title: Band 3 protein function in teleost fish erythrocytes: effect of oxygenation-deoxygenation.
abstract: During vertebrate evolution, structural changes in red blood cells (RBC) and hemoglobin (Hb), have probably resulted in the importance of blood carbon dioxide transport. The chloride/bicarbonate exchange across the RBC membrane, which is an integral part of the blood CO(2) transport process in vertebrates, has been examined on two different species of teleost fish, Euthynnus alletteratus and Thunnus thynnus, at several oxygenation states of erythrocyte HOS (high-oxygenation state, about 90 % of saturation) and LOS (low-oxygenation state, about 15 % of saturation). The results were compared with those observed in human RBC under the same experimental conditions and with the chicken (Gallus gallus) erythrocytes, which have particular modifications at the N-terminus of the band 3 protein (B3). In fish the kinetic measurements have shown a different anion transport in several oxygenation states of erythrocytes, indicating that also at lower levels of vertebrate evolution there exists a modulation of the anionic flow affected by oxygen. The functional correlation of anion transport to changes of parts of the hemoglobin sequence responsible for alterations in the interactions with the cytoplasmic domain of band 3 protein (cdb3) allowed us to suggest a hypothesis about fish physiology. The highest values of kinetic measurements observed in fish have been attributed to the metabolic need of the RBC in response to the removal of CO(2) that in teleosts is also of endogenous origin.
authors.affiliation: Department of Organic and Biological Chemistry, University of Messina, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Russo
authors.forename: E
authors.initials: E
authors.lastname: Tellone
authors.forename: S
authors.initials: S
authors.lastname: Ficarra
authors.forename: B
authors.initials: B
authors.lastname: Giardina
authors.forename: E
authors.initials: E
authors.lastname: Bellocco
authors.forename: G
authors.initials: G
authors.lastname: Lagana'
authors.forename: U
authors.initials: U
authors.lastname: Leuzzi
authors.forename: A
authors.initials: A
authors.lastname: Kotyk
authors.forename: A
authors.initials: A
authors.lastname: Galtieri
mesh_terms: D000328:Adult; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000502:physiology*; D002245:Carbon Dioxide / Q000097:blood*; D002645:Chickens; D004912:Erythrocytes / Q000378:metabolism*; D029941:Fish Proteins / Q000502:physiology*; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D017136:Ion Transport / Q000502:physiology*; D008875:Middle Aged; D010100:Oxygen / Q000097:blood; D013045:Species Specificity; D014413:Tuna / Q000378:metabolism*
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D029941:Fish Proteins; D006454:Hemoglobins; D002245:Carbon Dioxide; D010100:Oxygen