Human inhibin genes

Stewart, Andrew; Milborrow, Helen M.; Ring, Jennifer M.; Crowther, Carol; Forage, R G

doi:10.1016/0014-5793(86)81006-7

Cited by 87 publications

(7 citation statements)

References 17 publications

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“…1B), which is totally different from the composition of the human ␣ or ␤B subunits, since both have only two exons (20,21,34,42). When we sequenced and compared the 5Ј-flanking regions of both the human (Fig.…”

Section: Discussionmentioning

confidence: 99%

Human Activin βA Gene IDENTIFICATION OF NOVEL 5′

Tanimoto

Yoshida

Mita

et al. 1996

Journal of Biological Chemistry

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On the basis of cDNA cloning, primer extension, and transfection experiments, we identified a novel 5 exon of the human activin ␤A subunit gene, and found its enhancer and promoter regions as well as multiple transcription start sites. A series of deletion and mutation analyses of the enhancer sequences defined the 45-base pair core region (DR-1 core) containing two short elements with similarity to AP-1 (12-O-tetradecanoylphorbol-13-acetate response element; TRE) and CREB/ATF (cyclic AMP response element; CRE) binding sites, both of which were necessary for full enhancer activity. Gel shift and antibody supershift assays using DR-1 core region revealed the formation of two specific DNA-protein complexes, one of which could be partially dissociated by a competing oligonucleotide containing a single copy of the consensus TRE, but the other of which contained neither CREB/ATF nor AP-1 as major components. Although 12-O-tetradecanoylphorbol-13-acetate and cAMP induced the activin enhancer/promoterdriven CAT activity, such drug induction was obscured when either the TRE-or CRE-like elements were mutated in the native promoter context. Our results demonstrate that the promoter and enhancer regions identified here are essential for maintaining the efficient promoter activity of the human activin ␤A subunit gene.

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Section: Discussionmentioning

confidence: 99%

Human Activin βA Gene IDENTIFICATION OF NOVEL 5′

Tanimoto

Yoshida

Mita

et al. 1996

Journal of Biological Chemistry

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“…The structure of human inhibin was subsequently reported utilizing mRNA extracted from a patient with polycystic ovarian disease and a cDNA library produced and screened using fragments of porcine inhibin as a basis for making cDNA probes (Mason et al, 1986). The structure was independently confirmed using a human genomic DNA library screened with the bovine inhibin subunit probes (Stewart et al, 1986). The LY subunit cDNA was also isolated from human placenta using porcine inhibin c1 subunit probes (Mayo et al, 1986).…”

Section: Structural Analysismentioning

confidence: 99%

“…This material must be distinguished from non-gonadal proteins isolated from seminal plasma Seidah et al, 1984a) which share few physiological and no structural similarities and are not of gonadal origin. The structures of porcine (Mason et al, 1985) bovine human (Mason et al, 1986;Stewart et al, 1986) and rat (Shimasaki et al, 1987) inhibin have been deduced by molecular cloning techniques.…”

Section: Introductionmentioning

confidence: 99%

Advances in the Physiology of Inhibin and Inhibin‐related Peptides

McLachlan

Robertson

Kretser

et al. 1988

Clinical Endocrinology

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“…The PCR primers used (Fig. 2B) were designed to distinguish between the endogenous genomic activin type II receptor DNA, which contains introns 2 and 3 [Stewart et al, 1986], and the exogenous transgene of the receptor cDNA in the transfectants. As shown in Figure 2A, after PCR amplication with HActR2 ϩ /ActRm Ϫ primers, a 250-bp band was observed in samples prepared from wild-type K562 cells as well as from Act-RIIa transfected cells.…”

Section: Integration Of Actriia In Genome Of K562 Cellsmentioning

confidence: 99%

“…On the right panel, when the HActR1 ϩ /ActRm Ϫ primer set was used, a PCR product of 430 bp was found only in pRSV-ActRIIa transfected cells, but not in wild-type K562 cells. B: the locations of the PCR primers in cDNA and genomic DNA of type II activin receptor are shown with respect to introns 2 and 3 [Stewart et al, 1986].…”

Section: Effect Of Truncated Actriia On Induction Of Erythroid Differmentioning

confidence: 99%

Truncated activin type II receptor inhibits erythroid differentiation in K562 cells

Liu¹,

Shao²,

Yu³

2000

J. Cell. Biochem.

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Two receptor serine/threonine kinases (types I and II) have been identified as signaling transducing activin receptors. We studied the possibility of inhibiting activin A-dependent differentiation in K562 cells, using a dominant negative mutant of type II receptor. A vector was constructed expressing activin type II truncated receptor (ActRIIa) that lacks the cytoplasmic kinase domain. Since activin type I and II receptors form heteromeric complexes for signaling, the mutant receptors compete for binding to endogenous receptors, hence acting in a dominant negative fashion. K562 cells were stably transfected with ActRIIa, and independent clones were expanded. The truncated cDNA was integrated into the genome of the transfectants, as shown by polymerase chain reaction; and the surface expression of truncated receptors was shown by affinity cross-linking with (125)I-activin A. In wild-type K562 cells, activin A induced erythroid differentiation and cells started to express hemoglobins. In transfected cells expressing ActRIIa, the induction of erythroid differentiation was abrogated and less than 10% of cells were hemoglobin-containing cells after culture with activin A. Further transfection with wild-type type II receptors rescued the mutant phenotype of these transfectants, indicating that the effect of ActRIIa is dominant negative. In addition, phosphorylation of the cytoplasmic kinase domain of the type II receptor in vitro confirms the autophosphorylation of this portion of the receptor. Therefore, induction of erythroid differentiation in vitro is mediated through the cell surface activin receptor, and interference with this receptor signaling inhibits this process of differentiation in K562 cells.

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Human inhibin genes

Cited by 87 publications

References 17 publications

Human Activin βA Gene IDENTIFICATION OF NOVEL 5′

Human Activin βA Gene IDENTIFICATION OF NOVEL 5′

Advances in the Physiology of Inhibin and Inhibin‐related Peptides

Truncated activin type II receptor inhibits erythroid differentiation in K562 cells

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