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  • 1
    Online-Ressource
    Online-Ressource
    Cham :Springer International Publishing :
    Schlagwort(e): Medical genetics. ; Microbial genetics. ; Medical Genetics. ; Medical Genetics. ; Microbial Genetics.
    Beschreibung / Inhaltsverzeichnis: GADD45 in Stress Signaling, Cell Cycle Control, and Apoptosis -- GADD45 in Development and Cancer -- GADD45 in Normal Hematopoiesis and Leukemia -- GADD45 in DNA Methylation and DNA Repair -- GADD45 Proteins in Immunity -- GADD45 in Liver Function and Cancer -- GADD45 in Pre-Eclampsia -- GADD45 in Senescence -- GADD45 in Neuronal Development, Function, and Injury -- Index.
    Kurzfassung: This second edition is fully updated throughout and covers the emerging evidence that indicates that the Gadd45 family of proteins plays a unique and critical role as sensors of stress, including genotoxic, physiological, and oncogenic stress. It sheds light on the complex cellular stress response, encompassing myriad molecular pathways with a plethora of regulators and effectors. The GADD45 stress response genes encode small (18 kd) nuclear/cytoplasmic proteins. These genes are rapidly induced by a wide variety of endogenous and exogenous stress stimuli. Despite marked similarities, Gadd45 genes are regulated differentially and exhibit functional diversity. Gadd45 proteins respond to physiological and oncogenic stress, and are implicated in cell cycle arrest, DNA demethylation and repair, apoptosis, cell survival, genomic stability, and inflammation. The purpose of this book is to provide a comprehensive overview of the unique global role that Gadd45 proteins play as stress sensors and the molecular pathways involved.
    Materialart: Online-Ressource
    Seiten: IX, 153 p. 27 illus., 18 illus. in color. , online resource.
    Ausgabe: 2nd ed. 2022.
    ISBN: 9783030948047
    Serie: Advances in Experimental Medicine and Biology, 1360
    DDC: 616.042
    Sprache: Englisch
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 95 (1987), S. 105-112 
    ISSN: 1432-1424
    Schlagwort(e): Ca-activated K+ channel ; solubilization ; reconstitution ; thick ascending limb of Henle's loop ; calmodulin inhibitors ; trypsin ; pH
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary A barium-sensitive Ca-activated K+ channel in the luminal membrane of the tubule cells in thick ascending limb of Henle's loop is required for maintenance of the lumen positive transepithelial potential and may be important for regulation of NaCl reabsorption. In this paper we examine if the K+ channel can be solubilized and reconstituted into phospholipid vesicles with preservation of its native properties. The K+ channel in luminal plasma membrane vesicles can be quantitatively solubilized in CHAPS at a detergent/protein ratio of 3. For reconstitution, detergent is removed by passage over a column of Sephadex G 50 (coarse). K+-channel activity is assayed by measurement of86Rb+ uptake against a large opposing K+ gradient. The reconstituted K+ channel is activated by Ca2+ in the physiological range of concentration (K1/2∼2×10−7 m at pH 7.2) as found for the K+ channel in native plasma membrane vesicles and shows the same sensitivity to inhibitors (Ba2+, trifluoperazine, calmidazolium, quinidine) and to protons. Reconstitution of the K+ channel into phospholipid vesicles with full preservation of its native properties is an essential step towards isolation and purification of the K+-channel protein. Titration with Ca2+ shows that most of the active K+ channels in reconstituted vesicles have their cytoplasmic aspect facing outward in contrast to the orientation in plasma membrane vesicles, which requires also addition of Ca2+ ionophore in order to observe Ca2+ stimulation. The reconstituted K+ channel is highly sensitive to tryptic digestion. Brief digestion leads to activation of the K+ channel in absence of Ca2+, to the level of activity seen with saturating concentrations of Ca2+. This tryptic split is located in a cytoplasmic aspect of the K+ channel that appears to be involved in opening and closing the K+ channel in response to Ca2+ binding.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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