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Originally published In Press as doi:10.1074/jbc.M001209200 on March 27, 2000

J. Biol. Chem., Vol. 275, Issue 23, 17297-17305, June 9, 2000
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Isohemoglobin Differentiation in the Bimodal-breathing Amazon Catfish Hoplosternum littorale*

Roy E. WeberDagger §, Angela FagoDagger , Adalberto L. Val||, Anny BangDagger , Marie-Louise Van Hauwaert**, Sylvia Dewilde**, Franck Zal**Dagger Dagger , and Luc Moens**

From the Dagger  Department of Zoophysiology, University of Aarhus, DK 8000 Aarhus C, Denmark, the || Instituto Nacional de Pesquisas da Amazonia, Laboratory of Ecophysiology and Molecular Evolution, Alameda Cosme Ferreira 1756, 69083 Manaus, AM, Brazil, the ** Biochemistry Department, University of Antwerp, Universiteitsplein 1, B-2610 Antwerpen, Belgium, and the Dagger Dagger  Equipe Ecophysiologie, Station Biologique de Roscoff, CNRS-UPMC-INSU, Place G. Teissier, B.P. 74 29682 Roscoff Cedex, France

The bimodal gill(water)/gut(air)-breathing Amazonian catfish Hoplosternum littorale that frequents hypoxic habitats uses "mammalian" 2,3-diphosphoglycerate (DPG) in addition to "piscine" ATP and GTP as erythrocytic O2 affinity modulators. Its electrophoretically distinct anodic and cathodic hemoglobins (HbAn and HbCa) were isolated for functional and molecular characterization. In contrast to HbAn, phosphate-free HbCa exhibits a pronounced reverse Bohr effect (increased O2 affinity with decreasing pH) that is obliterated by ATP, and opposite pH dependences of KT (O2 association constant of low affinity, tense state) and the overall heat of oxygenation. Dose-response curves indicate small chloride effects and pronounced and differentiated phosphate effects, DPG < ATP < GTP < IHP. HbCa-O2 equilibria analyzed in terms of the Monod-Wyman-Changeux model show that small T state bond energy differences underlie the differentiated phosphate effects. Synthetic peptides, corresponding to N-terminal fragment of the cytoplasmic domain of trout band 3 protein, undergo oxygenation-linked binding to HbCa, suggesting a metabolic regulatory role for this hemoglobin. The amino acid sequences for the alpha  and beta  chains of HbCa obtained by Edman degradation and cDNA sequencing show unusual substitutions at the phosphate-binding site that are discussed in terms of its reverse Bohr effect and anion sensitivities.

* This work was supported by the Danish Natural Science Research Council, the Danish Centre for Respiratory Adaptation, and the Fund for Scientific Research Projects G.2023.94 and G.0314.00, Flanders, Belgium.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The sequences reported in this paper have been submitted to the Swiss Protein Database under Swiss-Prot accession numbers P82315 and P82316.

§ To whom correspondence should be addressed. Tel.: 45 8942 2599; Fax: 45 8619 4186; E-mail: roy.weber@biology.au.dk.

Postdoctoral fellows of the Danish Centre for Respiratory Adaptation and the Belgian Fund for Scientific Research, respectively.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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