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Study · Measured the body's own peptide · 1993

4 results

Thymosin beta 4 (T beta 4) in activated platelets.

Nachmias VT, Cassimeris L, Golla R, Safer D

European journal of cell biology1 Aug 1993Cited by 32 (Europe PMC)

PMID8223720 (opens in a new tab)PepBankPUB-08223720
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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 study4

No result from this study comes from a test of the peptide.

Natural levels measured4

These results measure the body's own peptide. Nobody was given the peptide. They are not evidence about taking it. They are left out of key results, evidence counts and charts.

  1. 01LabEndogenous levelEx vivo tissueMechanism

    In human platelets stimulated with thrombin, the increase in F-actin matched a decrease in the complex of G-actin with thymosin beta‑4.

    In plain wordsIn human platelets, thrombin lowered the body's own thymosin beta‑4-actin complex as filament actin rose.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseG-actin:Tb4 complex after thrombin
    Study

    humann: not reported in source

    Human blood platelets
    Outcome group
    Receptor activity and mechanism · Cardiovascular

    Source sentences

    Summary
    The increase in F-actin is correlated with a corresponding decrease in the complex of G-actin with T beta 4.
    1 context sentence
    Summary · context
    When resting human blood platelets are stimulated with thrombin, 50 to 60% of the G-actin polymerizes to F-actin within 60 seconds.

    This result measures the body's own Thymosin beta-4 (human). Nobody was given the peptide. It is not evidence about taking it.

  2. 02LabEndogenous levelEx vivo tissueMechanism

    In thrombin-stimulated human platelets, cytochalasin D also inhibited the fall in the thymosin beta‑4-actin complex.

    In plain wordsIn human platelets, cytochalasin D prevented the fall in the body's own thymosin beta‑4-actin complex after thrombin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeG-actin:Tb4 complex with cytochalasin D
    Study

    humann: not reported in source

    Human blood platelets
    Outcome group
    Receptor activity and mechanism · Cardiovascular

    Source sentences

    Summary
    Cytochalasin D, known to inhibit the increase in F-actin after thrombin, also inhibits the fall in T beta 4-actin complex and the increase in nucleation sites.
    1 context sentence
    Summary · context
    When resting human blood platelets are stimulated with thrombin, 50 to 60% of the G-actin polymerizes to F-actin within 60 seconds.

    This result measures the body's own Thymosin beta-4 (human). Nobody was given the peptide. It is not evidence about taking it.

  3. 03LabEndogenous levelEx vivo tissueMechanism

    In human platelets, phosphorylation of thymosin beta‑4 could not be detected in control or activated cells.

    In plain wordsIn human platelets, no phosphorylation of the body's own thymosin beta‑4 was detected, in resting or activated cells.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeTb4 phosphorylation
    Study

    humann: not reported in source

    Human blood platelets
    Outcome group
    Receptor activity and mechanism · Cardiovascular

    Source sentences

    Summary
    Phosphorylation of T beta 4 could not be detected in either control or activated cells.
    1 context sentence
    Summary · context
    When resting human blood platelets are stimulated with thrombin, 50 to 60% of the G-actin polymerizes to F-actin within 60 seconds.

    This result measures the body's own Thymosin beta-4 (human). Nobody was given the peptide. It is not evidence about taking it.

  4. 04LabEndogenous levelEx vivo tissueMechanism

    In lysates of thrombin-activated human platelets, free thymosin beta‑4 increased in line with the amount lost from the thymosin beta‑4-actin complex, and it could still complex with actin.

    In plain wordsIn human platelets, activation raised free levels of the body's own thymosin beta‑4, which could still bind actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseFree Tb4 in activated platelet lysates
    Study

    humann: not reported in source

    Human blood platelets
    Outcome group
    Receptor activity and mechanism · Cardiovascular

    Source sentences

    Summary
    Increased T beta 4 corresponding to that lost from the T beta 4-actin complex is present in lysates from activated platelets and retains the ability to complex with actin.
    1 context sentence
    Summary · context
    When resting human blood platelets are stimulated with thrombin, 50 to 60% of the G-actin polymerizes to F-actin within 60 seconds.

    This result measures the body's own Thymosin beta-4 (human). Nobody was given the peptide. It is not evidence about taking it.

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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