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At least 937 records · Page 52Linked to original sources
PubMed1989

Pentylenetetrazole-induced seizure activity produces an increased release of calcium from endoplasmic reticulum by mediating cyclic AMP-dependent protein phosphorylation in rat cerebral cortex.

1. To determine the involvement of the convulsant agent pentylenetetrazole (PTZ) in intracellular calcium release in neurons, its effect on stored calcium in the endoplasmic reticulum of rat cortical neurons was tested. 2. Intraperitoneal injection of PTZ caused marked release of calcium from the endoplasmic reticulum which was similar to that observed when cortical slices were incubated with this convulsant. 3. Superfusion of dibutyryl cAMP and isobutylmethylxanthine to the cortical slices mimicked PTZ-induced calcium release from this reservoir. A similar effect was observed under depolarizing conditions brought about by either an elevation of extracellular K+ concentration or addition of veratridine. 4. Isoquinolinesulfonamide, a protein kinase inhibitor, reduced PTZ-stimulatory effect of calcium release and blocked the cAMP-induced calcium release. 5. Intracellular cAMP level was enhanced at about 3-fold by both intraperitoneal injection of PTZ and its superfusion. 6. These findings are taken to suggest that PTZ may release stored calcium in the endoplasmic reticulum by mediating a cAMP-dependent protein phosphorylation in cortical neurons.

Animals↗
PubMed1990

Calcium uptake activity of cardiac sarcoplasmic reticulum in myo-inositol-treated diabetic rats.

1. Cardiac function of STZ-diabetic rats has been shown to be partially improved by myo-inositol treatment. We studied the effect of myo-inositol on Ca2(+)-uptake activity in sarcoplasmic reticulum in diabetic animals. 2. Cardiac sarcoplasmic reticulum Ca2(+)-uptake activity was significantly depressed in 8-week diabetic rats. 3. Myo-inositol treatment could not improve Ca2(+)-uptake activity in diabetic rats. 4. The data suggest that the cardiac dysfunction in diabetic rats is due to factors other than the decreased Ca2(+)-uptake activity in sarcoplasmic reticulum.

Adenosine Triphosphate↗
PubMed1984

Poststimulatory endocytosis, microvesicle repopulation and changes in smooth endoplasmic reticulum in nerve endings of the median eminence superfused in vitro.

Mediobasal hypothalami of adult rats were superfused in vitro. A single 5 min pulse of 60 mM KCl-containing medium was infused, followed by either 15, 30, 45, 60 or 75 min superfusions with standard medium. In some experiments, 5 or 10% dextran was added followed by a 15 min recovery. Morphologically, two recovery phases were recognized. The early phase (15-30 min) was characterized by two features: (1) A clear-cut increase in the quantity of large, pleomorphic vacuoles occupying the axoplasm of nerve endings; these vacuoles were observed to be connected to caveolae of the same diameter in the axolemma and they were either coated or uncoated. (2) Progressive increase in the quantity of microvesicles (synaptic vesicles) from an initial depleted state. The vacuoles were found to contain dextran aggregates. Microvesicle-like protrusions bulged from the membrane of vacuoles. The late phase, from 45 min poststimulation onward, was typically identified after the appearance of tubules of smooth endoplasmic reticulum at the most distal segments of the nerve terminals. During this period, large vacuoles tended to decrease in quantity. Granular vesicles remained scant during the entire observation period. Images suggesting formation of microvesicles from tubules of smooth endoplasmic reticulum were observed. These results open the possibility that endocytosis of patches of membranes forming large vacuoles be an important mechanism for retrieving the membranes belonging to microvesicles and granular vesicles. Some of these large vacuoles may contribute to the early regeneration of microvesicles. More microvesicles could later be produced from the smooth endoplasmic reticulum.

Animals↗
PubMed1991

Localization of an endoplasmic reticulum calcium ATPase mRNA in rat brain by in situ hybridization.

