Three distinct human thymopoietins are derived from alternatively spliced mRNAs

Crafford A. Harris, Paula J. Andryuk, Scott Cline, H. Karen Chan, Anan Natarajan, John J. Siekierka, Gideon Goldstein

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104 Scopus citations


Thymopoietin (TP) was originally isolated as a 5-kDa 49-aa protein from bovine thymus in studies of the effects of thymic extracts on neuromuscular transmission and was subsequently observed to affect T-cell differentiation and function. We now report the isolation of cDNA clones for three alternatively spliced mRNAs that encode three distinct human T-cell TPs. Proteins encoded by these mRNAs, which we have named TPα (75 kDa), TPβ (51 kDa), and TPγ (39 kDa), contain identical N-terminal regions, including sequences nearly identical to that of the originally isolated 49-aa protein, but divergent C-terminal regions. TP mRNAs are expressed in many tissues, most abundantly in adult thymus and fetal liver of the tissues so far examined. Distinct structural domains and functional motifs in TPs α, β, and γ suggest that the proteins have unique functions and may be directed to distinct subcellular compartments.

Original languageEnglish
Pages (from-to)6283-6287
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number14
StatePublished - 5 Jul 1994


  • alternative splicing
  • nuclear proteins
  • thymic proteins


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