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Study · Ex vivo tissue · 1991

4 results

Formation of acetyl-Ser-Asp-Lys-Pro, a new regulator of the hematopoietic system, through enzymatic processing of thymosin beta 4.

Lenfant M, Grillon C, Rieger KJ, Sotty D, Wdzieczak-Bakala J

Annals of the New York Academy of Sciences1 Jan 1991Cited by 10 (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 study4

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

  1. 01LabEx vivo tissueMechanism

    Incubating labeled thymosin beta‑4 with intact or lysed bone marrow cells led to the formation of labeled AcSDKP, which was not degraded.

    In plain wordsIn lab tests, bone marrow cells turned thymosin beta‑4 into AcSDKP.

    Outcome
    IncreaseAcSDKP formation from labeled thymosin beta 4
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Incubation of [3H]T beta 4 with either intact or lysed BMC led to the formation of [3H]AcSDKP, whereas the labeled tetrapeptide was not degraded under these conditions.
  2. 02LabIn vitro (cell-free)Mechanism

    Model degradation of thymosin beta‑4 with bacterial enzymes suggests that mammalian endoproteinase Asp-N could form AcSDKP by cleaving the Pro4-Asp5 bond.

    In plain wordsIn lab tests, enzyme experiments suggest that Asp-N could cut thymosin beta‑4 to make AcSDKP.

    Outcome
    Not applicableEnzymatic cleavage of thymosin beta 4 to AcSDKP
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Model enzymatic degradation of T beta 4 carried out with bacterial enzymes suggests that a mammalian endoproteinase Asp-N might be involved in the formation of AcSDKP through the specific cleavage of the Pro4-Asp5 peptidic bond of T beta 4.
  3. 03LabIn vitro (cell-free)Mechanism

    Alpha-prolyl-endopeptidase was ineffective in processing thymosin beta‑4 to AcSDKP in the model enzymatic system.

    In plain wordsIn lab tests, the enzyme alpha-prolyl-endopeptidase did not cut thymosin beta‑4 to make AcSDKP.

    Outcome
    No significant changeProcessing of thymosin beta 4 by alpha-prolyl-endopeptidase
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In contrast, alpha-prolyl-endopeptidase was ineffective in carrying out a similar processing.

Natural levels measured1

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. 04LabEndogenous levelEx vivo tissueMechanism

    Both AcSDKP and the body's own thymosin beta‑4 were detected in bone marrow cells.

    In plain wordsIn lab tests, bone marrow cells contained the body's own thymosin beta‑4 and AcSDKP.

    Outcome
    Not applicableDetection of thymosin beta 4 and AcSDKP in bone marrow cells
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Immune and inflammation

    Source sentences

    Summary
    AcSDKP and T beta 4 were both detected in bone marrow cells (BMC).

    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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