SERCA-2 is an endoplasmic reticulum Ca2+ ATPase present in brain [Gunteski-Hamblin A.-M. et al. (1988) J. biol. Chem. 263, 15032-15040]. We sought to map the distribution of this pump in the rat brain and investigate its relationship to Ca2+ uptake by brain endoplasmic reticulum. Using in situ hybridization and Northern blots with antisense oligonucleotide probes, we found that SERCA-2 is concentrated most densely in the cerebellum, especially in Purkinje cells, and in the hippocampus, with heavy labeling also in cortex, thalamus, pontine nuclei and the mitral cell layer of the olfactory bulb. 45Ca2+ uptake displayed a similar pattern with heaviest accumulation in cerebellum, hippocampus, cortex, thalamus and olfactory bulb. In corpus striatum and substantia nigra, relative 45Ca2+ accumulation was greater than SERCA-2 mRNA. Thus, SERCA-2 appears to be involved in Ca2+ uptake into endoplasmic reticulum in brain for release by inositol 1,4,5-trisphosphate and other agents.

Animals↗
PubMed1986

Effect of mononuclear cell factors on calcium transport in sarcoplasmic reticulum vesicles.

The effect of supernatants from cultures of mitogen-stimulated human mononuclear cells on calcium transport by sarcoplasmic reticulum was examined. Calcium transport was assayed by measuring the time course of calcium accumulation by sarcoplasmic reticulum incubated with supernatants from stimulated mononuclear cells was 20% less than that by vesicles exposed to control supernatants (P less than 0.001). In contrast, no difference in calcium-dependent ATPase activity was noted between vesicles incubated with either active or control supernatants. The results suggest that mononuclear cell factors disturb calcium transport in sarcoplasmic reticulum membrane.

Animals↗
PubMed1989

G-protein dependent potentiation of calcium release from sarcoplasmic reticulum of skeletal muscle.

Skinned fibre experiments were conducted to determine if guanine nucleotide-binding proteins play a role in excitation-contraction coupling of skeletal muscle. By itself, the GTP-gamma S, a non hydrolysable GTP analogue was unable to induce calcium release from the sarcoplasmic reticulum, even at concentrations as high as 500 microM. However, calcium- or caffeine-induced calcium releases were enhanced by GTP-gamma S in micromolar concentrations. This response was blocked by GDP-beta S or Pertussis toxin. 32P-ADP-ribosylation catalysed by Pertussis toxin, radiolabelled G-protein alpha subunits in the range of 40 kDa on membrane subcellular fractions of rat skeletal muscle. Using Western blot analysis with antibodies raised against the bovine transducin, G-proteins were identified in frog and rat skeletal muscle subcellular fractions. In most of the muscle fractions (plasma membrane, T-tubules, triads, sarcoplasmic reticulum), the anti-beta subunit antibodies recognized a 36 kDa protein which comigrated with transducin beta subunit. It appears therefore that some of the G-proteins identified by ADP-ribosylation or immunostaining in several subcellular fractions from skeletal muscle, are implicated in the modulation of calcium release from sarcoplasmic reticulum. These results suggest that a Pertussis toxin sensitive G-protein is present at the loci of E-C coupling, and that it serves to regulate the calcium release.

Adenosine Diphosphate Ribose↗
PubMed2006

Opposite effects of endotoxin on mitochondrial and endoplasmic reticulum functions.

In this study, we determined functional integrity and reactive oxygen species generation in mitochondria and endoplasmic reticulum in liver of rats subjected to endotoxic shock to clarify whether intracellular reactive oxygen species (ROS) destabilize cellular integrity causing necrosis in rats challenged with lipopolysaccharide (LPS). LPS caused drastically increased plasma levels of alanine aminotransferase, suggesting damage to plasma membranes of liver cells. Liver necrosis was confirmed by histological examination. LPS induced a significant increase in ROS production in rat liver mitochondria (RLM), but did not impair mitochondrial function. In contrast to mitochondria, enzymatic activity and ROS production of cytochrome P450 were lower in microsomal fraction obtained from LPS-treated animals, suggesting the dysfunction of endoplasmic reticulum. Protein patterns obtained from RLM by two-dimensional electrophoresis showed significant upregulation of mitochondrial superoxide dismutase by LPS. We hypothesize that upregulation of this enzyme protects mitochondria against mitochondrial ROS, but does not protect other cellular compartments such as endoplasmic reticulum and plasma membrane causing necrosis.

