Assuntos
Canais de Cálcio/metabolismo , Proteínas Mitocondriais/metabolismo , Complexos Multiproteicos/metabolismo , Canais de Cálcio/química , Canais de Cálcio/genética , Células HEK293 , Humanos , Proteínas Mitocondriais/química , Proteínas Mitocondriais/genética , Complexos Multiproteicos/química , Complexos Multiproteicos/genéticaRESUMO
MS4A4A regulates the expression of arginase 1 in macrophages under IL4 stimulation. Also, MS4A4A regulates eosinophil infiltration during lung allergic inflammation induced by intranasal administration of house dust mite.
Assuntos
Arginase/metabolismo , Eosinófilos/imunologia , Hipersensibilidade/imunologia , Pulmão/imunologia , Macrófagos/fisiologia , Proteínas de Membrana/metabolismo , Pneumonia/imunologia , Animais , Antígenos de Dermatophagoides/imunologia , Arginase/genética , Diferenciação Celular , Ativação de Macrófagos , Proteínas de Membrana/genética , Camundongos , Camundongos Knockout , Pyroglyphidae , Regulação para CimaRESUMO
Stress resistance and growth are important aspects to consider when engineering Oenococcus oeni strains for winemaking. We identified 3 previously unreported structural phenomena in the cell ontogeny of O. oeni sampled in northern China. We show that budding and binary fission (BBF) occur simultaneously in the growth process; that a novel 'pomegranate-shaped structure' (PSS) occurs mainly in the stationary and death phases; and that symbiosis and cyclical phenomena (SCP) occur throughout the various cell growth phases. These observations add to the current knowledge of the cell growth process of O. oeni. BBF, PSS, and SCP sufficiently describe the characteristics of the cellular ontogeny of O. oeni. We highlight a newly identified structure that explains the complex cell growth process. These findings will help understand the growth and development of O. oeni, supplementing the knowledge base of the established phases and providing new perspectives into its complex growth patterns.
Assuntos
Divisão Celular , Oenococcus/fisiologia , Oenococcus/ultraestrutura , China , SimbioseRESUMO
B cells that express the isotype-switched IgG-B cell receptor (IgG-BCR) are one of the driving forces for antibody memory. To allow for a rapid memory IgG antibody response, IgG-BCR evolved into a highly effective signalling machine. Here, we report that the positively charged cytoplasmic domain of mIgG (mIgG-tail) specifically interacts with negatively charged acidic phospholipids. The key immunoglobulin tail tyrosine (ITT) in mIgG-tail is thus sequestered in the membrane hydrophobic core in quiescent B cells. Pre-disruption of such interaction leads to excessive recruitment of BCRs and inflated BCR signalling upon antigen stimulation, resulting in hyperproliferation of primary B cells. Physiologically, membrane-sequestered mIgG-tail can be released by antigen engagement or Ca(2+) mobilization in the initiation of B cell activation. Our studies suggest a novel regulatory mechanism for how dynamic association of mIgG-tail with acidic phospholipids governs the enhanced activation of IgG-BCR.
