Thymosin beta4 is not always the main beta-thymosin in mammalian platelets.

beta-thymosins constitute a family of highly conserved 5-kDa polypeptides. Thymosin beta(4), the most abundant member of this family, is expressed in most mammalian cell types and is regarded as the main intracellular G-actin sequestering peptide. In addition to this important intracellular function several other activities have been attributed to this peptide. Thymosin beta(4) is released from human platelets and cross-linked to fibrin after activation of platelets with thrombin. While in most mammalian tissues thymosin beta(4) is accompanied by a second member of this peptide family, in human platelets only thymosin beta(4) is present. To elucidate if it is common to mammalian platelets that only one beta-thymosin is present, we analyzed platelets from several mammals for their beta-thymosin content. In human platelets only thymosin beta(4) could be detected, whereas in bovine platelets thymosin beta(9), which is normally the minor beta-thymosin in bovine tissues, was identified as the main beta-thymosin. In rabbit platelets, thymosin beta(4) is not simply replaced by the most homologous thymosin beta(4)(Ala), as might be expected from sequence homology. Thymosin beta(4)(Ala) and thymosin beta(10) were found, but thymosin beta(10) is present in about 2.5-fold higher amounts. Because thymosin beta(4)(Ala) possesses about threefold higher affinity to G-actin, compared to thymosin beta(4), beta(10), and beta(9), we suggest that expression of beta-thymosins is triggered by functional requirements and not sequence homology.