The Carbonic Anhydrases

1. Front Matter

   Pages I-XVIII

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2. Exordium: Remarks on the discovery of carbonic anhydrase

   1. Remarks on the discovery of carbonic anhydrase

      • Robert E. Forster

      Pages 1-11

   2. Introduction to the carbonic anhydrases

      • W. Richard Chegwidden, Nicholas D. Carter

      Pages 13-28

   3. Evolution and distribution of the carbonic anhydrase gene families

      • David Hewett-Emmett

      Pages 29-76

3. Carbonic Anhydrase Isoforms and their Expression in Mammals

   1. Front Matter

      Pages 77-77

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   2. An overview of the distribution and function of carbonic anhydrase in mammals

      • Seppo Parkkila

      Pages 79-93

   3. The membrane carbonic anhydrases: from CO2 transport to tumor markers

      • William S. Sly

      Pages 95-104

   4. Carbonic anhydrase (CA)-related proteins (CA-RPs), and transmembrane proteins with CA or CA-RP domains

      • Richard E. Tashian, David Hewett-Emmett, Nick Carter, Nils C. H. Bergenhem

      Pages 105-120

   5. Regulation of the CA1, CA2 and CA3 genes

      • Yvonne Edwards, Felicity Drummond, Jane Sowden

      Pages 121-141

   6. Use of carbonic anhydrase II-deficient mice in uncovering the cellular location of membrane-associated isoforms

      • Yvonne Ridderstråle, Per J. Wistrand, Lena Holm, Nicholas D. Carter

      Pages 143-155

4. Structure and Mechanism

   1. Front Matter

      Pages 157-157

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   2. X-ray crystallographic studies of mammalian carbonic anhydrase isozymes

      • Travis Stams, David W. Christianson

      Pages 159-174

   3. The catalytic mechanism of mammalian carbonic anhydrases

      • Sven Lindskog, David N. Silverman

      Pages 175-195

   4. Activation of carbonic anhydrase isozymes

      • Claudiu T. Supuran, Andrea Scozzafava

      Pages 197-219

   5. Active-site engineering of carbonic anhydrase and its application to biosensors

      • Jennifer A. Hunt, Charles A. Lesburg, David W. Christianson, Richard B. Thompson, Carol A. Fierke

      Pages 221-240

   6. Folding and stability of human carbonic anhydrase II

      • Uno Carlsson, Bengt-Harald Jonsson

      Pages 241-259

5. Physiology

   1. Front Matter

      Pages 261-261

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   2. Membrane transport and provision of substrates for carbonic anhydrase: in vertebrates

      • Robert E. Forster, Susanna J. Dodgson

      Pages 263-280

   3. Respiratory and renal roles of carbonic anhydrase in gas exchange and acid-base regulation

      • Erik R. Swenson

      Pages 281-341

   4. The roles of carbonic anhydrase in metabolism, cell growth and cancer in animals

      • W. Richard Chegwidden, Susanna J. Dodgson, Ian M. Spencer

      Pages 343-363

Carbonic anhydrase (CA) is a seemingly ubiquitous enzyme of profound physiological importance, which plays essential roles in respiration, acid-base homeostasis, bone resorption, calcification, photosynthesis, several biosynthetic pathways and a variety of processes involving ion, gas and fluid transfer. This enzyme, which is present in at least three gene families (a, ß, ?), has found favour as a model for the study of evolution of gene families and for site-directed mutagenesis in structure/function relationships, for protein folding and for transgenic and gene target studies. Since the early use of CA inhibitors as diuretics and in treating congestive heart failure, the enzyme has been target of considerable clinical attention. Much of this is now focused on endeavours to produce a new generation of such drugs for the effective treatment of glaucoma and other potential applications. Recent data, suggesting links between CA and various disease processes, including cancer, have stimulated further...

• Resorption
• biochemistry
• bone
• carbon
• enzyme
• enzymes
• evolution
• membrane transport
• metabolism
• photosynthesis
• physiology
• protein
• protein folding
• respiration
• synthesis

• Lake Erie College of Osteopathic Medicine, Erie, USA

  W. Richard Chegwidden

• Medical Genetics Unit, St George’s Hospital Medical School, London, UK

  Nicholas D. Carter

• MRC Human Biochemical Genetics Unit, Wolfson House, University College London, London, UK

  Yvonne H. Edwards

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