Evidence map›Paper›PMID 21315725›Full record

ArticleJournal of insect physiology2011

Function and immuno-localization of aquaporins in the Antarctic midge Belgica antarctica.

Shu-Xia Yi, Joshua B Benoit, Michael A Elnitsky, Nancy Kaufmann, Jeffrey L Brodsky, Mark L Zeidel, David L Denlinger, Richard E Lee

Open access · greenAbstract read
In one paragraph

Article in Journal of insect physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
5.0field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  9. Article
  10. Emerging roles of aquaporins in relation to the physiology of blood-feeding arthropods.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2014
    Review
  11. Article
  12. Article
  13. Gene expression changes governing extreme dehydration tolerance in an Antarctic insect.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Water homeostasis: evolutionary medicine.Transactions of the American Clinical and Climatological Association · 2012
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 6 institutions in 1 country.

Shu-Xia YiMiami University, Oxford, OH 45056, USA.
Joshua B Benoit
Michael A Elnitsky
Nancy Kaufmann
Jeffrey L Brodsky
Mark L Zeidel
David L Denlinger
Richard E Lee
Miami University · USUniversity of Pittsburgh · USBeth Israel Deaconess Medical Center · USMercyhurst University · USThe Ohio State University · USYale University · US

Funding

Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2008 to 2022
$13.4M
NIDDK NIH HHS DK79307NIDDK NIH HHS P30 DK079307
6 · The paper itself

Abstract

Aquaporin (AQP) water channel proteins play key roles in water movement across cell membranes. Extending previous reports of cryoprotective functions in insects, this study examines roles of AQPs in response to dehydration, rehydration, and freezing, and their distribution in specific tissues of the Antarctic midge, Belgica antarctica (Diptera, Chironomidae). When AQPs were blocked using mercuric chloride, tissue dehydration tolerance increased in response to hypertonic challenge, and susceptibility to overhydration decreased in a hypotonic solution. Blocking AQPs decreased the ability of tissues from the midgut and Malpighian tubules to tolerate freezing, but only minimal changes were noted in cellular viability of the fat body. Immuno-localization revealed that a DRIP-like protein (a Drosophila aquaporin), AQP2- and AQP3 (aquaglyceroporin)-like proteins were present in most larval tissues. DRIP- and AQP2-like proteins were also present in the gut of adult midges, but AQP4-like protein was not detectable in any tissues we examined. Western blotting indicated that larval AQP2-like protein levels were increased in response to dehydration, rehydration and freezing, whereas, in adults DRIP-, AQP2-, and AQP3-like proteins were elevated by dehydration. These results imply a vital role for aquaporin/aquaglyceroporins in water relations and freezing tolerance in B. antarctica.

Indexed as

DehydrationFreezingAcclimatizationAnimalsAquaglyceroporinsAquaporinsChironomidaeImmunoblottingInsect ProteinsLarvaMercuric ChlorideWaterAquaglyceroporinsAquaporinsInsect ProteinsMercuric ChlorideWater

Identifiers

PMID21315725
PMCPMC8875278
OpenAlexW2170139297

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.