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  • 11
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 32 (2000), S. 35-46 
    ISSN: 1573-6881
    Keywords: Ca2+ signaling ; inositol 1,4,5-trisphosphate receptor ; mitochondrial Ca2+ uptake ; mitochondrial Ca2+ efflux ; permeability transition ; apoptosis ; Bcl-2 family
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Cellular Ca2+ signals are crucial in the control of most physiological processes, cell injuryand programmed cell death; mitochondria play a pivotal role in the regulation of such cytosolicCa2+ ([Ca2+]c) signals. Mitochondria are endowed with multiple Ca2+ transport mechanismsby which they take up and release Ca2+ across their inner membrane. These transport processesfunction to regulate local and global [Ca2+]c, thereby regulating a number of Ca2+-sensitivecellular mechanisms. The permeability transition pore (PTP) forms the major Ca2+ effluxpathway from mitochondria. In addition, Ca2+ efflux from the mitochondrial matrix occursby the reversal of the uniporter and through the inner membrane Na+/Ca2+ exchanger. Duringcellular Ca2+ overload, mitochondria take up [Ca2+]c, which, in turn, induces opening of PTP,disruption of mitochondrial membrane potential (ΔΨm) and cell death. In apoptosis signaling,collapse of ΔΨ;m and cytochrome c release from mitochondria occur followed by activationof caspases, DNA fragmentation, and cell death. Translocation of Bax, an apoptotic signalingprotein from the cytosol to the mitochondrial membrane, is another step during thisapoptosis-signaling pathway. The role of permeability transition in the context of cell death in relationto Bcl-2 family of proteins is discussed.
    Type of Medium: Electronic Resource
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  • 12
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular neurobiology 11 (1991), S. 321-331 
    ISSN: 1573-6830
    Keywords: secretion ; oxytocin ; vasopressin ; neurosecretosomes ; ionomycin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. We studied the effects of extracellular sodium on the secretion of vasopressin (VP) and oxytocin (OT) and the efflux of45Ca from isolated, perfused nerve endings of the rat neurohypophysis (neurosecretosomes). 2. Upon removal of sodium from the perfusing medium, basal release of VP and OT increased by 3.95 ± 0.23- and 3.71 ± 0.22-fold, respectively, followed by a decline to about double the levels in normal (150 mM) sodium (P ⩽ 0.1). 3. Compared to neurosecretosomes perfused in normal (150 mM) sodium, omission of sodium from the medium augmented ionomycin-induced VP and OT secretion by 66 ± 5- and 20 ± 3-fold, respectively, and A23187-induced secretion was increased 1.3 ± 0.4- and 1.3 ± 0.1-fold (P ⩽ 0.01 for both ionophores). 4. The inhibition of ionomycin-induced secretion by sodium was concentration dependent (P ⩽ 0.01 for sodium ⩾ 5 mM); the IC50 was about 10 mM sodium for both hormones, and the Hill slope was close to -1. 5. The rate of45Ca efflux from neurosecretosomes showed 2.7 ± 0.1-fold stimulation upon increasing sodium from 4.5 to 150 mM (P ⩽ 0.01). 6. Our results suggest that sodium inhibits basal and stimulated secretion at the nerve terminal, possibly by reducing intraterminal calcium through sodium/calcium exchange.
    Type of Medium: Electronic Resource
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  • 13
    ISSN: 1573-6830
    Keywords: monoclonal antibodies ; neurophysin ; phylogenetic ; antibody crossreactivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Previously described mouse monoclonal antibodies against rat neurophysins [Ben-Barak, Y.,et al. (1985); Whitnall, M. H.,et al. (1985)] were studied here for their crossreactivities to neurophysins (NPs) from other vertebrate species. 2. Posterior pituitary extracts from various mammals (rat, mouse, cow, human) and lower vertebrates (frog, ratfish) were studied. 3. The monoclonal antibodies displayed several distinct patterns of crossreactivity to the various species, indicating that the epitopes which they recognized were different. PS 67 bound strongly to rat pituitary extract in solid-phase radioimmunoassay (RIA) but showed no cross-reactivity with extracts from any of the other species tested, including the mouse. PS 36 cross-reacted with mouse and frog extracts but showed almost no cross-reactivity with cow and none to ratfish extracts. PS 41 cross-reacted with mouse, cow, and frog extracts. PS 45 was the most cross-reactive antibody and recognized an antigen in extracts from mouse, cow, frog, and ratfish pituitaries. 4. Electrophoresis of proteins extracted from posterior pituitaries, followed by immunoblot staining with either PS 36 or PS 45, demonstrated that the NP-like molecules within each species are heterogeneous, i.e., more than two bands stained in each species. The frog NP stained by PS 45 was about twice the molecular weight of the mammalian NPs. 5. The possible valve of the PS 45 antibody for future molecular cloning experiments on the arginine vasotocin precursor in lower vertebrates is discussed.
    Type of Medium: Electronic Resource
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