Evidence map›Paper›PMID 7479872›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Chimeric Na+/H+ exchangers: an epithelial membrane-bound N-terminal domain requires an epithelial cytoplasmic C-terminal domain for regulation by protein kinases.

C H Yun, C M Tse, M Donowitz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

9 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms of the regulation of the intestinal Na+/H+ exchanger NHE3.Journal of biomedicine & biotechnology · 2010
    Review
  4. Article
  5. Luminal Na(+)/H (+) exchange in the proximal tubule.Pflugers Archiv : European journal of physiology · 2009
    Review
  6. Article
  7. PKC stimulated by glucagon decreases UT-A1 urea transporter expression in rat IMCD.Pflugers Archiv : European journal of physiology · 2008
    Article
  8. Article
  9. Concerted roles of SGK1 and the Na+/H+ exchanger regulatory factor 2 (NHERF2) in regulation of NHE3.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2003
    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

3 authors at 2 institutions in 1 country.

C H YunDepartment of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
C M Tse
M Donowitz
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

DIARRHEAL DISEASES: A PHYSIOLOGIC APPROACH TO TREATMENTR01DK026523 · NIDDK · TUFTS MEDICAL CENTER · PI DONOWITZ, MARK · 1986 to 2016
$7.8M
STRUCTURE AND FUNCTION STUDIES OF CLONED SODIUM AND HYDROGEN EXCHANGERSP01DK044484 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MONTROSE, MARSHALL H · 1992 to 2002
$2.6M
CLONING &REGULATION OF INTESTINAL NA+/H+ EXCHANGERSR29DK043778 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI TSE, CHUNG-MING · 1991 to 1995
–
NIDDK NIH HHS P01DK44484NIDDK NIH HHS R01DK26523NIDDK NIH HHS R29DK43778
6 · The paper itself

Abstract

All cloned members of the mammalian Na+/H+ exchanger gene family encode proteins that consist of two functionally distinct domains: a membrane-bound N terminus and a cytoplasmic C terminus, which are required for ion transport and regulation of transport, respectively. Despite their similarity in structure, three members of this family, designated NHE1, NHE2, and NHE3, exhibit different kinetic mechanisms in response to growth factors and protein kinases. For instance, growth factors stimulate NHE1 by a change in the affinity constant for intracellular H+, K'(Hi+), and regulate NHE2 and NHE3 by a change in Vmax. We have constructed chimeric Na+/H+ exchangers by exchanging the N and C termini among three cloned rabbit Na+/H+ exchangers (NHE1 to NHE3) to determine which domain is responsible for the above Vmax-vs.-K'(H(i)+) effect of the Na+/H+ isoforms. All of the chimeras had functional exchange activity and basal kinetic properties similar to those of wild-type exchangers. Studies with serum showed that the N terminus is responsible for the Vmax-vs.-K'(H(i)+) stimulation of the Na+/H+ exchanger isoforms. Moreover, phorbol 12-myristate 13-acetate and fibroblast growth factor altered Na+/H+ exchange only in chimeras that had an epithelial N-terminal domain matched with an epithelial C-terminal domain. Therefore, the protein kinase-induced regulation of Na+/H+ exchangers is mediated through a specific interaction between the N- and C-termini, whcih is restricted so that epithelial N- and epithelial N-and C-terminal portions of the exchangers are required for regulation.

Indexed as

Base SequenceBiological TransportEpithelial CellsMembrane ProteinsModels, MolecularMolecular Sequence DataProtein KinasesProtonsRecombinant Fusion ProteinsSodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersStructure-Activity Relationshipgrowth factor-activatable Na-H exchanger NHE-1Membrane ProteinsProtein KinasesProtonsRecombinant Fusion ProteinsSodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen Exchangers

Identifiers

PMID7479872
PMCPMC40684
OpenAlexW2016121757

What OpenQuestion holds

Textmetadata
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.