Literature DB >> 11159923

Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development.

P D Kingsley1, K G Hagen, K M Maltby, J Zara, L A Tabak.   

Abstract

Cell migration and adhesion during embryonic development are complex processes which likely involve interactions among cell-surface carbohydrates. While considerable work has implicated proteoglycans in a wide range of developmental events, only limited attention has been directed towards understanding the 7role(s) played by the related class of mucin-type O-glycans. The initial step of mammalian mucin-type O-glycosylation is catalyzed by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases). The spatial expression patterns of the messenger RNAs of seven ppGaNTase family members were investigated from gastrulation through organogenesis stages of mouse development. The seven glycosyltransferases were expressed in unique patterns during embryogenesis. ppGaNTase-T1, -T2, -T4, and -T9 were expressed more ubiquitously than ppGaNTase-T3, -T5, and -T7. Organ systems with discrete accumulation patterns of ppGaNTase family members include the gastrointestinal tract (intestine, liver, stomach, submandibular gland), nervous system (brain, eye), lung, bone, yolk sac, and developing craniofacial region. The pattern in the craniofacial region included differential expression by family members in developing mandible, teeth, tongue and discrete regions of the brain including the pons and migratory, differentiating neurons. Additionally, ppGaNTase-T5 accumulates in a subset of mesenchymal cells at the ventral-most portions of the E12.5 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.

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Year:  2000        PMID: 11159923     DOI: 10.1093/glycob/10.12.1317

Source DB:  PubMed          Journal:  Glycobiology        ISSN: 0959-6658            Impact factor:   4.313


  22 in total

1.  Dissecting the biological role of mucin-type O-glycosylation using RNA interference in Drosophila cell culture.

Authors:  Liping Zhang; Kelly G Ten Hagen
Journal:  J Biol Chem       Date:  2010-08-31       Impact factor: 5.157

2.  An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand.

Authors:  Liping Zhang; Duy T Tran; Kelly G Ten Hagen
Journal:  J Biol Chem       Date:  2010-04-06       Impact factor: 5.157

Review 3.  Mucin overproduction in chronic inflammatory lung disease.

Authors:  Hans-Peter Hauber; Susan C Foley; Qutayba Hamid
Journal:  Can Respir J       Date:  2006-09       Impact factor: 2.409

4.  Initiation of protein O glycosylation by the polypeptide GalNAcT-1 in vascular biology and humoral immunity.

Authors:  Mari Tenno; Kazuaki Ohtsubo; Fred K Hagen; David Ditto; Alexander Zarbock; Patrick Schaerli; Ulrich H von Andrian; Klaus Ley; Dzung Le; Lawrence A Tabak; Jamey D Marth
Journal:  Mol Cell Biol       Date:  2007-10-08       Impact factor: 4.272

5.  Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1.

Authors:  Hazuki E Miwa; Thomas A Gerken; Oliver Jamison; Lawrence A Tabak
Journal:  J Biol Chem       Date:  2009-10-30       Impact factor: 5.157

Review 6.  Mucin-type O-glycosylation during development.

Authors:  Duy T Tran; Kelly G Ten Hagen
Journal:  J Biol Chem       Date:  2013-01-17       Impact factor: 5.157

7.  Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides.

Authors:  D Tetaert; K G Ten Hagen; C Richet; A Boersma; J Gagnon; P Degand
Journal:  Biochem J       Date:  2001-07-01       Impact factor: 3.857

Review 8.  O-Linked glycosylation in Drosophila melanogaster.

Authors:  Liping Zhang; Kelly G Ten Hagen
Journal:  Curr Opin Struct Biol       Date:  2019-03-07       Impact factor: 6.809

9.  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.

Authors:  Sasha M Daskalova; Josiah E Radder; Zbigniew A Cichacz; Sam H Olsen; George Tsaprailis; Hugh Mason; Linda C Lopez
Journal:  BMC Biotechnol       Date:  2010-08-24       Impact factor: 2.563

Review 10.  Recent insights into the biological roles of mucin-type O-glycosylation.

Authors:  E Tian; Kelly G Ten Hagen
Journal:  Glycoconj J       Date:  2008-08-10       Impact factor: 2.916

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