Follistatin inhibits the mesoderm-inducing activity of activin A and the vegetalizing factor from chicken embryo

Asashima, Makoto; Nakano, Hiroshi; Uchiyama, Hideho; Sugino, Hiromu; Nakamura, Takanori; Eto, Yuzuru; Ejima, Daisuke; Davids, Michael; Plessow, Sigrun; Cichocka, Ivona; Kinoshita, Kentaro

doi:10.1007/bf02457635

Cited by 60 publications

(17 citation statements)

References 35 publications

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“…The cDNA sequence of each subunit and follistatin was identical to the corresponding region of rat mhibm. actlvin [2] and folhstatin [14]. respectively.…”

Section: Rt-pcr and Sequencrngmentioning

confidence: 99%

Expression of α,βA and βB subunits of inhibin or activin and follistatin in rat pancreatic islets

et al. 1993

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We first detected the mRNA expression of follistatin and three subunits of inhibimactivin m rat pancreatic islets by reverse transcription-polymerase chain reaction (RT-PCR). Immunohistochemistry using anti-follistatin serum (against residues 123-l 34) revealed that follistatin was localized only in insulin-producing B cells. Although the PA subunit was detectable in the islets, the immunostainable cell types were completely different with two PA antisera, i.e. anti-/IA (1-lO)-Tyr stained B cells, while anti-PA (87-99) stained glucagon-producing A cells. This inconsistent immunoreactivity was probably related to follistatin binding top subunits of inhibimactivin. This study indicates that follistatin and inhibimactivin in the islet serve as paracrine or autocrine modulators in the endocrine pancreas.

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“…The cDNA sequence of each subunit and follistatin was identical to the corresponding region of rat mhibm. actlvin [2] and folhstatin [14]. respectively.…”

Section: Rt-pcr and Sequencrngmentioning

confidence: 99%

Expression of α,βA and βB subunits of inhibin or activin and follistatin in rat pancreatic islets

et al. 1993

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“…Follistatin binds to both inhibin and activin through the common b subunit (18). Neutralization of activin's activity by follistatin is proven in various systems, such as the stimulation of FSH secretion in cultured pituitary cells (8), induction of mesoderm tissue formation in Xenopus oocytes (19), and differentiation of rat granulosa cells (20). These results indicated that follistatin is a functional regulator of activin's activity.…”

Section: Introductionmentioning

confidence: 99%

Follistatin-like immunoreactivity in the cytoplasm and nucleus of spermatogenic cells in the rat

Ogawa

Hashimoto²,

Kurohmaru³

et al. 1997

European Journal of Endocrinology

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Immunohistochemistry using an antiserum raised against the synthetic follistatin peptide (residues 123-134) was used, in the present study, to detect the stage-specific appearance of immunoreactive follistatin in the rat testis. Follistatin immunoreactivity was not found in Sertoli and Leydig cells, while it was clearly detected in spermatogenic cells. Follistatin-like immunoreactivity was detected in the cytoplasm and nucleus of late pachytene spermatocytes. Although the reaction in the cytoplasm disappeared after meiosis, it continued to be intense in the nucleus from pachytene spermatocytes to round spermatids. This finding indicated that follistatin or its closely related peptide produced in late pachytene spermatocytes migrates from the cytoplasm to the nucleus. We subjected rat testis homogenate to affinity chromatography on a sulfate-cellulofine and anti-follistatin Cys (123-134)-Affi-Gel Hz column followed by reverse-phase HPLC and analyzed the resulting fractions by Western blotting using follistatin antiserum. Three major bands at 57, 45 and 39 kDa or four bands at 52, 44, 39 and 34 kDa were detected in crude preparations from rat testis homogenate, under reducing or non-reducing SDS-PAGE respectively. The protein from rat testis, which was recognized by antifollistatin (123-134) antiserum, exhibited a characteristic pattern for follistatin on SDS-PAGE, i.e. slower migration under reducing conditions than under non-reducing conditions, suggesting that it was follistatin or its closely related protein. Follistatin or its closely related protein may be a stagespecific modulator of spermatogenesis. Since follistatin-like immunoreactivity was not found in oocytes in any stage of development from embryonic to adult rats, it may act in an event specific to spermatogenesis, such as nuclear condensation.

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“…The injected cells express chordin mRNA (Rebbert & David 1997). Zygotic transcripts of cerberus accumulate in the Xenopus embryo 1 h later than those of chordin (Bouwmeester et al 1996) (Glinka et al 1998 (Asashima et al 1991;Grunz 1996).…”

Section: Partial Purification Of a Neuralizing Factor From The Cytosolmentioning

confidence: 99%

Neural inducing factors from Xenopus laevis eggs and embryos

Tiedemann

1999

Dev Growth Differ

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Follistatin inhibits the mesoderm-inducing activity of activin A and the vegetalizing factor from chicken embryo

Cited by 60 publications

References 35 publications

Expression of α,βA and βB subunits of inhibin or activin and follistatin in rat pancreatic islets

Expression of α,βA and βB subunits of inhibin or activin and follistatin in rat pancreatic islets

Follistatin-like immunoreactivity in the cytoplasm and nucleus of spermatogenic cells in the rat

Neural inducing factors from Xenopus laevis eggs and embryos

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