Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (622 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
Thymosin. A family of heat-stable, polypeptide hormones secreted by the thymus gland. Their biological activities include lymphocytopoiesis, restoration of immunological competence and enhancement of expression of T-cell characteristics and function. They have therapeutic potential in patients having primary or secondary immunodeficiency diseases, cancer or diseases related to aging.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Thymosins; Thymosin Fs.
Where it fits in the MeSH classification
- Broader topics
- Thymus Hormones; Peptide Hormones; Proteins
- Narrower topics
- Thymalfasin; Thymosin beta(4)
Research landscape
PubMed indexes 2,875 records tagged with the MeSH heading “Thymosin” (counts retrieved 2026-10-31). 314 of them (10.9%) were published from 2020 onward, and the busiest period so far is through 1999 with 1,307 records.
Reviews account for 314 records (10.9%) and meta-analyses for 24. Randomized controlled trials number 85 (3.0%) as a share of all records on the topic.
Show the data
| Period | Records |
|---|---|
| through 1999 | 1,307 |
| 2000-2009 | 557 |
| 2010-2019 | 697 |
| 2020 onward | 314 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 314 | 10.9% |
| Meta-analyses | 24 | 0.8% |
| Randomized controlled trials | 85 | 3.0% |
Method: PubMed query "Thymosin"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Progress on the Function and Application of Thymosin β4 | 2021 | Review article Design not recorded in structured metadata | 56 | cc by PMID 34992578 · DOI · PMC8724243 |
| Tumour prothymosin alpha content, a potential prognostic marker for primary breast cancer | 2000 | Research article Design not recorded in structured metadata | 47 | cc by PMID 10682670 · DOI · PMC2363325 |
| TMSB4Y is a candidate tumor suppressor on the Y chromosome and is deleted in male breast cancer | 2015 | Research article Design not recorded in structured metadata | 35 | cc by PMID 26702755 · DOI · PMC4792601 |
| Decidualization-empowered ECM hydrogel integrating sustained Tβ4 release drives endometrial regeneration in intrauterine adhesions | 2026 | Research article Design not recorded in structured metadata | 3 | cc by PMID 41565687 · DOI · PMC12923885 |
Progress on the Function and Application of Thymosin β4 [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Thymosin β4 (Tβ4) is a multifunctional and widely distributed peptide that plays a pivotal role in several physiological and pathological processes in the body, namely, increasing angiogenesis and proliferation and inhibiting apoptosis and inflammation.
- Closing excerpt
- The present study reveals the progress regarding functions and applications of Tβ4.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (94 words)
Thymosin β4 (Tβ4) is a multifunctional and widely distributed peptide that plays a pivotal role in several physiological and pathological processes in the body, namely, increasing angiogenesis and proliferation and inhibiting apoptosis and inflammation. Moreover, Tβ4 is effectively utilized for several indications in animal experiments or clinical trials, such as myocardial infarction and myocardial ischemia-reperfusion injury, xerophthalmia, liver and renal fibrosis, ulcerative colitis and colon cancer, and skin trauma. Recent studies have reported the potential application of Tβ4 and its underlying mechanisms. The present study reveals the progress regarding functions and applications of Tβ4.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34992578 · DOI · PMC8724243
Tumour prothymosin alpha content, a potential prognostic marker for primary breast cancer [2]
Abstract reading summary — source excerpts
- Opening excerpt
- In a previous report we suggested that the estimation of prothymosin alpha (PTA) levels in primary breast tumours might be used to identify breast cancer patients at high risk for distant metastasis (Dominguez F et al (1993) Eur J Cancer 29A: 893-897).
- Closing excerpt
- In conclusion, these data support the hypothesis that tumour high PTA levels is associated with a worse outcome.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (196 words)
In a previous report we suggested that the estimation of prothymosin alpha (PTA) levels in primary breast tumours might be used to identify breast cancer patients at high risk for distant metastasis (Dominguez F et al (1993) Eur J Cancer 29A: 893-897). Here the role of tumour PTA levels as predictor was investigated with respect to both disease-free survival (DFS) and survival. Tumours were obtained from a series of 210 consecutive female patients with ductal carcinoma who underwent surgery at the Hospital Xeral de Galicia (Santiago de Compostela, Spain). Characteristics including PTA tumour levels, number of positive axillary nodes, patient's age at surgery and tumour histological grade were significantly associated with DFS and survival, as determined by univariate analysis. Patients with tumours with low or moderate PTA levels demonstrated a statistically decreased rate of tumour recurrence and a statistically significant increased overall survival in comparison with those whose tumours had high PTA levels. Patient's relative risk of dying was 2.1 times greater for tumours with high PTA levels than for those tumours with low or moderate PTA levels. In conclusion, these data support the hypothesis that tumour high PTA levels is associated with a worse outcome.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 10682670 · DOI · PMC2363325
TMSB4Y is a candidate tumor suppressor on the Y chromosome and is deleted in male breast cancer [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Male breast cancer comprises less than 1% of breast cancer diagnoses.
