Epidermal growth factor (EGF) promotes oocyte maturation in the zebrafish and its effect is mediated via the activin system. However, the mechanisms by which EGF regulates activin subunits in the follicle cells remain unknown. The present study demonstrated that EGF controlled expression of three activin subunits (inhbaa, inhbab and inhbb) in the follicle cells via diverse signaling pathways. The expression of inhbaa and inhbb was often co-regulated via similar pathways. Suppression of MAPK3/1, p38 MAPK, PKC and PKA each blocked or partially reduced the stimulatory effects of EGF on the expression of inhbaa and inhbb while up-regulated that of inhbab. Conversely, inhibition of PI3K did not have any effect on the expression of inhbaa and inhbb but significantly suppressed the stimulatory effect of EGF on inhbab. In summary, EGF action in the zebrafish ovary involves activin system and its regulation of activin subunits is mediated by diverse signaling pathways downstream of EGFR.
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http://dx.doi.org/10.1016/j.mce.2012.03.022 | DOI Listing |
Cancer Med
December 2024
Department of Pathology, College of Medicine, The Catholic University of Korea, Seoul, Republic of Korea.
Hereditas
November 2024
Department of Gastroenterology, First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310003, China.
Objective: Gastric cancer (GC) is characterized by its high malignancy and poor prognosis. However, the role of Inhibin subunit beta A (INHBA) in GC remains insufficiently understood. This study aims to comprehensively evaluate the clinical significance, biological roles, and possible mechanisms of INHBA in GC.
View Article and Find Full Text PDFCommun Biol
October 2024
Ecole Polytechnique Fédérale de Lausanne (EPFL) SV ISREC, Station 19, Lausanne, Switzerland.
The Activin-A precursor dimer can be cleaved by furin, but how this proteolytic maturation is regulated in vivo and how it facilitates access to signaling receptors is unclear. Here, analysis in a syngeneic melanoma grafting model shows that without furin coexpression, Activin-A failed to accelerate tumor growth, correlating with failure of one or both subunits to undergo cleavage in signal-sending cells, even though compensatory processing by host cells nonetheless sustained elevated circulating Activin-A levels. In reporter assays, furin-independent cleavage of one subunit enabled juxtacrine Activin-A signaling, whereas completion of proteolytic maturation by coexpressed furin or by recipient cells stimulated contact-independent activity, crosstalk with BMP receptors, and signal inhibition by follistatin.
View Article and Find Full Text PDFInt J Mol Med
November 2024
Department of Otolaryngology‑Head and Neck Surgery, Shandong Provincial ENT Hospital, Shandong University, Jinan, Shandong 250022, P.R. China.
The present study aimed to investigate the role and mechanism of inhibin βA (INHBA) in thyroid cancer (TC), and to determine its potential impact on the aggressive behavior of TC cells. The present study employed a comprehensive approach, using public databases, such as the Gene Expression Omnibus and The Cancer Genome Atlas, to identify and analyze the expression of INHBA in TC. Cell transfection, reverse transcription‑quantitative PCR, western blot analysis, immunohistochemistry and assays were conducted to investigate the functional effects of INHBA on TC.
View Article and Find Full Text PDFCancer Med
September 2024
Department of Pathology, University of Alabama at Birmingham Heersink School of Medicine, Birmingham, Alabama, USA.
Objective: The TGF-β superfamily member activin, a dimer of the gene products of INHBA and/or INHBB, has been implicated in immune cell maturation and recruitment, but its immune impact within epithelial ovarian cancer (EOC) is not well characterized. We sought to explore differences in activin (INHBA/ Inhibin-βA and INHBB/ Inhibin-βB) between malignant and ovarian tissues at the RNA and protein level and assess the relationship between activin and immune cells in EOC.
Methods: Publicly available RNA sequencing data were accessed from GEO (#GSE143897) with normalization and quantification performed via DESeq2.
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