Animals↗
PubMed2004

The endoplasmic reticulum-related events in S-nitrosoglutathione-induced neurotoxicity in cerebellar granule cells.

Nitric oxide (NO)-induced neurotoxicities are involved in the pathogenesis of several neurodegenerative disorders featured by misfolded proteins. However, the details remain to be investigated. In the present work, we focus on the study of some endoplasmic reticulum-related events in S-nitrosoglutathione (GSNO)-induced neurotoxicity in cerebellar granule cells (CGCs) and we demonstrated that: (1) GSNO caused sustained elevation of intracellular calcium; (2) This calcium elevation resulted partially from the depletion of endoplasmic reticulum (ER) calcium stores; (3) There was ER stress which was indicated by the incomplete splicing of X-box binding protein (XBP-1) mRNA by 8-polysialyltransferase (Pst1); (4) GSNO upregulated the expression of the proapoptotic growth arrest and DNA damage-inducible gene (Gadd153) and caused the depletion of intracellular glutathione (GSH) pools. At the same time, GSNO downregulated the expression of the antiapoptotic gene Sarco/endoplasmic reticulum calcium-ATPase (SERCA2b) in parallel with the downregulation of the antiapoptotic ER chaperones-glucose-regulated protein genes (Grp78 and Grp94). These effects indicate that ER is one of the NO targets in GSNO-induced neurotoxicity in cerebellar granule cells besides mitochondria.

Animals↗
PubMed2004

Cloning and characterization of a novel endoplasmic reticulum localized G-patch domain protein, IER3IP1.

The endoplasmic reticulum (ER) is the site of protein synthesis, folding, post-translational modifications and export. The ER membrane and its lumen contain various chaperones and enzymes that are involved in every aspect of the ER function. In this report, we identified a novel endoplasmic reticulum protein (immediate early response 3 interacting protein 1, IER3IP1) during the large-scale partial sequencing of a liver cDNA library. The full-length 1304 bp IER3IP1 cDNA has a predicted open reading frame (ORF), which encodes an 82 amino-acid protein possessing a G-patch domain. This domain is found in several RNA associated proteins and has been suggested to be involved in RNA binding. IER3IP1 gene was mapped to the chromosome 18q12 by radiation hybrid analysis. In northern blot hybridization, it was shown that IER3IP1 gene has a high expression in heart, skeletal muscle and kidney, a moderate expression in liver and brain and a low expression in placenta, lung and peripheral blood leukocyte. With the presence of transmembrane domain at the C-terminal, the translated IER3IP1 protein was localized to endoplasmic reticulum of HepG2 cells and was confirmed by co-localization with ER specific marker.

Amino Acid Sequence↗
PubMed2004

About the morphological relationships of the sarcoplasmic reticulum in the sole plate area of the frog.

In the present investigation the sole plate area of motor end plates of the frog is ultrastructurally examined with different postfixation methods. We concentrated in this case on the proof of the smooth and rough sarcoplasmic reticulum of the sole plate. The relations of the smooth and rough sarcoplasmic reticulum to subsynaptic folds and the local T-system and its connections to diads and triads in the sole plate area are represented. The morphological differences between mammal and frog are pointed out. The possible functions of the sarcoplasmic reticulum in the myofibril-free sarcoplasm are discussed.

Animals↗
PubMed2003

The membrane-interactive tail of cytochrome b(5) can function as a stop-transfer sequence in concert with a signal sequence to give inversion of protein topology in the endoplasmic reticulum.

