Thymosin α1

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2l9i thymosin alpha-1.png
Available structures
PDBHuman UniProt search: PDBe RCSB
AliasesPTMA, prothymosin, alpha, TMSA, prothymosin alpha
External IDsOMIM: 188390 HomoloGene: 136511 GeneCards: PTMA
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for PTMA
Genomic location for PTMA
Band2q37.1Start231,706,895 bp[1]
End231,713,541 bp[1]
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 2: 231.71 – 231.71 Mbn/a
PubMed search[2]n/a
View/Edit Human

Thymosin α1 is a peptide fragment derived from prothymosin alpha, a protein that in humans is encoded by the PTMA gene.[3]

It was the first of the peptides from Thymosin Fraction 5 to be completely sequenced and synthesized. Unlike β thymosins, to which it is genetically and chemically unrelated, thymosin α1 is produced as a 28-amino acid fragment, from a longer, 113-amino acid precursor, prothymosin α.[4]


Thymosin α1 is believed to be a major component of Thymosin Fraction 5 responsible for the activity of that preparation in restoring immune function in animals lacking thymus glands. It has been found to enhance cell-mediated immunity in humans as well as experimental animals.[5]

Therapeutic application[edit]

As of 2009 Thymosin α1 is approved in 35 under-developed or developing countries for the treatment of Hepatitis B and C, and it is also used to boost the immune response in the treatment of other diseases.[6][7]

Clinical studies[edit]

Clinical trials suggest it may be useful in cystic fibrosis, septic shock, acute respiratory distress syndrome, peritonitis, acute cytomegalovirus infection, TB, severe acute respiratory syndrome, and lung infections in critically ill patients.,[7] and for chronic hepatitis B.[8]

It has been studied for possible use in treating cancer (eg with chemotherapy).[9]

See also[edit]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000187514 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ Manrow RE, Leone A, Krug MS, Eschenfeldt WH, Berger SL (Jul 1992). "The human prothymosin alpha gene family contains several processed pseudogenes lacking deleterious lesions" (PDF). Genomics. 13 (2): 319–31. doi:10.1016/0888-7543(92)90248-Q. PMID 1612591.
  4. ^ Garaci E (September 2007). "Thymosin alpha1: a historical overview". Ann. N. Y. Acad. Sci. 1112: 14–20. doi:10.1196/annals.1415.039. PMID 17567941.
  5. ^ Wara DW, Goldstein AL, Doyle NE, Ammann AJ (January 1975). "Thymosin activity in patients with cellular immunodeficiency". N. Engl. J. Med. 292 (2): 70–4. doi:10.1056/NEJM197501092920204. PMID 1078552.
  6. ^ Garaci E, Favalli C, Pica F, et al. (September 2007). "Thymosin alpha 1: from bench to bedside". Ann. N. Y. Acad. Sci. 1112: 225–34. doi:10.1196/annals.1415.044. PMID 17600290.
  7. ^ a b Goldstein AL, Goldstein AL (May 2009). "From lab to bedside: emerging clinical applications of thymosin alpha 1". Expert Opin Biol Ther. 9 (5): 593–608. doi:10.1517/14712590902911412. PMID 19392576.
  8. ^ Wu X, Jia J, You H (2015). "Thymosin alpha-1 treatment in chronic hepatitis B". Expert Opinion on Biological Therapy. 15: 129–132. doi:10.1517/14712598.2015.1007948.
  9. ^ Garaci E, Pica F, Rasi G, Favalli C (2000). "Thymosin alpha 1 in the treatment of cancer: from basic research to clinical application". Int J Immunopharmacol. 22: 1067–76. PMID 11137613.

Further reading[edit]