Improving the anti-carbon deposition and anti-sintering ability under the premise of maintaining high catalytic activity is the core issue of Ni-based catalysts applied in CO methanation reactions. ...To address this issue, a La0.75A0.25NiO3/SiO2 (A = Ce, Sr, Sm, and Ca) catalyst is prepared via a citric acid complexation method. XRD results show that the substituted elements (Sr, Sm, and Ca) enter the LaNiO3 lattice and partially replace the A-site element La. The reduced Ni0 is beneficial to improve the medium temperature activity of the catalyst. The substitution of different elements produces different electronic effects that significantly affect the size of the Ni particles and the interaction between Ni and La2O3. The catalyst with doped Ca2+ as the A-site substituted element demonstrates better adsorption, storage, and migration capabilities for oxygen due to the lattice distortion that easily produces oxygen vacancies. Catalysts doped with Sr, Sm, and Ca as the A-site substituted element produce La2O2CO3 after the reactions, which plays a role in eliminating carbon deposits.
Improving the anti-carbon deposition and anti-sintering ability under the premise of maintaining high catalytic activity is the core issue of Ni-based catalysts applied in CO methanation reactions. ...To address this issue, a La
0.75
A
0.25
NiO
3
/SiO
2
(A = Ce, Sr, Sm, and Ca) catalyst is prepared via a citric acid complexation method. XRD results show that the substituted elements (Sr, Sm, and Ca) enter the LaNiO
3
lattice and partially replace the A-site element La. The reduced Ni
0
is beneficial to improve the medium temperature activity of the catalyst. The substitution of different elements produces different electronic effects that significantly affect the size of the Ni particles and the interaction between Ni and La
2
O
3
. The catalyst with doped Ca
2+
as the A-site substituted element demonstrates better adsorption, storage, and migration capabilities for oxygen due to the lattice distortion that easily produces oxygen vacancies. Catalysts doped with Sr, Sm, and Ca as the A-site substituted element produce La
2
O
2
CO
3
after the reactions, which plays a role in eliminating carbon deposits.
The auto-phosphorylation of murine receptor-interacting protein 3 (Rip3) on Thr 231 and Ser 232 in the necrosome is required to trigger necroptosis. However, how Rip3 phosphorylation is regulated is ...still largely unknown. Here we identified protein phosphatase 1B (Ppm1b) as a Rip3 phosphatase and found that Ppm1b restricts necroptosis in two settings: spontaneous necroptosis caused by Rip3 auto-phosphorylation in resting cells, and tumour necrosis factor-α (TNF)-induced necroptosis in cultured cells. We revealed that Ppm1b selectively suppresses necroptosis through the dephosphorylation of Rip3, which then prevents the recruitment of mixed lineage kinase domain-like protein (Mlkl) to the necrosome. We further showed that Ppm1b deficiency (Ppm1b(d/d)) in mice enhanced TNF-induced death in a Rip3-dependent manner, and the role of Ppm1b in inhibiting necroptosis was evidenced by elevated Rip3 phosphorylation and tissue damage in the caecum of TNF-treated Ppm1b(d/d) mice. These data indicate that Ppm1b negatively regulates necroptosis through dephosphorylating Rip3 in vitro and in vivo.
Smad7 is a negative feedback product of TGF-β superfamily signaling and fine tunes a plethora of pleiotropic responses induced by TGF-β ligands. However, its noncanonical functions independent of ...TGF-β signaling remain to be elucidated. Here, we show that Smad7 activates signal transducers and activators of transcription 3 (STAT3) signaling in maintaining mouse embryonic stem cell pluripotency in a manner independent of the TGF-β receptors, yet dependent on the leukemia inhibitory factor (LIF) coreceptor glycoprotein 130 (gp130). Smad7 directly binds to the intracellular domain of gp130 and disrupts the SHP2–gp130 or SOCS3–gp130 complex, thereby amplifying STAT3 activation. Consequently, Smad7 facilitates LIF-mediated self-renewal of mouse ESCs and is also critical for induced pluripotent stem cell reprogramming. This finding illustrates an uncovered role of the Smad7–STAT3 interplay in maintaining cell pluripotency and also implicates a mechanism involving Smad7 underlying cytokine-dependent regulation of cancer and inflammation.
Loss of TGF-β tumour suppressive response is a hallmark of human cancers. As a central player in TGF-β signal transduction, SMAD4 (also known as DPC4) is frequently mutated or deleted in ...gastrointestinal and pancreatic cancer. However, such genetic alterations are rare in most cancer types and the underlying mechanism for TGF-β resistance is not understood. Here we describe a mechanism of TGF-β resistance in ALK-positive tumours, including lymphoma, lung cancer and neuroblastoma. We demonstrate that, in ALK-positive tumours, ALK directly phosphorylates SMAD4 at Tyr 95. Phosphorylated SMAD4 is unable to bind to DNA and fails to elicit TGF-β gene responses and tumour suppressing responses. Chemical or genetic interference of the oncogenic ALK restores TGF-β responses in ALK-positive tumour cells. These findings reveal that SMAD4 is tyrosine-phosphorylated by an oncogenic tyrosine kinase during tumorigenesis. This suggests a mechanism by which SMAD4 is inactivated in cancers and provides guidance for targeted therapies in ALK-positive cancers.
Bone morphogenetic proteins (BMPs) play vital roles in regulating stem cell maintenance and differentiation. BMPs can induce osteogenesis and inhibit myogenesis of mesenchymal stem cells. Canonical ...BMP signaling is stringently controlled through reversible phosphorylation and nucleocytoplasmic shuttling of Smad1, Smad5, and Smad8 (Smad1/5/8). However, how the nuclear export of Smad1/5/8 is regulated remains unclear. Here we report that the Ran-binding protein RanBP3L acts as a nuclear export factor for Smad1/5/8. RanBP3L directly recognizes dephosphorylated Smad1/5/8 and mediates their nuclear export in a Ran-dependent manner. Increased expression of RanBP3L blocks BMP-induced osteogenesis of mouse bone marrow-derived mesenchymal stem cells and promotes myogenic induction of C2C12 mouse myoblasts, whereas depletion of RanBP3L expression enhances BMP-dependent stem cell differentiation activity and transcriptional responses. In conclusion, our results demonstrate that RanBP3L, as a nuclear exporter for BMP-specific Smads, plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation.
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