Source:http://linkedlifedata.com/resource/pubmed/id/12643899
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2003-3-19
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pubmed:abstractText |
The inhibition of the tumor-associated transmembrane carbonic anhydrase IX (CA IX) isozyme has been investigated with a series of aromatic and heterocyclic sulfonamides, including the six clinically used derivatives acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide and brinzolamide. Inhibition data for the physiologically relevant isozymes I and II (cytosolic forms) and IV (membrane-bound) were also provided for comparison. A very interesting and unusual inhibition profile against CA IX with these sulfonamides has been observed. Several nanomolar (K(I)-s in the range of 14-50 nM) CA IX inhibitors have been detected, both among the aromatic (such as orthanilamide, homosulfonilamide, 4-carboxy-benzenesulfonamide, 1-naphthalenesulfonamide and 1,3-benzenedisulfonamide derivatives) as well as the heterocylic (such as 1,3,4-thiadizole-2-sulfonamide, etc.) sulfonamides examined. Because CA IX is a highly active isozyme predominantly expressed in tumor tissues with poor prognosis of disease progression, this finding is very promising for the potential design of CA IX-specific inhibitors with applications as anti-tumor agents.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CA9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrases,
http://linkedlifedata.com/resource/pubmed/chemical/Heterocyclic Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrocarbons, Aromatic,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfonamides
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1005-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12643899-Animals,
pubmed-meshheading:12643899-Antigens, Neoplasm,
pubmed-meshheading:12643899-Carbonic Anhydrase Inhibitors,
pubmed-meshheading:12643899-Carbonic Anhydrases,
pubmed-meshheading:12643899-Cattle,
pubmed-meshheading:12643899-Heterocyclic Compounds,
pubmed-meshheading:12643899-Humans,
pubmed-meshheading:12643899-Hydrocarbons, Aromatic,
pubmed-meshheading:12643899-Isoenzymes,
pubmed-meshheading:12643899-Kinetics,
pubmed-meshheading:12643899-Neoplasm Proteins,
pubmed-meshheading:12643899-Neoplasms,
pubmed-meshheading:12643899-Structure-Activity Relationship,
pubmed-meshheading:12643899-Sulfonamides
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pubmed:year |
2003
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pubmed:articleTitle |
Carbonic anhydrase inhibitors: inhibition of the tumor-associated isozyme IX with aromatic and heterocyclic sulfonamides.
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pubmed:affiliation |
Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino (Firenze), Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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