Sequence analyses of the C-terminal membrane intercalative region of the rat cytochrome b(5) indicated that this domain has, in addition to a signal sequence, a combined element of the classic stop-transfer sequence typically found in a variety of transmembrane proteins. Such bitopic protein arrangements arise by tandem but topogenically displaced activities of cleavable/noncleavable signal and stop-transfer sequences. A fusion precursor comprising an N-terminally linked prokaryotic signal sequence and the full-length of mammalian cytochrome b(5), including its C-terminal membrane insertion sequence, was engineered to investigate the outcome of this combination of signals on the targeting and topology of the cytochrome b(5) in the endoplasmic reticulum membrane. Precytochrome b(5) was cotranslationally translocated across the endoplasmic reticulum membrane. The signal-processed cytochrome b(5) was integrally anchored in the membrane with the globular domain facing the lumen. Thus, the topology of the signal sequence-directed cytochrome b(5) in the microsomal vesicle was reversed with respect to that of the native form. Posttranslational incubation of the precytochrome b(5) with microsomes resulted in a "loose" incorporation of the unprocessed form onto the surface of the vesicle. Our findings suggest that the membrane-insertion sequence of cytochrome b(5) has a functional stop-transfer sequence. We discuss the implications of these findings with respect to selective targeting of cytochrome b(5) to the endoplasmic reticulum membrane in the view that signal and stop-transfer sequences are often interchangeable or combined for topogenic functions.

Amino Acid Sequence↗
PubMed1997

Histidine-containing dipeptides as endogenous regulators of the activity of sarcoplasmic reticulum Ca-release channels.

It is shown that histidine-containing dipeptide carnosine (beta-alanyl-L-histidine), which is present in skeletal muscles in millimolar concentrations, decreases the rate of Ca2+ accumulation by the heavy fraction of sarcoplasmic reticulum from rabbit skeletal muscles. This effect results from the ability of carnosine to induce a rapid Ca2+ release from the heavy sarcoplasmic reticulum vesicles via activation of the ruthenium red-sensitive Ca-channels. The effect of carnosine is dose-dependent that indicates the presence of saturable site(s) for carnosine in the molecules of Ca-channels. The C0.5 value carnosine (the concentration that induces the half-maximal Ca2+ release) is 8.7 mM. The 1 N-methylated derivative of carnosine, i.e., anserine, also induces a rapid Ca2+ release with the half-maximal effect at 2.7 mM. Conversely, neither histidine nor beta-alanine (both separately and in the mixture) cause Ca2+ release. In addition, carnosine increases the sensitivity of Ca-channels to their well-known activators (caffeine, AMP, and Ca2+) and decreases inhibitory effect of low concentrations of Mg2+. It is concluded that carnosine as a component of skeletal muscles can be an endogenous regulator of the sarcoplasmic reticulum Ca-channel activity.

Adenosine Monophosphate↗
PubMed1997

Rotational mobility of Ca2+-ATPase of sarcoplasmic reticulum in viscous media.

The rotational diffusion of Ca2(+)-ATPase [Ca2+,Mg2(+)-activated ATP phosphohydrolase E.C. 3.6.1.38] was studied in native sarcoplasmic reticulum membrane by saturation transfer ESR spectroscopy after covalent labelling of intramembranous sulfhydryl groups with nitroxyl derivative of maleimide (5-MSL) as a function of sucrose and glycerol in the suspending medium. The relative enzymatic activity of sarcoplasmic reticulum was followed by increasing the viscosity of the aqueous phase. The ATP hydrolysing activity of the enzyme decreased differently on adding sucrose and glycerol. In the case of sucrose the reciprocal of power dependence of viscosity was observed, whereas for glycerol an exponential decay law was obtained, indicating solvent-protein interaction. On increasing the viscosity of the aqueous phase by either sucrose or glycerol, no changes were observed in the intramembranous viscosity as measured using intercalated spin-labelled stearic acid (16-SASL). The effective rotational correlation time of the protein was measured, as a mobility parameter, using saturation transfer ESR spectroscopy and found to be increased linearly with the viscosity of the sucrose containing medium and for the extramembranous size a height of 6.8 nm was obtained, indicating that approx. 82% of the volume of Ca2(+)-ATPase protein is external to the sarcoplasmic reticulum. The addition of glycerol probably promoted protein-protein interaction, as indicated by the larger changes in rotational diffusion and non-linear viscosity dependence.

