Strategies for drug discovery by targeting sulfation pathways

A new class of kinase-related drug targets with the promise of novel therapies for inflammation, cancer, and infectious diseases. Posttranslational modifications of proteins such as phosphorylation have been recognized as pivotal modulators of biological activity in healthy and diseased tissues. Sul...

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Bibliographic Details
Published in:Drug Discovery Today 2004-11, Vol.9 (22), p.967-975
Main Authors: Hemmerich, Stefan, Verdugo, Dawn, Rath, Virginia L.
Format: Article
Language:English
Subjects:
Angiogenesis
Animals
Biological and medical sciences
Cancer
Cell Adhesion
Drug Design
General pharmacology
Golgi Apparatus - metabolism
Heparin
Humans
Inflammation
Medical sciences
Pharmaceutical technology. Pharmaceutical industry
Pharmacology. Drug treatments
Protein Processing, Post-Translational
Proteome
Sulfation
Sulfotransferases
Sulfotransferases - antagonists & inhibitors
Sulfotransferases - chemistry
Sulfotransferases - metabolism
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Summary:A new class of kinase-related drug targets with the promise of novel therapies for inflammation, cancer, and infectious diseases. Posttranslational modifications of proteins such as phosphorylation have been recognized as pivotal modulators of biological activity in healthy and diseased tissues. Sulfation is a key posttranslational modification the role of which in physiology and pathology is only now becoming appreciated. Whereas phosphorylation is central to intracellular signal transduction, sulfation modulates cell-cell and cell-matrix communication. Sulfation involves a class of enzymes known as sulfotransferases, which transfer sulfate from the ATP-like sulfate donor 3′phosphoadenosine-5′phosphosulate to glycoproteins, glycolipids or metabolites. This review focuses on Golgi-localized sulfotransferases, their molecular biology and biochemistry, and strategies towards discovery of sulfotransferase inhibitors that could have potential as therapeutics in inflammation, cancer and infectious diseases.
ISSN:1359-6446
1878-5832
DOI:10.1016/S1359-6446(04)03261-1