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  • 1
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    Comparison of Single and Sequential Extraction Procedures for Assessing Metal Leaching from Dredged Coastal Sediments (2005)
    Springer
    Details
    Publication Date: 2005-03-01
    Print ISSN: 0049-6979
    Electronic ISSN: 1573-2932
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Published by Springer
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  • 2
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    Relationship between Ca2+-transport and ATP hydrolytic activities in guinea-pig pancreatic acinar plasma membranes (1991)
    Springer
    Details
    Publication Date: 1991-01-01
    Print ISSN: 0300-8177
    Electronic ISSN: 1573-4919
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Springer
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  • 3
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    Regulation of calcium transport in pancreatic acinar plasma membranes from guinea pig (1992)
    Springer
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    Publication Date: 1992-06-01
    Print ISSN: 0300-8177
    Electronic ISSN: 1573-4919
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Springer
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  • 4
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    A non-specific Ca2+ (or Mg2+)-stimulated ATPase in rat heart sarcoplasmic reticulum (1990)
    Springer
    Details
    Publication Date: 1990-01-01
    Print ISSN: 0300-8177
    Electronic ISSN: 1573-4919
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Springer
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  • 5
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    Phosphorylation of cardiac junctional and free sarcoplasmic reticulum by PKC?, PKC?, PKA and the Ca2+/calmodulin-dependent protein kinase (1996)
    Springer
    Details
    Publication Date: 1996-02-01
    Print ISSN: 0300-8177
    Electronic ISSN: 1573-4919
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Springer
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  • 6
    Electronic Resource
    Electronic Resource
    Regulation of calcium transport in pancreatic acinar plasma membranes from guinea pig (1992)
    Springer
    Molecular and cellular biochemistry 112 (1992), S. 155-162 
    Details
    ISSN: 1573-4919
    Keywords: Ca2+-pump ; Ca2+-ATPase ; protein kinase A ; protein kinase C ; calmodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The regulation of the guinea-pig pancreatic acinar plasma membrane Ca2+ pump by protein kinase A, protein kinase C and calmodulin was investigated. The results were compared with the effects of these regulators on the high affinity Ca2+-ATPase found in this membrane preparation. The catalytic subunit of cyclic AMP-dependent protein kinase stimulated Ca2+ transport 2-fold, but had no effect on Ca2+-dependent ATPase activity. Purified protein kinase C, the phorbol ester 12-O-tetradecanoyl phorbol-13-acetate and diacylglycerol derivative, 1-stearoyl-2-arachidonoyl-sn-glycerol, failed to stimulate the Ca2+-uptake but augmented the Ca2+-dependent ATPase activity. Exogenously added calmodulin failed to stimulate either activity. In addition, two antagonists of calmodulin activity, trifluoperazine and compound 48/80 produced a concentration-dependent inhibition of Ca2+-transport. These data suggest the presence of endogenous calmodulin within guinea-pig pancreatic acinar plasma membranes. Both calmodulin antagonists failed to influence the Ca2+-dependent ATPase activity. The ability of boiled extracts from guinea-pig pancreatic acinar plasma membranes to stimulate the Ca2+-ATPase activity in calmodulin-depleted erythrocyte plasma membranes confirmed the presence of endogenous calmodulin. Our results imply a role for calmodulin and cAMP-dependent protein kinase, but not protein kinase C, in the regulation of Ca2+ efflux from pancreatic acinar cells. These results also provide further evidence suggesting that the high affinity Ca2+-ATPase does not catalyze the plasma membrane Ca2+-transport activity observed in pancreatic acini.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227572
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  • 7
    Electronic Resource
    Electronic Resource
