Deconvoluting the Functions of Polypeptide N-α-Acetylgalactosaminyltransferase Family Members by Glycopeptide Substrate Profiling
| Autor: | Thomas A. Gerken, Matthew R. Pratt, Howard C. Hang, Lawrence A. Tabak, Jason M. Rarick, Carolyn R. Bertozzi, Kelly G. Ten Hagen |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Glycan biosynthesis
Gene isoform Scaffold protein Glycan Molecular Sequence Data Clinical Biochemistry Enzyme-Linked Immunosorbent Assay Biochemistry Substrate Specificity 03 medical and health sciences Drug Discovery Animals Amino Acid Sequence Molecular Biology 030304 developmental biology chemistry.chemical_classification Pharmacology 0303 health sciences biology 030302 biochemistry & molecular biology Mucin Glycopeptides General Medicine Glycopeptide Rats carbohydrates (lipids) chemistry biology.protein N-Acetylgalactosaminyltransferases Molecular Medicine Glycoprotein |
| Zdroj: | Chemistry & Biology. 11(7):1009-1016 |
| ISSN: | 1074-5521 |
| DOI: | 10.1016/j.chembiol.2004.05.009 |
| Popis: | The polypeptide N-α-acetylgalactosaminyltransferases (ppGalNAcTs) play a key role in mucin-type O-linked glycan biosynthesis by installing the intial GalNAc residue on the protein scaffold. The preferred substrates and functions of the >20 isoforms in mammals are not well understood. However, current data suggest that glycosylated mucin domains are created by the successive, often hierarchical, action of several specific ppGalNAcTs. Herein we analyzed the glycopeptide substrate preferences of several ppGalNAcT family members using a library screening approach. A 56-member glycopeptide library designed to reflect a diversity of glycan clustering was assayed for substrate activity with ppGalNAcT isoforms using an azido-ELISA. The data suggest that the ppGalNAcTs can be classified into at least four types, which working together, are able to produce densely glycosylated mucin glycoproteins. |
| Databáze: | OpenAIRE |
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