Abstract
The retinoic acid-responsive thymosin beta-10 gene is known to be developmentally regulated in the human brain. We now report the novel finding that thymosin beta-4, a structurally related 5-kDa actin-sequestering protein, is also subject to a similar but not identical pattern of expression during normal human neuroembryogenesis. However, while thymosin beta-10 mRNA was undetectable (by northern blot analysis) in adult human brain, levels of thymosin beta-4 mRNA, although greatly reduced, were still present. Moreover, a novel thymosin beta-10-like gene was also found to exhibit a unique stage-specific expression during early human neural development. These experiments, together with previous findings, indicate that the products of the two thymosin genes, possibly in association with cytoskeletal elements, may play different roles during early neuroembryogenesis and neural maturation.
Similar content being viewed by others
References
Angelini, G., De Preval, C., Gorski, J., Mach, B. (1986). High resolution analysis of the human HLA-DR polymorphism by hybridization with sequence-specific oligonucleotide probes. Proc. Natl. Acad. Sci. U.S.A. 83:4489–4493
Atkinson, M.J., Freeman, M.W., Kronenberg, H.M. (1990). Thymosin beta-4 is expressed in ROS 17/2.8 osteosarcoma cells in a regulated manner. Mol. Endocrinol. 4:67–74
Bamberg, J.R., Bernstein, B.W. (1991). Actin and actin-binding proteins in neurons: The Neuronal Cytoskeleton. R.D. Burgoyne (ed). Wiley Press, New York, pp 121–160.
Border, B., Lin, S.-C., Griffin, W.S.T., Morrison-Bogorad, M. (1990). Evidence for the presence of two members of the thymosin peptide family in developing rat cerebellum. Soc. Neurosci. 16(1):80.8, p 176 (abstract)
Burgoyne, R.D. (1991). The Neuronal Cytoskeleton. Wiley Press, New York
Chomczynski, P., Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanatephenol-chloroform extraction. Anal. Biochem. 162:591–593
Dalakas, C., Trapp, B.D. (1986). Thymosin beta-4 is a shared antigen between lymphoid cells and oligodendrocytes of normal brain. Ann. Neurol. 19:349–355
Faivre-Sarrailh, C., Rabie, A. (1988). A lower proportion of filamentous to monomeric actin in the developing cerebellum of thyroid-deficient rats. Dev. Brain Res. 41:293–297
Feinberg, A.P., Vogelstein, B. (1984). A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 137:266–267
Goodall, G.J., Horecker, B.L. (1987). Molecular cloning of the cDNA for rat spleen thymosin beta-10 and the deduced amino acid sequence. Arch. Biochem. Biophys. 256:402–405
Goodall, G.J., Morgan, J.I., Horecker, B.L. (1983). Thymosin beta-4 in cultured mammalian cell lines. Arch. Biochem. Biophys. 221:598–601
Goodall, G.J., Richardson, M., Furuichi, Y., Wodnar-Filipowicz, Horecker, B.L. (1985). Sequence of a cloned 523bp cDNA for thymosin beta-4. Arch. Biochem. Biophys. 236:445–447
Grillon, C., Rieger, K., Bakala, J., Schott, D., Morgat, J.-L., Hannappel, E., Voelter, W., Lenfant, M. (1990). Involvement of thymosin beta-4 and endoproteinase Asp-N in the biosynthesis of the tetrapeptide AcSerAspLysPro a regulator of the hematopoietic system. FEBS Lett. 274:30–34
Hall, A.K. (1991a). Developmental regulation of thymosin beta-10 mRNA in the human brain. Mol. Brain Res. 9:175–177
Hall, A.K. (1991b). Retinoic acid and serum modulation of thymosin beta-10 gene expression in rat neuroblastoma cells. J. Mol. Neurosci. 2:229–237
Hall, A.K., Hempstead, J., Morgan, J.I. (1990). Thymosin beta-10 levels in the developing human brain and its regulation by retinoic acid in the HTB-10 neuroblastoma. Mol. Brain Res. 8:129–135
Hall, A.K., Chen, S.-C., Hempstead, J., Morgan, J.I. (1991). Retinoic acid regulates thymosin beta-10 levels in rat neuroblastoma cells. J. Neurochem. 56:462–468
Hannappel, E., Xu, G.-J., Morgan, J., Hempstead, J., Horecker, B.L. (1982). Thymosin beta-4, a ubiquitous peptide in rat and mouse tissues. Proc. Natl. Acad. Sci. U.S.A. 79:2172–2175
Harris, H.E., Weeds, A.G. (1978). Platelet actin: Subcellular distribution and association with profilin. FEBS Lett. 90:84–88
Horecker, B.L., Morgan, J.I. (1984). Ubiquitous distribution of thymosin beta-4 and related peptides in vertebrate cells and tissues. Lymphokines 9:15–35
Lin, S.-C., Morrison-Bogorad, M. (1990). Developmental expression of mRNAs encoding thymosins beta-4 and beta-10 in rat brain and other tissues. J. Mol. Neurosci. 2:35–44
Low, T.L.K., Goldstein, A.L. (1982). Chemical characterization of thymosin beta-4. J. Biol. Chem. 257:1000–1006
Low, T.L.K., Hu, S.-K., Goldstein, A.L. (1981). Complete amino acid sequence of bovine thymosin beta-4: A thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations. Proc. Natl. Acad. Sci. U.S.A. 78:1162–1166
Lugo, D.I., Chen, S.-C., Hall, A.K., Ziai, R., Hempstead, J.I., Morgan, J.I. (1991). Developmental regulation of beta-thymosins in the rat central nervous system. J. Neurochem. 56:457–461
Markey, F., Lindberg, U., Eriksson, L. (1978). Human platelets contain profilin, a potential regulator of actin polymerisability. FEBS Lett. 88:75–79
McCreary, V., Kartha, S., Bell, G.I., Toback, F.G. (1988). Sequence of a human kidney cDNA clone encoding thymosin beta-10. Biochem. Biophys. Res. Commun. 152:862–866
Safer, D., Elzinga, M., Nachmias, V.T. (1991). Thymosin beta-4 and Fx, an actin-sequestering peptide, are indistinguishable. J. Biol. Chem. 266:4029–4032
Schroeder, T.E. (1973). Actin in dividing cells: Contractive ring filaments bind heavy meromyosin. Proc. Natl. Acad. Sci. U.S.A. 70:1688–1692
Thomas, P.S. (1980). Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. U.S.A. 77:5201–5205
Watts, J.D., Cary, P.D., Sautiere, P., Crane-Robinson, C. (1990): Thymosins: Both nuclear and cytoplasmic proteins. Ein. J. Biochem. 192:643–651
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Condon, M.R., Hall, A.K. Expression of thymosin beta-4 and related genes in developing human brain. J Mol Neurosci 3, 165–170 (1992). https://doi.org/10.1007/BF02919408
Issue Date:
DOI: https://doi.org/10.1007/BF02919408