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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Esterase activity of carbonic anhydrases serves as surrogate for selecting antibodies blocking hydratase activity.
J. Enzyme Inhib. Med. Chem. 30, 955-960 (2015)
Carbonic anhydrase 9 (CA9) and carbonic anhydrase 12 (CA12) were proposed as potential targets for cancer therapy more than 20 years ago. However, to date, there are only very few antibodies that have been described to specifically target CA9 and CA12 and also block the enzymatic activity of their targets. One of the early stage bottlenecks in identifying CA9- and CA12-inhibiting antibodies has been the lack of a high-throughput screening system that would allow for rapid assessment of inhibition of the targeted carbon dioxide hydratase activity of carbonic anhydrases. In this study, we show that measuring the esterase activity of carbonic anhydrase offers a robust and inexpensive screening method for identifying antibody candidates that block both hydratase and esterase activities of carbonic anhydrase's. To our knowledge, this is the first implementation of a facile surrogate-screening assay to identify potential therapeutic antibodies that block the clinically relevant hydratase activity of carbonic anhydrases.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cancer Therapy ; Carbonic Anhydrase 9 & 12 ; Enzyme Inhibition ; High-throughput Screening ; Renal Cell Cancer; Renal-cell Carcinoma; Monoclonal-antibody; Intracellular Ph; Hydrophobic Pocket; Enzymatic-activity; Ix; Protein; Xii; Inhibitors; Hypoxia
ISSN (print) / ISBN
1475-6366
e-ISSN
1475-6374
Quellenangaben
Volume: 30,
Issue: 6,
Pages: 955-960
Publisher
Informa Healthcare
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Research Unit Gene Vector (AGV)