Animals↗
PubMed2002

Ca(2+) signals in Pmr1-GFP-expressing COS-1 cells with functional endoplasmic reticulum.

We studied the role of the Pmr1-containing Ca(2+) store in COS-1 cells endowed with a functional endoplasmic reticulum. Transfected cells could be recognized by using a green-fluorescent-protein (GFP)-tagged form of Pmr1. Pmr1-GFP fluorescence showed a typical juxtanuclear Golgi-like distribution. Pmr1-GFP-containing cells with functional endoplasmic reticulum responded to 100 microM ATP with baseline Ca(2+) spiking, while non-transfected cells produced an initial Ca(2+) peak followed by a long-lasting plateau. The Ca(2+) signal often appeared after a long latency in Pmr1-GFP-expressing cells. ATP-stimulated Pmr1-GFP-expressing cells with functional endoplasmic reticulum responded after a latency period to extracellular Ca(2+) with a regenerative Ca(2+) signal, while non-transfected control cells responded with an immediate slow rise in free cytosolic Ca(2+) concentration. These results demonstrate the importance of the Pmr1-containing Ca(2+) store in generating or modifying cellular Ca(2+) signals.

Adenosine Triphosphate↗
PubMed2004

Mechanism of calmodulin inhibition of cardiac sarcoplasmic reticulum Ca2+ release channel (ryanodine receptor).

The functional effects of calmodulin (CaM) on single cardiac sarcoplasmic reticulum Ca(2+) release channels (ryanodine receptors) (RyR2s) were determined in the presence of two endogenous channel effectors, MgATP and reduced glutathione, using the planar lipid bilayer method. Single-channel activities, number of events, and open and close times were determined at varying cytosolic Ca(2+) concentrations. CaM reduced channel open probability at <10 micro M Ca(2+) by decreasing channel events and mean open times and increasing mean close times. At >10 micro M Ca(2+), CaM was less effective in inhibiting RyR2. CaM decreased mean open times but increased channel events, without significantly affecting mean close times. A series of voltage pulses was applied to the bilayer from +50 to -50 mV and from -50 mV to +50 mV to rapidly increase and decrease open channel-mediated sarcoplasmic reticulum lumenal to cytosolic Ca(2+) fluxes. CaM decreased the duration of the open events after the voltage switch from -50 mV to +50 mV. In parallel experiments, a Ca(2+)-insensitive calmodulin mutant was without effect on RyR2 activity. The results are discussed in terms of a possible role of CaM in the termination of cardiac sarcoplasmic reticulum Ca(2+) release.

Animals↗
PubMed1981

Functional characteristics of reconstituted sarcoplasmic reticulum membranes as a function of the lipid-to-protein ratio.

