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A Systematic Study of Site-specific GalNAc-type O-Glycosylation Modulating Proprotein Convertase Processing

Authors
Publisher
American Society for Biochemistry and Molecular Biology, Inc.
Publication Date
Keywords
  • Site-Specific Galnac-Type O-Glycosylation Is Emerging As An Important Co-Regulator Of Proprotein Con
  • Pc Processing Is Crucial In Regulating Many Fundamental Biological Pathways And O-Glycans In Or Imme
  • Thus
  • We Previously Demonstrated That Deficiency In Site-Specific O-Glycosylation In A Pc Site Of The Fibr
  • Fgf23
  • Resulted In Marked Reduction In Secretion Of Active Unprocessed Fgf23
  • Which Cause Familial Tumoral Calcinosis And Hyperostosis Hyperphosphatemia
  • Galnac-Type O-Glycosylation Is Found On Serine And Threonine Amino Acids And Up To 20 Distinct Polyp
  • There Is No Reliable Prediction Model For O-Glycosylation Especially Of Isolated Sites
  • But Serine And To A Lesser Extent Threonine Residues Are Frequently Found Adjacent To Pc Processing
  • In The Present Study We Used In Vitro Enzyme Assays And Ex Vivo Cell Models To Systematically Addres
  • The Results Demonstrate That O-Glycans Within At Least ±3 Residues Of The Rxxr Furin Cleavage Site
Disciplines
  • Biology

Abstract

A Systematic Study of Site-specific GalNAc-type O-Glycosylation Modulating Proprotein Convertase Processing - DTU Orbit (18/04/14) A Systematic Study of Site-specific GalNAc-type O-Glycosylation Modulating Proprotein Convertase Processing - DTU Orbit (18/04/14) Schjoldager KT-BG, Vester-Christensen MB, Goth CK, Petersen TN, Brunak S, Bennett EP, Levery SB, Clausen H. 2011. A Systematic Study of Site-specific GalNAc-type O-Glycosylation Modulating Proprotein Convertase Processing. Journal of Biological Chemistry. 286(46):40122-40132. Available from: 10.1074/jbc.M111.287912

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