Abstract
Activin, a peptide growth factor, is a member of the transforming growth factor-β (TGF-β) superfamily. It was originally isolated from follicle fluid as a gonadal hormone that stimulates follicle-stimulating hormone (FSH) secretion and is identical to EDF, the erythroid differentiation factor (which stimulates erythroleukemia cells to differentiate into hemoglobin-producing cells) (1). It also appears to be related, if not identical, to the so-called “vegetalizing factor”described originally by Tiedemann and colleagues, which can induce amphibian embryonic tissue rudiments to display various differentiation patterns (reviewed in ref. 2). In addition, it appears to be identical to the XTC factor isolated by Smith et al. (3) from transformed Xenopus fibroblasts. Thus, the identification of activin as a potential morphogen in amphibian embryos (4) solved several mysteries surrounding the puzzle regarding the molecular nature of various hitherto ill-characterized “inducing substances.“
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Murata, M., Eto, Y., Shibai, H., Sakai, M., and Muramatsu, M. (1988) Erythroid differentiation factor is encoded by the same mRNA as that of inhibin βA chain. Proc. Natl. Acad. Sci. USA 85, 2434–2438.
Tiedemann, H., Asashima, M., Born, J., Grunz, H., Knochel, W., and Tiedemann, H. (1996) Determination, inductin and pattern formation in early amphibian embryos. Dev. Growth Differ. 36, 233–246.
Smith, J. C., Price, B. M. J., van Nimmen, K., and Huylebroek, D. (1990) Identification of a potent Xenopus mesoderm inducing factor as a homologue of activin A. Nature 345, 729–731.
Asashima, M., Nakano, H., Shimada, K., Kinoshita, K., Ishi, K., Shibai, H., and Ueno, N. (1990) Mesodermal induction in early amphibian embryos by activin A. Roux’s Arch. Dev. Biol. 198, 330–335.
Fukui, A., Nakamura, T., Uchiyama, H., Sugino, K., and Asashima, M. (1994) Identification of activins A, AB, and B and follistatin proteins in Xenopus embryos. Dev. Biol. 163, 279–281.
Asashima, M., Nakano, H., Uchiyama, H., Sugino, H., Nakamura, T., Eto, Y, Ejima, D., Nishimatsu, S., Ueno, N., and Kinoshita, K. (1991) Presence of activin (erythroid differentiation factor) in unfertilized eggs and blastulae of Xenopus laevis. Proc. Natl. Acad. Sci. USA 88, 6511–6514.
Uchiyama, H., Nakamura, T., Komazaki, S., Takio, K., Asashima, M., and Sugino, H. (1994) Localization of activin and follistatin proteins in the Xenopus oocyte. Biochem. Biophys. Res. Commun. 202, 484–489.
Dohrmann, C. E., Hemmati-Brivanlou, A., Thomsen, G. H., Fields, A., Woolf, T. M., and Melton, D. A. (1993) Expression of activin mRNA during early development in Xenopus laevis. Dev. Biol. 157, 474–483.
Okabayashi, K., Shoji, H., Nakamura, O., Nakamura, T., Hashimoto, O., Asashima, M., and Sugino, H. (1996) cDNA cloning and expression of the Xenopus laevis vitellogenin receptor. Biochem. Biophys. Res. Commun. 224, 406–413.
Dohrmann, C. A., Hemmati-Brivanlou, A., Thomsen, G. H., Fields, A., Woolf, T. M., and Melton, D. A. (1993) Expression of activin mRNA during early development of Xenopus laevis. Dev. Biol. 157, 474–483.
Ariizumi, T., Moriya, N., Uchiyama, H., and Asashima, M. (1991) Concentration dependent inducing activity of activin A. Roux’s Arch. Dev. Biol. 200, 230–233.
Green, J. B. and Smith, J. C. (1990) Graded changes in dose of a Xenopus activin A homologue elicit stepwise transitions in embryonic cell fate. Nature 347, 391–394.
Ariizumi, T. and Asashima, M. (1995) Head and trunk-tail organizing effects of the gas-trula ectoderm of Cynops pyrrogaster after treatment with activin A. Roux’s Arch. Dev. Biol. 204, 427–435.
Uochi, T., and Asashima, M. (1996) Sequential gene expression during pronephric tubule formation in vitro in Xenopus ectoderm. Dev. Growth Differ. 38, 625–634.
Ariizumi, T., Komazaki, S., Asashima, M., and Malacinski, G. M. (1996) Activin treated urodele ectoderm: a model experimental system for cardiogenesis. Int. J. Dev. Biol. 40, 715–718.
Ariizumi, T., Sawamura, K., Uchiyama, H., and Asashima, M. (1991) Dose and time-dependent mesoderm induction and outgrowth formation by activin A in Xenopus laevis. Int. J. Dev. Biol. 35, 407–414.
Kondo, M., Tashiro, K., Fujii, G., Asano, M., Miyoshi, R., Yamada, R., Muramatsu, M., and Shiokawa, K. (1991) Activin receptor mRNA is expressed early in Xenopus embryogenesis and the level of the expression affects the body axis formation. Biochem. Biophys. Res. Commun. 181, 684–690.
Hemmati-Brivanlou, A., Wright, D. A., and Melton, D. A. (1992) Embryonic expression and functional analysis of a Xenopus activin receptor. Dev. Dyn. 194, 1–11.
Armes, N. A. and Smith, J. C. (1997) The ALK-2 and ALK-4 activin receptors transduce distinct mesoderm-inducing signals during early Xenopus development but do not cooperate to establish thresholds. Development 124, 3797–3804.
Hemmati-Brivanlou, A., and Melton, D. A. (1994) Inhibition of activin receptor signaling promotes neuralization in Xenopus. Cell 77, 273–281.
New, H. V., Kavka, A. I., Smith, J. C., and Green, J. B. (1997) Differential effects on Xenopus development of interference with type IIA and type IIB activin receptors. Mech. Dev. 61, 175–186.
Ying, S.-Y., Zhang, Z., Furst, B., Batres, Y., Huang, G., and Li, G. (1997) Activins and activin receptors in cell growth. Proc. Soc. Exp. Biol. Med. 214, 114–122.
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Asashima, M., Ariizumi, T., Takahashi, S., Malacinski, G.M. (2000). Bioassays for Studying the Role of the Peptide Growth Factor Activin in Early Amphibian Embryogenesis. In: Tuan, R.S., Lo, C.W. (eds) Developmental Biology Protocols: Volume II. Methods in Molecular Biology™, vol 136. Humana Press. https://doi.org/10.1385/1-59259-065-9:15
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DOI: https://doi.org/10.1385/1-59259-065-9:15
Publisher Name: Humana Press
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Online ISBN: 978-1-59259-065-0
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