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Study · Animal study (in vivo) · mouse · 2006

4 results

Thymosin beta4 promotes matrix metalloproteinase expression during wound repair.

Philp D, Scheremeta B, Sibliss K, Zhou M, Fine EL, Nguyen M, Wahl L, Hoffman MP, Kleinman HK

Journal of cellular physiology1 Jul 2006Cited by 51 (Europe PMC)

PMID16607611 (opens in a new tab)DOI10.1002/jcp.20650 (opens in a new tab)PepBankPUB-16607611
Publisher pagePubMedAsk about this study
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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

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

  1. 01AnimalAnimal study (in vivo)Activity measurement

    In mouse dermal wounds, Tbeta4 increased expression of several metalloproteinases, including MMP-2 and MMP-9, several-fold over control on day 2 after wounding.

    In plain wordsIn mice, Tbeta4 raised levels of several wound-related enzymes, including MMP-2 and MMP-9, compared with control on day 2.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseMMP-2 and MMP-9 expression in mouse wounds
    Study

    mousen: not reported in source

    excised dermal wounds
    Comparator
    Control
    Outcome group
    Wound healing · Skin and wound
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Analysis by RT-PCR of whole excised mouse dermal wounds on days 1, 2, and 3 after wounding showed that Tbeta4 increased several metalloproteinases, including MMP-2 and -9 expression by several-fold over control on day 2 after wounding.
  2. 02LabIn vitro (cells)Activity measurement

    In cultured keratinocytes, endothelial cells and fibroblasts, increasing Tbeta4 concentrations raised MMP-1, MMP-2 and MMP-9 levels in a cell-specific manner.

    In plain wordsIn cells, Tbeta4 raised levels of several wound-related enzymes, differing by cell type.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseMMP-1, MMP-2 and MMP-9 levels in cultured wound cells
    Study

    n: not reported in source

    cultured keratinocytes, endothelial cells and fibroblasts
    Outcome group
    Wound healing · Skin and wound
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Western blot analysis of cultured keratinocytes, endothelial cells, and fibroblasts that were treated with increasing concentrations of Tbeta4 showed increases in the levels of MMP-1, -2, and -9 in a cell-specific manner.
  3. 03LabIn vitro (cells)Activity measurement

    In activated monocytes, Tbeta4 enhanced secretion of MMP-1 and MMP-9.

    In plain wordsIn cells, Tbeta4 increased release of two wound-related enzymes from activated monocytes.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseMMP-1 and MMP-9 secretion by activated monocytes
    Study

    n: not reported in source

    activated monocytes
    Outcome group
    Wound healing · Skin and wound
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Tbeta4 also enhanced the secretion of MMP-1 and MMP-9 by activated monocytes.

Studies that did not test the peptide alone1

In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin beta-4 (human).

  1. 04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cells)Mechanism

    The central actin-binding domain of Tbeta4, amino acids 17-23, had all of the metalloproteinase induction activity.

    In plain wordsIn lab tests, a short central region of Tbeta4 carried all of its ability to raise wound-related enzymes.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableDomain of Tbeta4 responsible for MMP induction
    Study

    n: not reported in source

    cultured wound cells
    Outcome group
    Receptor activity and mechanism · Skin and wound

    Source sentences

    Summary
    The central actin-binding domain, amino acids 17-23, had all of the activity for metalloproteinase induction.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

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.

Publication types

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