Evidence map›Paper›PMID 19734321›Full record

ArticleMolecular pharmacology2009

N6-substituted cAMP analogs inhibit bTREK-1 K+ channels and stimulate cortisol secretion by a protein kinase A-independent mechanism.

Haiyan Liu, Judith A Enyeart, John J Enyeart

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Two-pore domain potassium channels in the adrenal cortex.Pflugers Archiv : European journal of physiology · 2015
    Review
  4. Article
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 1 institution in 1 country.

Haiyan LiuDepartment of Neuroscience, OSU College of Medicine and Public Health, Columbus, OH, USA.
Judith A Enyeart
John J Enyeart
The Ohio State University · US

Funding

PROPERTIES OF K+ CURRENT THAT CONTROLS SECRETIONR01DK047875 · NIDDK · OHIO STATE UNIVERSITY · PI ENYEART, JOHN J · 1995 to 2008
$2.1M
NIDDK NIH HHS R01 DK047875NIDDK NIH HHS R01-DK47875
6 · The paper itself

Abstract

Bovine adrenal zona fasciculata (AZF) cells express bTREK-1 K+ channels whose inhibition by cAMP is coupled to membrane depolarization and cortisol secretion through complex signaling mechanisms. cAMP analogs with substitutions in the 6 position of the adenine ring selectively activate cAMP-dependent protein kinase (PKA) but not exchange proteins activated by cAMP (Epacs). In whole-cell patch-clamp recordings from AZF cells, we found that 6-benzoyl-cAMP (6-Bnz-cAMP) and 6-monobutyryl-cAMP potently inhibit bTREK-1 K+ channels, even under conditions in which PKA activity was abolished. Specifically, when applied through the patch electrode, 6-Bnz-cAMP inhibited bTREK-1 with an IC(50) of less than 0.2 microM. Inhibition of bTREK-1 by 6-Bnz-cAMP was not diminished by PKA antagonists, including N-[2-(4-bromocinnamylamino)ethyl]-5-isoquinoline (H-89), adenosine 3'-5'cyclic monophosphothiate, Rp-isomer, protein kinase inhibitor (PKI) (6-22) amide, and myristoylated PKI (14-22), applied alone or in combination, externally and intracellularly through the patch pipette. Under similar conditions, these same antagonists completely blocked PKA activation by 6-Bnz-cAMP. Inhibition of bTREK-1 by 6-Bnz-cAMP was voltage-independent and eliminated in the absence of ATP in the pipette solution. 6-Bnz-cAMP also produced delayed increases in cortisol synthesis and the expression of CYP11a1 mRNA that were only partially blocked by PKA antagonists. These results indicate that 6-Bnz-cAMP and other 6-substituted cAMP analogs can inhibit bTREK-1 K+ channels and stimulate delayed increases in cortisol synthesis by AZF cells through a PKA- and Epac-independent mechanism. They also suggest that adrenocorticotropin and cAMP function in these cells through a third cAMP-dependent protein. Finally, although 6-modified cAMP analogs exhibit high selectivity in activating PKA over Epac, they also may interact with other unidentified proteins expressed by eukaryotic cells.

Indexed as

Adrenocorticotropic HormoneAnimalsBlotting, NorthernCattleCells, CulturedCyclic AMPCyclic AMP-Dependent Protein KinasesHydrocortisoneMalePotassium Channel BlockersPotassium ChannelsPotassium Channels, Tandem Pore DomainTransfectionZona FasciculataAdrenocorticotropic HormoneCyclic AMPCyclic AMP-Dependent Protein KinasesHydrocortisoneN(6)-benzoyl-cyclic AMPPotassium Channel Blockerspotassium channel protein TREK-1Potassium ChannelsPotassium Channels, Tandem Pore Domain

Identifiers

PMID19734321
PMCPMC2784727
OpenAlexW2107490875

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.