Evidence map›Paper›PMID 25480783›Full record

ArticleThe Journal of biological chemistry2015

The TRPM8 protein is a testosterone receptor: I. Biochemical evidence for direct TRPM8-testosterone interactions.

Swapna Asuthkar, Pia A Elustondo, Lusine Demirkhanyan, Xiaohui Sun, Padmamalini Baskaran, Kiran Kumar Velpula, Baskaran Thyagarajan, Evgeny V Pavlov, Eleonora Zakharian

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Ion channels of cold transduction and transmission.The Journal of general physiology · 2024
    Review
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  10. Review
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  15. Article
  16. Frontiers in neurology · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. The role of the androgen receptor in the pathogenesis of obesity and its utility as a target for obesity treatments.Obesity reviews : an official journal of the International Association for the Study of Obesity · 2022
    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

9 authors at 5 institutions in 2 countries.

Swapna AsuthkarFrom the Department of Cancer Biology and Pharmacology, University of Illinois College of Medicine, Peoria, Illinois 61605.
Pia A ElustondoDalhousie University, Halifax, Nova Scotia B3H 4R2, Canada.
Lusine DemirkhanyanFrom the Department of Cancer Biology and Pharmacology, University of Illinois College of Medicine, Peoria, Illinois 61605.
Xiaohui SunFrom the Department of Cancer Biology and Pharmacology, University of Illinois College of Medicine, Peoria, Illinois 61605.
Padmamalini Baskaranthe College of Health Sciences, School of Pharmacy, University of Wyoming, Laramie, Wyoming 82071, and.
Kiran Kumar VelpulaFrom the Department of Cancer Biology and Pharmacology, University of Illinois College of Medicine, Peoria, Illinois 61605.
Baskaran Thyagarajanthe College of Health Sciences, School of Pharmacy, University of Wyoming, Laramie, Wyoming 82071, and.
Evgeny V PavlovDalhousie University, Halifax, Nova Scotia B3H 4R2, Canada, the Department of Basic Sciences, College of Dentistry, New York University, New York, New York 10010.
Eleonora ZakharianFrom the Department of Cancer Biology and Pharmacology, University of Illinois College of Medicine, Peoria, Illinois 61605, zakharel@uic.edu.
University of Illinois Urbana-Champaign · USIllinois College · USUniversity of Wyoming · USDalhousie University · CANew York University · US

Funding

Wyoming INBRE Phase 4- Equipment Supplement for x-ray diffractometer for Center for Advanced Scientific InstrumentationP20GM103432 · NIGMS · UNIVERSITY OF WYOMING · PI Robert Scott Seville · 2012 to 2026
$56.8M
TRP channels in supramolecular complexes with Inorganic Polyphosphate and PolyhydR01GM098052 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI ZAKHARIAN, ELEONORA · 2011 to 2015
$1.5M
NIGMS NIH HHS 8P20GM103432-12NIGMS NIH HHS P20 GM103432NIGMS NIH HHS R01 GM098052NIGMS NIH HHS R01GM098052
6 · The paper itself

Abstract

The transient receptor potential ion channel of the melastatin subfamily, TRPM8, is a major cold receptor in the peripheral nervous system. Along with the sensory neurons, the TRPM8 protein is highly expressed in the prostate epithelial cells, and this expression is regulated by androgens. Here we investigated the expression and intracellular localization of the TRPM8 channel in relationship to androgens. We performed experiments using human prostate tissues obtained from healthy individuals and patients with prostate cancer at various stages of the disease as well as in cultured cells. Using an immunohistochemistry approach, we detected an intensive colocalization pattern of the TRPM8 protein with endogenous androgens in all tissues tested, suggesting possible interactions. Co-immunoprecipitation experiments performed using cultured prostate epithelial cells, prostate cancer cells, and HEK-293 cells stably expressing TRPM8 further confirmed direct binding of the steroid hormone, testosterone, to the TRPM8 protein. Applications of picomolar concentrations of testosterone to the primary human prostate cells, endogenously expressing TRPM8, elicited Ca(2+) responses and channel currents, and those were inhibited in the presence of TRPM8 antagonist, N-(2-aminoethyl)-N-(4-(benzyloxy)-3-methoxybenzyl)thiophene-2-carboxamide hydrochloride. These results indicate that the TRPM8 channel is physically associated with testosterone and suggest that, in addition to a genomic role, testosterone plays a role in direct regulation of the TRPM8 channel function.

Indexed as

Cell LineCell Line, TumorEnzyme-Linked Immunosorbent AssayHEK293 CellsHumansImmunohistochemistryImmunoprecipitationMaleProtein BindingReceptors, AndrogenTestosteroneTRPM Cation ChannelsReceptors, AndrogenTestosteroneTRPM8 protein, humanTRPM Cation ChannelsAndrogenCalcium ChannelCold and Menthol Receptor TRPM8Ion ChannelTestosteroneTransient Receptor Potential Channels (TRP Channels)Transient Receptor Potential Melastatin 8 Channel

Identifiers

PMID25480783
PMCPMC4317017
OpenAlexW2016421933

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.