The ATP-induced Ca2+ accumulation efficiency and rates of Ca2+ uptake of the reconstituted sarcoplasmic reticulum (RSR) model membrane system were measured over an extended range of lipid-to-protein (L/P) molar ratios and were compared to those of isolated light sarcoplasmic reticulum (LSR). Highly purified sarcoplasmic reticulum (SR), dissociated in the presence of deoxycholate, was reconstituted for several L/P ratios, according to the same procedure, forming closed membranes vesicles composed of greater than 95% Ca2+ pump protein and SR lipids which were capable of ATP-induced Ca2+ accumulation in the absence of oxalate or other Ca2+ precipitating agents. This suggests that dissociation of SR and reconstitution to form RSR does not significantly affect the ability of the Ca2+ pump protein incorporated into the SR lipid bilayer to establish Ca2+ gradients. Electron micrographs of fixed and stained dispersions of RSR revealed a structural organization of the membrane that was dependent upon the L/P molar ratio. RSR with L/P greater than 88 were composed of closed vesicles whose membranes stained asymmetrically, similar to that observed for LSR. Closed vesicles of RSR with L/P less than 88 were composed of membrane that stained symmetrically. In addition, reconstituted SR preparations with well-defined L/P molar ratios greater than 88 possess a functional behavior similar to that of LSR (in the absence of oxalate, energy efficiencies are 60-70% and apparent initial uptake rates are 80% that of isolated LSR controls); RSR preparations with L/P less than 88 are characterized by significantly depressed values of the energy efficiencies and apparent initial uptake rates especially at low L/P ratios. Thus, we are the first to report a reconstituted SR model membrane system capable of attaining rates of Ca2+ uptake comparable to isolated LSR controls at comparable L/P ratios in the absence of oxalate or other Ca2+ precipitating agents.

Animals↗
PubMed1981

Evidence for the influence of the protein-phospholipid interface on sarcoplasmic reticulum Ca++ Mg++ ATPase activity.

Sarcoplasmic reticulum from the white hind leg muscle of the rabbit was examined with 31P nuclear magnetic resonance as a nonperturbing probe of phospholipid-protein interactions in the intact membrane. The phospholipids of the sarcoplasmic reticulum appear to inhabit two distinct environments: one very similar in behavior to pure phospholipid lamellar dispersions and the other immobilized by the protein in the membrane. Measurement of the population of the latter environment suggests that it is dependent on salt concentration and probably not due to the Ca++ Mg++ ATPase of the sarcoplasmic reticulum. This immobilization can be removed completely by papain proteolysis of the membrane protein, but only partially by trypsin treatment. The phospholipid composition of recombinants with the Ca++ Mg++ ATPase was varied in order to look for effects of the phospholipid-protein interface on enzymatic activity of the Ca++ Mg++ ATPase. Both transphosphatidylated phosphatidylethanolamine (from egg phosphatidylcholine) and bovine brain phosphatidylserine readily partitioned into the putative boundary layer, whereas under the same conditions soybean phosphatidylethanolamine was excluded. Only phosphatidylserine affected the activity of the enzyme, causing an inhibition that was proportional to the phosphatidylserine content, relative to phosphatidylcholine.

Animals↗
PubMed1986

Single channel and 45Ca2+ flux measurements of the cardiac sarcoplasmic reticulum calcium channel.

Purified canine cardiac sarcoplasmic reticulum vesicles were passively loaded with 45CaCl2 and assayed for Ca2+ releasing activity according to a rapid quench protocol. Ca2+ release from a subpopulation of vesicles was found to be activated by micromolar Ca2+ and millimolar adenine nucleotides, and inhibited by millimolar Mg2+ and micromolar ruthenium red. 45Ca2+ release in the presence of 10 microM free Ca2+ gave a half-time for efflux of 20 ms. Addition of 5 mM ATP to 10 microM free Ca2+ increased efflux twofold (t1/2 = 10 ms). A high-conductance calcium-conducting channel was incorporated into planar lipid bilayers from the purified cardiac sarcoplasmic reticulum fractions. The channel displayed a unitary conductance of 75 +/- 3 pS in 53 mM trans Ca2+ and was selective for Ca2+ vs. Tris+ by a ratio of 8.74. The channel was dependent on cis Ca2+ for activity and was also stimulated by millimolar ATP. Micromolar ruthenium red and millimolar Mg2+ were inhibitory, and reduced open probability in single-channel recordings. These studies suggest that cardiac sarcoplasmic reticulum contains a high-conductance Ca2+ channel that releases Ca2+ with rates significant to excitation-contraction coupling.

Animals↗