The beta -thymosins are a family of highly conserved polar 5 kDa peptides o
riginally thought to be thymic hormones. About 10 years ago, thymosin beta
(4) as well as other members of this ubiquitous peptide family were identif
ied as the main intracellular G-actin sequestering peptides, being present
in high concentrations in almost every cell. beta -Thymosins bind monomeric
actin in a 1:1 complex and act as actin buffers, preventing polymerization
into actin filaments but supplying a pool of actin monomers when the cell
needs filaments. Changes in the expression of beta -thymosins appear to be
related to the differentiation of cells. Increased expression of beta -thym
osins or even the synthesis of a beta -thymosin normally not expressed migh
t promote metastasis possibly by increasing mobility of the cells. Thymosin
beta (4) is detected outside of cells in blood plasma or in wound fluid. S
everal biological effects are attributed to thymosin beta (4), oxidized thy
mosin beta (4), or to the fragment, acSDKP, possibly generated from thymosi
n beta (4). Among the effects are induction of metallo-proteinases, chemota
xis, angiogenesis and inhibition of inflammation as well as the inhibition
of bone marrow stem cell proliferation. However, nothing is known about the
molecular mechanisms mediating the effects attributed to extracellular bet
a -thymosins. (C) 2001 Elsevier Science Ltd. All rights reserved.