Evidence map›Paper›PMID 24065526›Full record

ArticleMolecular biology reports2013

Molecular characterization and expression analysis of three hypoxia-inducible factor alpha subunits, HIF-1α, -2α and -3α in hypoxia-tolerant Indian catfish, Clarias batrachus [Linnaeus, 1758].

Vindhya Mohindra, Ratnesh Kumar Tripathi, Rajeev Kumar Singh, Kuldeep K Lal

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Article in Molecular biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 49 citations in OpenAlex.

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  15. Sequence and functional characterization of hypoxia-inducible factors, HIF1α, HIF2αa, and HIF3α, from the estuarine fish,American journal of physiology. Regulatory, integrative and comparative physiology · 2017
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Vindhya MohindraNational Bureau of Fish Genetic Resources (ICAR), Canal Ring Road, P.O. Dilkusha, Lucknow, 226002, UP, India, vindhyamohindra@gmail.com.
Ratnesh Kumar Tripathi
Rajeev Kumar Singh
Kuldeep K Lal
Indian Council of Agricultural Research · INNational Bureau of Fish Genetic Resources · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study aimed at characterization of three HIF-α subunits, HIF-1α -2α and -3α from hypoxia-tolerant Clarias batrachus, as well as to elucidate their expression pattern under short and long-term hypoxic conditions and identification of biomarker candidate. The complete cDNAs of HIF-1α, -2α and -3α were 2,833, 4,270 and 3,256 bp in length, encoding 774, 818 and 628 amino acid residues, respectively. In C. batrachus, HIF-α subunits were structurally similar in DNA binding, dimerization, degradation and transcriptional activation domains, but differed in their oxygen-dependent degradation domains. Presence of c-Jun N-terminal kinase binding domain in HIF-α subunits was reported here for the first time in fish. In adult C. batrachus, three HIF-α mRNAs were detected in different tissues under normoxic conditions, however HIF-1α was highly expressed in all the tissues studied, in comparison to HIF-2α and -3α. Short-term hypoxia exposure caused significant increase in three HIF-α transcripts in brain, liver and head kidney, while after long-term hypoxia exposure, significant up-regulation of HIF-1α in spleen and -2α in muscle was observed and HIF-3α significantly down-regulated in head kidney. These observations suggest that the differential expression of HIF-α subunits in C. batrachus was hypoxic time period dependent and may play specialized roles in adaptive response to hypoxia. HIF-2α, with its highly elevated expression in muscle tissues, can be a robust biomarker candidate for exposure to hypoxic environment.

Indexed as

Gene Expression RegulationAdaptation, PhysiologicalAmino Acid SequenceAnimalsBasic Helix-Loop-Helix ProteinsCatfishesDNA, ComplementaryGene Expression ProfilingHypoxiaMolecular Sequence DataOpen Reading FramesProtein IsoformsProtein SubunitsRNA, MessengerSequence AlignmentBasic Helix-Loop-Helix ProteinsDNA, ComplementaryProtein IsoformsProtein SubunitsRNA, Messenger

Identifiers

PMID24065526
OpenAlexW2056783482

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.