Add time:08/13/2019         Source:sciencedirect.com

The beta-thymosins are a family of <5kDa (MW), mostly acidic, proteins which were originally defined in the immune system. Recently, specific members of this family of cytoplasmic polypeptides, namely beta-4 and beta-10, were shown to bind monomeric G-actin both in vitro and in vivo. Whilst many aspects of programmed cell death or ‘apoptosis’ remain to be defined, the Ca2+Mg2+-dependent endonuclease, DNase I does feature in this process. Monomeric G-actin binds to and inhibits the DNA-degrading activity of DNase I. Given that the intracellular abundance of thymosins beta-4 and beta-10 is related to cell division and differentiation and that anticancer/morphogenic agents such as retinoic acid (RA) and cyclic AMP modulate expression of their respective genes, it is possible that these G-actin sequestering proteins play significant roles in apoptosis perhaps mediated via DNase I.

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