. Epub 2008 Jul 31. Glycobiology. 2008. PMID: 18669915 Free PMC article.
-
Recent insights into the biological roles of mucin-type O-glycosylation.Glycoconj J. 2009 Apr;26(3):325-34. doi: 10.1007/s10719-008-9162-4. Epub 2008 Aug 10. Glycoconj J. 2009. PMID: 18695988 Free PMC article. Review.
-
Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma.Cell Mol Life Sci. 2013 Mar;70(5):829-39. doi: 10.1007/s00018-012-1082-6. Epub 2012 Aug 3. Cell Mol Life Sci. 2013. PMID: 22864623 Free PMC article. Review.
-
Human Lectins, Their Carbohydrate Affinities and Where to Find Them.Biomolecules. 2021 Jan 29;11(2):188. doi: 10.3390/biom11020188. Biomolecules. 2021. PMID: 33572889 Free PMC article. Review.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
- Actions
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous