Sequence and functional characterization of hypoxia-inducible factors, HIF1α, HIF2αa, and HIF3α, from the estuarine fish, Fundulus heteroclitus .

Autor:	Townley IK; Department of Biological Sciences, University of New Orleans, New Orleans, Louisiana.; College of Pharmacy, Xavier University of New Orleans, New Orleans, Louisiana; and., Karchner SI; Biology Department, Woods Hole Oceanographic Institution, Woods Hole, Massachusetts., Skripnikova E; Department of Biological Sciences, University of New Orleans, New Orleans, Louisiana.; College of Pharmacy, Xavier University of New Orleans, New Orleans, Louisiana; and., Wiese TE; College of Pharmacy, Xavier University of New Orleans, New Orleans, Louisiana; and., Hahn ME; Biology Department, Woods Hole Oceanographic Institution, Woods Hole, Massachusetts., Rees BB; Department of Biological Sciences, University of New Orleans, New Orleans, Louisiana brees@uno.edu.
Jazyk:	angličtina
Zdroj:	American journal of physiology. Regulatory, integrative and comparative physiology [Am J Physiol Regul Integr Comp Physiol] 2017 Mar 01; Vol. 312 (3), pp. R412-R425. Date of Electronic Publication: 2016 Dec 30.
DOI:	10.1152/ajpregu.00402.2016
Abstrakt:	The hypoxia-inducible factor (HIF) family of transcription factors plays central roles in the development, physiology, pathology, and environmental adaptation of animals. Because many aquatic habitats are characterized by episodes of low dissolved oxygen, fish represent ideal models to study the roles of HIF in the response to aquatic hypoxia. The estuarine fish Fundulus heteroclitus is found in habitats prone to hypoxia. It responds to low oxygen via behavioral, physiological, and molecular changes, and one member of the HIF family, HIF2α, has been previously described. Herein, cDNA sequencing, phylogenetic analyses, and genomic approaches were used to determine other members of the HIFα family from F. heteroclitus and their relationships to HIFα subunits from other vertebrates. In vitro and cellular approaches demonstrated that full-length forms of HIF1α, HIF2α, and HIF3α independently formed complexes with the β-subunit, aryl hydrocarbon receptor nuclear translocator, to bind to hypoxia response elements and activate reporter gene expression. Quantitative PCR showed that HIFα mRNA abundance varied among organs of normoxic fish in an isoform-specific fashion. Analysis of the F. heteroclitus genome revealed a locus encoding a second HIF2α-HIF2αb-a predicted protein lacking oxygen sensing and transactivation domains. Finally, sequence analyses demonstrated polymorphism in the coding sequence of each F. heteroclitus HIFα subunit, suggesting that genetic variation in these transcription factors may play a role in the variation in hypoxia responses among individuals or populations. (Copyright © 2017 the American Physiological Society.)
Databáze:	MEDLINE
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