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Study · In vitro (cell-free) · 2007

7 results

Thymosin beta4: actin regulation and more.

Yarmola EG, Klimenko ES, Fujita G, Bubb MR

Annals of the New York Academy of Sciences1 Sept 2007Cited by 24 (Europe PMC)

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 study7

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

  1. 01LabIn vitro (cell-free)Mechanism

    In biochemical tests, thymosin beta‑4 affected the critical concentration of actin.

    In plain wordsIn lab tests, thymosin beta‑4 changed the critical concentration of actin.

    Outcome
    Not applicableEffect on actin critical concentration
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Our recent studies revealed that thymosin beta(4) affects actin critical concentration and forms a ternary complex with actin and profilin.
  2. 02LabIn vitro (cell-free)Mechanism

    In biochemical tests, thymosin beta‑4 formed a ternary complex with actin and profilin.

    In plain wordsIn lab tests, thymosin beta‑4 formed a three-part complex with actin and profilin.

    Outcome
    Not applicableTernary complex with actin and profilin
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Our recent studies revealed that thymosin beta(4) affects actin critical concentration and forms a ternary complex with actin and profilin.
  3. 03LabIn vitro (cell-free)Mechanism

    In biochemical tests, profilin likely affected binding of thymosin beta‑4 to actin in the ternary complex through allosteric changes in actin rather than competition for the binding site.

    In plain wordsIn lab tests, profilin likely changed how thymosin beta‑4 binds actin by altering actin shape, not by competing for the site.

    Outcome
    Not applicableProfilin effect on thymosin beta-4 binding to actin
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Our new data demonstrate that it is likely that profilin affects binding of thymosin beta(4) to actin in the ternary complex through allosteric changes in actin rather than through competition for the binding site.
  4. 04LabIn vitro (cell-free)Mechanism

    In biochemical tests, TMAO significantly increased the affinity of intact thymosin beta‑4 for actin.

    In plain wordsIn lab tests, TMAO made intact thymosin beta‑4 bind actin more strongly.

    Outcome
    IncreaseTMAO effect on binding of intact thymosin beta-4 to actin
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Osmolytes stabilize protein structure, and TMAO (trimethylamine N-oxide) specifically stabilizes hydrogen bonds. This increases affinity of intact thymosin beta(4) to actin significantly, but the increase is much less for thymosin beta(4) sulfoxide.
  5. 05LabIn vitro (cell-free)Mechanism

    In biochemical tests, the TMAO-induced increase in affinity for actin was much smaller for thymosin beta‑4 sulfoxide than for intact thymosin beta‑4.

    In plain wordsIn lab tests, TMAO raised actin binding much less for oxidized thymosin beta‑4 than for intact thymosin beta‑4.

    Outcome
    IncreaseTMAO effect on binding of thymosin beta-4 sulfoxide to actin
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    but the increase is much less for thymosin beta(4) sulfoxide.
    1 context sentence
    Summary · context
    Osmolytes stabilize protein structure, and TMAO (trimethylamine N-oxide) specifically stabilizes hydrogen bonds.
  6. 06LabIn vitro (cell-free)Mechanism

    In biochemical tests, oxidation of thymosin beta‑4 did not alter binding of profilin to form the ternary complex.

    In plain wordsIn lab tests, oxidizing thymosin beta‑4 did not change how profilin joined the three-part complex.

    Outcome
    No significant changeOxidation effect on profilin ternary complex formation
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Our data show that oxidation does not alter binding of profilin to form a ternary complex, and therefore it is very likely that there is no direct steric interference by methionine 6 of thymosin beta(4).
  7. 07LabIn vitro (cell-free)Mechanism

    In biochemical tests, actin and, to a lesser extent, the profilin-actin complex protected thymosin beta‑4 from oxidation.

    In plain wordsIn lab tests, actin and, less so, the profilin-actin complex shielded thymosin beta‑4 from oxidation.

    Outcome
    DecreaseProtection of thymosin beta-4 from oxidation
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    We found that actin and, in lesser extent, profilin-actin complex protect thymosin beta(4) from oxidation.

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

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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