- Closing excerpt
- Taken together, our results suggest that clonal loss of the Y chromosome may contribute to male breast carcinogenesis, and that the TMSB4Y gene has tumor suppressor properties.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (190 words)
Male breast cancer comprises less than 1% of breast cancer diagnoses. Although estrogen exposure has been causally linked to the development of female breast cancers, the etiology of male breast cancer is unclear. Here, we show via fluorescence in situ hybridization (FISH) and droplet digital PCR (ddPCR) that the Y chromosome was clonally lost at a frequency of ~16% (5/31) in two independent cohorts of male breast cancer patients. We also show somatic loss of the Y chromosome gene TMSB4Y in a male breast tumor, confirming prior reports of loss at this locus in male breast cancers. To further understand the function of TMSB4Y, we created inducible cell lines of TMSB4Y in the female human breast epithelial cell line MCF-10A. Expression of TMSB4Y resulted in aberrant cellular morphology and reduced cell proliferation, with a corresponding reduction in the fraction of metaphase cells. We further show that TMSB4Y interacts directly with β-actin, the main component of the actin cytoskeleton and a cell cycle modulator. Taken together, our results suggest that clonal loss of the Y chromosome may contribute to male breast carcinogenesis, and that the TMSB4Y gene has tumor suppressor properties.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 26702755 · DOI · PMC4792601
Decidualization-empowered ECM hydrogel integrating sustained Tβ4 release drives endometrial regeneration in intrauterine adhesions [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Intrauterine adhesions (IUA), a leading cause of female infertility, result from a pathological switch in the uterine injury response from regeneration to fibrotic scarring.
- Closing excerpt
- Together, these findings demonstrate that mimicking the biological intelligence of a physiological niche can resolve complex fibrotic diseases and restore organ function.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (142 words)
Intrauterine adhesions (IUA), a leading cause of female infertility, result from a pathological switch in the uterine injury response from regeneration to fibrotic scarring. Current treatments are often inadequate as they fail to address this fundamental shift. Here, we report a "decidualization-empowered" hydrogel that reverses this pathology by synergistically combining a bioactive extracellular matrix from decidualized endometrium (DEndo-UdECM) with the sustained release of the anti-fibrotic peptide Thymosin β4 (Tβ4). In a murine IUA model, a single administration of the hydrogel restores endometrial architecture, resolves fibrosis, and, most critically, leads to a near-complete recovery of fertility. Mechanistically, the hydrogel orchestrates a pro-regenerative niche by reprogramming macrophages to an M2 phenotype while dually inhibiting pyroptosis-driven inflammation and the canonical TGF-β/Smad3 fibrotic cascade. Together, these findings demonstrate that mimicking the biological intelligence of a physiological niche can resolve complex fibrotic diseases and restore organ function.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41565687 · DOI · PMC12923885
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article beta-Thymosins, small acidic peptides with multiple functions [5]
- Research article Thymosin beta4: actin-sequestering protein moonlights to repair injured tissues [6]
- Research article Reconsidering an active role for G-actin in cytoskeletal regulation [7]
- Research article Thymosin beta4: structure, function, and biological properties supporting current and future clinical applications [8]
- Research article Biological activities of thymosin beta4 defined by active sites in short peptide sequences [9]
- Research article The beta-thymosins: intracellular and extracellular activities of a versatile actin binding protein family [10]
References
- Xing Y, Ye Y, Zuo H, Li Y. Progress on the Function and Application of Thymosin β4. . 2021. PMID 34992578 · DOI · PMC8724243
- Magdalena C, Dominguez F, Loidi L, Puente JL. Tumour prothymosin alpha content, a potential prognostic marker for primary breast cancer. . 2000. PMID 10682670 · DOI · PMC2363325
- Wong HY, Wang GM, Croessmann S, Zabransky DJ, Chu D, Garay JP, et al.. TMSB4Y is a candidate tumor suppressor on the Y chromosome and is deleted in male breast cancer. . 2015. PMID 26702755 · DOI · PMC4792601
- Liang Y, Yu Z, Du S, Guo Y, Li J, Yan Y, et al.. Decidualization-empowered ECM hydrogel integrating sustained Tβ4 release drives endometrial regeneration in intrauterine adhesions. . 2026. PMID 41565687 · DOI · PMC12923885
- Huff T, Müller CS, Otto AM, Netzker R, Hannappel E. beta-Thymosins, small acidic peptides with multiple functions. Int J Biochem Cell Biol. 2001. PMID 11311852 · DOI
- Goldstein AL, Hannappel E, Kleinman HK. Thymosin beta4: actin-sequestering protein moonlights to repair injured tissues. Trends Mol Med. 2005. PMID 16099219 · DOI
- Skruber K, Read TA, Vitriol EA. Reconsidering an active role for G-actin in cytoskeletal regulation. J Cell Sci. 2018. PMID 29321224 · DOI · PMC5818056
- Crockford D, Turjman N, Allan C, Angel J. Thymosin beta4: structure, function, and biological properties supporting current and future clinical applications. Ann N Y Acad Sci. 2010. PMID 20536467 · DOI
- Sosne G, Qiu P, Goldstein AL, Wheater M. Biological activities of thymosin beta4 defined by active sites in short peptide sequences. FASEB J. 2010. PMID 20179146 · DOI
- Mannherz HG, Hannappel E. The beta-thymosins: intracellular and extracellular activities of a versatile actin binding protein family. Cell Motil Cytoskeleton. 2009. PMID 19405116 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
See how EvidenceLib is built. Spotted an error? Email support@evidencehelix.com.
Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.