RESUMO
Of the TRIM/RBCC family proteins taking part in a variety of cellular processes, TRIM50 is a stomach-specific member with no defined biological function. Our biochemical data demonstrated that TRIM50 is specifically expressed in gastric parietal cells and is predominantly localized in the tubulovesicular and canalicular membranes. In cultured cells ectopically expressing GFP-TRIM50, confocal microscopic imaging revealed dynamic movement of TRIM50-associated vesicles in a phosphoinositide 3-kinase-dependent manner. A protein overlay assay detected preferential binding of the PRY-SPRY domain from the TRIM50 C-terminal region to phosphatidylinositol species, suggesting that TRIM50 is involved in vesicular dynamics by sensing the phosphorylated state of phosphoinositol lipids. Trim50 knock-out mice retained normal histology in the gastric mucosa but exhibited impaired secretion of gastric acid. In response to histamine, Trim50 knock-out parietal cells generated deranged canaliculi, swollen microvilli lacking actin filaments, and excess multilamellar membrane complexes. Therefore, TRIM50 seems to play an essential role in tubulovesicular dynamics, promoting the formation of sophisticated canaliculi and microvilli during acid secretion in parietal cells.
Assuntos
Ácidos/química , Mucosa Gástrica/metabolismo , Regulação da Expressão Gênica , Proteínas de Membrana/genética , Células Parietais Gástricas/citologia , Animais , Linfócitos/citologia , Proteínas de Membrana/metabolismo , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Knockout , Microvilosidades/metabolismo , Modelos Biológicos , Fosfatidilinositol 3-Quinases/metabolismo , Fosfatidilinositóis/química , Estrutura Terciária de Proteína , Transporte Proteico , Ratos , Ratos WistarRESUMO
Lithium-ion batteries lay the foundation for satisfying the fast-growing demand of portable electronics and electric vehicles. However, due to the complexity of material syntheses, high fabrication temperature condition, and toxic gas emission, high volume manufacturing of lithium-ion batteries is still challenging. Here, we propose a modified coprecipitation method to synthesize Li1.0Ni0.6Mn0.2Co0.2O2 (NMC622-MCP) as a cathode material in a simple, cost-effective, and environmentally friendly approach. We demonstrate that the proposed method can be operated in a lower temperature environment, with respect to the requirement of conventional synthesis methods. Furthermore, only CO2 gas is emitted during synthesis. We also employed first-principles simulations to evaluate the crystallinity of the synthesized materials via X-ray diffractometer patterns. During charge/discharge processes, the obtained cathode materials induce outstanding electrochemical performance with a maximum specific capacity of up to 206.9 mAh g-1 at 0.05 C and a retention capacity of 83.22% after 100 cycles. Thus, the simple, cost-effective, environmentally friendly, and highly electrochemical performance of the newly acquired material envisages the modified coprecipitation method as a promising tool to manufacture cathode materials for lithium-ion batteries.
RESUMO
Mitsugumin 56 (MG56), also known as the membrane-bound O-acyl-transferase family member hedgehog acyltransferase-like, was identified as a new sarcoplasmic reticulum component in striated muscle. Mg56-knockout mice grew normally for a week after birth, but shortly thereafter exhibited a suckling defect and died under starvation conditions. In the knockout skeletal muscle, regular contractile features were largely preserved, but sarcoplasmic reticulum elements swelled and further developed enormous vacuoles. In parallel, the unfolded protein response was severely activated in the knockout muscle, and presumably disrupted muscle development leading to the suckling failure. Therefore, MG56 seems essential for postnatal skeletal muscle maturation.