Evidence map›Paper›PMID 23085358›Full record

ArticleInsect biochemistry and molecular biology2013

Cloning and functional characterization of inward-rectifying potassium (Kir) channels from Malpighian tubules of the mosquito Aedes aegypti.

Peter M Piermarini, Matthew F Rouhier, Matthew Schepel, Christin Kosse, Klaus W Beyenbach

Open access · greenAbstract read
In one paragraph

Article in Insect biochemistry and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
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  15. Malpighian Tubules as Novel Targets for Mosquito Control.International journal of environmental research and public health · 2017
    Review
  16. Article
  17. Two inwardly rectifying potassium channels, Irk1 and Irk2, play redundant roles in Drosophila renal tubule function.American journal of physiology. Regulatory, integrative and comparative physiology · 2015
    Article
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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

5 authors at 2 institutions in 1 country.

Peter M PiermariniDepartment of Entomology, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Avenue, 224 Thorne Hall, Wooster, OH 44691, USA. piermarini.1@osu.edu
Matthew F Rouhier
Matthew Schepel
Christin Kosse
Klaus W Beyenbach
Cornell University · USThe Ohio State University · US

Funding

An epithelial model for V-type H+-ATPase-driven acid-base transportK01DK080194 · NIDDK · OHIO STATE UNIVERSITY · PI PIERMARINI, PETER M · 2008 to 2010
$375k
NIDDK NIH HHS K01 DK080194NIDDK NIH HHS K01 DK080194-01
6 · The paper itself

Abstract

Inward-rectifying K(+) (Kir) channels play critical physiological roles in a variety of vertebrate cells/tissues, including the regulation of membrane potential in nerve and muscle, and the transepithelial transport of ions in osmoregulatory epithelia, such as kidneys and gills. It remains to be determined whether Kir channels play similar physiological roles in insects. In the present study, we sought to 1) clone the cDNAs of Kir channel subunits expressed in the renal (Malpighian) tubules of the mosquito Aedes aegypti, and 2) characterize the electrophysiological properties of the cloned Kir subunits when expressed heterologously in oocytes of Xenopus laevis. Here, we reveal that three Kir subunits are expressed abundantly in Aedes Malpighian tubules (AeKir1, AeKir2B, and AeKir3); each of their full-length cDNAs was cloned. Heterologous expression of the AeKir1 or the AeKir2B subunits in Xenopus oocytes elicits inward-rectifying K(+) currents that are blocked by barium. Relative to the AeKir2B-expressing oocytes, the AeKir1-expressing oocytes 1) produce larger macroscopic currents, and 2) exhibit a modulation of their conductive properties by extracellular Na(+). Attempts to functionally characterize the AeKir3 subunit in Xenopus oocytes were unsuccessful. Lastly, we show that in isolated Aedes Malpighian tubules, the cation permeability sequence of the basolateral membrane of principal cells (Tl(+) > K(+) > Rb(+) > NH(4)(+)) is consistent with the presence of functional Kir channels. We conclude that in Aedes Malpighian tubules, Kir channels contribute to the majority of the barium-sensitive transepithelial transport of K(+).

Indexed as

AedesAmino Acid SequenceAnimalsBariumCloning, MolecularDNA, ComplementaryFemaleGenes, InsectInsect ProteinsIsotonic SolutionsMalpighian TubulesMembrane PotentialsMolecular Sequence DataPotassiumPotassium Channels, Inwardly RectifyingRinger's SolutionBariumDNA, ComplementaryInsect ProteinsIsotonic SolutionsPotassiumPotassium Channels, Inwardly RectifyingRinger's SolutionSodium

Identifiers

PMID23085358
PMCPMC3595064
OpenAlexW2031997105

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Registered trials

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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.