Anion Transport Protein of the Red Blood Cell Membrane [antikvár]

PREFACE The papers in this volume represent contributions to the INTERNATIONAL MEETING ON ANION TRANSPORT PROTEIN OF THE RED BLOOD CELL MEMBRANE, held at The University of Fukuoka on May 1-3, 1989. The meeting was made possible by the generous sponsorship of Fukuoka University Foundation, Alumni of the School of Medicine and Mr. Akira Moriyama. The meeting was organized in response to numerous recent advances in the understanding of anion exchange proteins in both erythroid and non-erythroid cells. The first evidence for the rapid exchange of anions across the red blood cell membrane was published over 100 years ago, and the role of chloride-bicarbonate exchange in carbón dioxide transport was described by Roughton over 50 years ago. However, it was only 15 years ago that chemical labeling studies in three laboratories led to the identification of the protein responsible for catalyzing the anion exchange. The protein, known as band 3 or capnophorin, is the major integral membrane protein of red cells. Because of the abundance of the protein and because the red cell is well suited for detailed studies of transport, the red cell anion exchange protein is one of the best characterized of transport proteins. Although much still remains to be learned, there has been steady progress in the understanding of the topography of the protein, its interaction with other proteins, the kinetics and asymmetry of transport, and the roles of particular amino acid residues in the catalysis of transport. In the past few years there have been important developments in the application of recombinant DNA technology to the study of the anion transporter. The cDNA coding band 3 from mouse, chicken, and human has been cloned and sequenced, as has the genomic DNA for mouse band 3. There have also been rapid advances in the expression of the band 3 gene for site-directed mutagenesis studies. The availability of cDNA probes and antibodies against band 3 has made possible the identification of homologous proteins in non-erythroid tissues. The roles of these proteins in cell physiology are currently being studied intensely. The meeting was organized with the goal of brining together individuáis who represent a broad spectrum of approaches to a narrowly defined area: anion exchange proteins. The resuit was a lively exchange of data and ideas. The organizers are grateful to ail the participants and to Professor Akira Omachi (University of Illinois at Chicago) and a number of people associated with Fukuoka University for their help in many aspects of the symposium's organization. Naotaka Hamasaki Michael L. Jennings June 22, 1989