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Study · In vitro (cells) · 2018

3 results

Sodium functions as a negative allosteric modulator of the oxytocin receptor.

Schiffmann A, Gimpl G

Biochimica et biophysica acta. Biomembranes7 Mar 2018Cited by 12 (Europe PMC)

PMID29524392 (opens in a new tab)DOI10.1016/j.bbamem.2018.03.003 (opens in a new tab)PepBankPUB-29524392
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study3

3 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Mechanism

    In membranes from HEK293 cells expressing the oxytocin receptor, raising sodium chloride from 0 to 300 mM lowered oxytocin binding affinity about 15-fold.

    In plain wordsIn cell membranes, more sodium made oxytocin bind its receptor about 15 times more weakly.

    Peptide
    Oxytocin
    Outcome
    DecreaseOxytocin binding affinity with increasing sodium chloride
    Study

    humann: not reported in source

    HEK293 cell membranes expressing the oxytocin receptor
    Comparator
    0 mM sodium chloride
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Affinity decrease
    ≈ 15 fold
    NaCl 0 to 300 mM

    Source sentences

    Summary
    In membranes from HEK293 cells stably expressing the oxytocin receptor, oxytocin binding occurred with about 15-fold lower affinity when sodium chloride was increased from 0 to 300 mM, whereas antagonist binding remained largely unchanged.
    1 context sentence
    Summary · context
    Using displacement assays with a high-affinity fluorescent antagonist (OTAN-A647), we now show that sodium functions as a negative allosteric modulator of the oxytocin receptor.
  2. 02LabIn vitro (cells)Mechanism

    The sodium-dependent reduction of oxytocin binding was also seen for oxytocin receptors that Hs578T breast cancer cells express naturally.

    In plain wordsIn cells, the sodium effect on oxytocin binding also occurred in breast cancer cells with their own oxytocin receptors.

    Peptide
    Oxytocin
    Outcome
    DecreaseSodium effect on oxytocin binding in Hs578T cells
    Study

    humann: not reported in source

    Hs578T breast cancer cells (endogenous oxytocin receptor)
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The effect was concentration-dependent, sodium-specific, and it was also observed for oxytocin receptors endogenously expressed in Hs578T breast cancer cells.
    1 context sentence
    Summary · context
    Using displacement assays with a high-affinity fluorescent antagonist (OTAN-A647), we now show that sodium functions as a negative allosteric modulator of the oxytocin receptor.
  3. 03LabIn vitro (cells)Mechanism

    A sodium effect on oxytocin binding was not detectable for the D85E mutant oxytocin receptor.

    In plain wordsIn cells, sodium had no detectable effect on oxytocin binding to the mutant receptor with Asp 85 replaced by Glu.

    Peptide
    Oxytocin
    Outcome
    No significant changeSodium effect on oxytocin binding to D85E mutant receptor
    Study

    humann: not reported in source

    Cells expressing the D85E mutant oxytocin receptor
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    However, a sodium effect was not detectable for the mutant D85E oxytocin receptors.
    1 context sentence
    Summary · context
    Using displacement assays with a high-affinity fluorescent antagonist (OTAN-A647), we now show that sodium functions as a negative allosteric modulator of the oxytocin receptor.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    11 Oct 2026, 01:30 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 02:48 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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