Retinoic acid (RA) and bone morphogenetic protein 4 (BMP4) restore the germline competence of in vitro cultured chicken blastodermal cells

2019 ◽  
Vol 55 (3) ◽  
pp. 169-176 ◽  
Author(s):  
Xiaochuan Tang ◽  
Jun Shi ◽  
Xiaolian Qin ◽  
Ning Xiao ◽  
Rongyang Li ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 4 ◽  
Morphogenetic Protein ◽  
Blastodermal Cells

scholarly journals Evidence for involvement of activin A and bone morphogenetic protein 4 in mammalian mesoderm and hematopoietic development.

1995 ◽  
Vol 15 (1) ◽  
pp. 141-151 ◽  
Author(s):  
B M Johansson ◽  
M V Wiles
Keyword(s):  
Growth Factor ◽  
Bone Morphogenetic Protein ◽  
Activin A ◽  
Bone Morphogenetic Protein 4 ◽  
Mesoderm Induction ◽  
Dependent Manner ◽  
Tgf Beta ◽  
Mouse Development ◽  
Morphogenetic Protein

Xenopus in vitro studies have implicated both transforming growth factor beta (TGF-beta) and fibroblast growth factor (FGF) families in mesoderm induction. Although members of both families are present during mouse mesoderm formation, there is little evidence for their functional role in mesoderm induction. We show that mouse embryonic stem cells, which resemble primitive ectoderm, can differentiate to mesoderm in vitro in a chemically defined medium (CDM) in the absence of fetal bovine serum. In CDM, this differentiation is responsive to TGF-beta family members in a concentration-dependent manner, with activin A mediating the formation of dorsoanterior-like mesoderm and bone morphogenetic protein 4 mediating the formation of ventral mesoderm, including hematopoietic precursors. These effects are not observed in CDM alone or when TGF-beta 1, -beta 2, or -beta 3, acid FGF, or basic FGF is added individually to CDM. In vivo, at day 6.5 of mouse development, activin beta A RNA is detectable in the decidua and bone morphogenetic protein 4 RNA is detectable in the egg cylinder. Together, our data strongly implicate the TGF-beta family in mammalian mesoderm development and hematopoietic cell formation.

scholarly journals Bone Morphogenetic Protein-4 Inhibits Corticotroph Tumor Cells: Involvement in the Retinoic Acid Inhibitory Action

Endocrinology ◽  
2006 ◽  
Vol 147 (1) ◽  
pp. 247-256 ◽  
Author(s):  
Damiana Giacomini ◽  
Marcelo Páez-Pereda ◽  
Marily Theodoropoulou ◽  
Marta Labeur ◽  
Damian Refojo ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Bone Morphogenetic Protein ◽  
Cushing’S Disease ◽  
Inhibitory Action ◽  
Molecular Mechanisms ◽  
Dominant Negative ◽  
Cushing's Disease ◽  
Bone Morphogenetic Protein 4 ◽  
Morphogenetic Protein

The molecular mechanisms governing the pathogenesis of ACTH-secreting pituitary adenomas are still obscure. Furthermore, the pharmacological treatment of these tumors is limited. In this study, we report that bone morphogenetic protein-4 (BMP-4) is expressed in the corticotrophs of human normal adenohypophysis and its expression is reduced in corticotrophinomas obtained from Cushing’s patients compared with the normal pituitary. BMP-4 treatment of AtT-20 mouse corticotrophinoma cells has an inhibitory effect on ACTH secretion and cell proliferation. AtT-20 cells stably transfected with a dominant-negative form of the BMP-4 signal cotransducer Smad-4 or the BMP-4 inhibitor noggin have increased tumorigenicity in nude mice, showing that BMP-4 has an inhibitory role on corticotroph tumorigenesis in vivo. Because the activation of the retinoic acid receptor has an inhibitory action on Cushing’s disease progression, we analyzed the putative interaction of these two pathways. Indeed, retinoic acid induces both BMP-4 transcription and expression and its antiproliferative action is blocked in Smad-4dn- and noggin-transfected Att-20 cells that do not respond to BMP-4. Therefore, retinoic acid induces BMP-4, which participates in the antiproliferative effects of retinoic acid. This new mechanism is a potential target for therapeutic approaches for Cushing’s disease.

scholarly journals Stimulation of Epithelial Sodium Channels in Endothelial Cells by Bone Morphogenetic Protein-4 Contributes to Salt-Sensitive Hypertension in Rats

2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Xu Yang ◽  
Na Niu ◽  
Chen Liang ◽  
Ming-Ming Wu ◽  
Liang-Liang Tang ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Bone Morphogenetic Protein ◽  
Salt Intake ◽  
High Salt ◽  
Bone Morphogenetic Protein 4 ◽  
Sodium Influx ◽  
Morphogenetic Protein ◽  
High Salt Intake ◽  
Stimulation Of

Previous studies have shown that high salt induces artery stiffness by causing endothelial dysfunction via increased sodium influx. We used our unique split-open artery technique combined with protein biochemistry and in vitro measurement of vascular tone to test a hypothesis that bone morphogenetic protein 4 (BMP4) mediates high salt-induced loss of vascular relaxation by stimulating the epithelial sodium channel (ENaC) in endothelial cells. The data show that high salt intake increased BMP4 both in endothelial cells and in the serum and that exogenous BMP4 stimulated ENaC in endothelial cells. The data also show that the stimulation is mediated by p38 mitogen-activated protein kinases (p38 MAPK) and serum and glucocorticoid-regulated kinase 1 (Sgk1)/neural precursor cell expressed developmentally downregulated gene 4-2 (Nedd4-2) (Sgk1/Nedd4-2). Furthermore, BMP4 decreased mesenteric artery relaxation in a benzamil-sensitive manner. These results suggest that high salt intake stimulates endothelial cells to express and release BMP4 and that the released BMP4 reduces artery relaxation by stimulating ENaC in endothelial cells. Therefore, stimulation of ENaC in endothelial cells by BMP4 may serve as another pathway to participate in the complex mechanism of salt-sensitive (SS) hypertension.

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