    Phosphorylation of cardiac junctional and free sarcoplasmic reticulum by PKCα, PKCβ, PKA and the Ca2+/calmodulin-dependent protein kinase (1996)
    Springer
    Molecular and cellular biochemistry 155 (1996), S. 91-103 
    Details
    ISSN: 1573-4919
    Keywords: cardiac ; sarcoplasmic reticulum ; protein kinase C ; isoenzymes ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Phosphorylation of cardiac junctional and free sarcoplasmic reticulum (SR) by protein kinase C (PKC) isoforms α and β was investigated. Both SR and PKC were isolated from canine heart. Junctional and free SR vesicles were prepared by calcium-phosphate-loading. The substrate specificities of PKCα and PKCβ were found to be similar in both SR fractions. A high molecular weight junctionally-associated protein was phosphorylated by PKA, PKC and an endogenous Ca2+/calmodulin-dependent protein kinase activity: the highest levels of phosphate incorporation being catalysed by the latter kinase. In addition to this high molecular weight junctionally-associated protein, PKC induced phosphorylation of 45, 96 kDa and several proteins of greater than 200 kDa in junctional SR. A protein of 96 kDa was phosphorylated by both isoforms in junctional and free SR. The major substrate for PKA, PKCα, PKCβ and the Ca2+/calmodulin-dependent protein kinase, in both junctional and free SR, was phospholamban. Although the phosphorylation of phospholamban by PKC was activated by Ca2+, a component of this activity appeared to be independent of Ca2+. PKC-mediated phosphorylation of phospholamban was fully activated by 1 μM Ca2+ whereas the Ca2+/calmodulin dependent kinase required concentrations in excess of 5 μM Ca2+. In the in vitro system employed in these studies, the concentrations of either PKCα or the catalytic subunit of PKA required to phosphorylate phospholamban were found to be similar. In addition, in the presence of a 15 kDa sarcolemmal-associated protein, which becomes phosphorylated upon activation of PKC in vivo, phosphorylation of phospholamban by PKC was unaffected. These results demonstrate that, although substrates for both subtypes are found in both junctional and free SR, PKCα and PKCβ do not show differences in selectivity towards these substrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00229306
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  • 8
    Electronic Resource
    Electronic Resource
    Relationship between Ca2+-transport and ATP hydrolytic activities in guinea-pig pancreatic acinar plasma membranes (1991)
    Springer
    Molecular and cellular biochemistry 105 (1991), S. 137-147 
    Details
    ISSN: 1573-4919
    Keywords: Ca2+-pump ; Ca2+-ATPase ; high affinity ; Mg2+-dependent ; substrate specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Partially purified plasma membrane fractions were prepared from guinea-pig pancreatic acini. These membrane preparations were found to contain an ATP-dependent Ca2+-transporter as well as a heterogenous ATP-hydrolytic activity. The Ca2+-transporter showed high affinity for Ca2+ (KCa 2+ = 0.04 ± 0.01 μM), an apparent requirement for Mg2+ and high substrate specificity. The major component of ATPase activity could be stimulated by either Ca2+ or Mg2+ but showed a low affinity for these cations. At low concentrations, Mg2+ appeared to inhibit the Ca2+-dependent ATPase activity expressed by these membranes. However, in the presence of high Mg2+ concentration (0.5–1 mM), a high affinity Ca2+-dependent ATPase activity was observed (KCa 2+ = 0.08 ± 0.02 μM). The hydrolytic activity showed little specificity towards ATP. Neither the Ca2+-transport nor high affinity Ca2+-ATPase activity were stimulated by calmodulin. The results demonstrate, in addition to a low affinity Ca2+ (or Mg+)-ATPase activity, the presence of both a high affinity Ca2+-pump and high affinity Ca2+-dependent ATPase. However, the high affinity Ca2+-ATPase activity does not appear to be the biochemical expression of the Ca2+-pump.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227753
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of calcium-dependent forms of protein kinase C in adult rat ventricular myocytes (1997)
    Springer
    Molecular and cellular biochemistry 166 (1997), S. 11-23 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The presence and subcellular localization of the Ca2+-dependent protein kinase C (PKC) isoforms α and β were investigated in freshly isolated adult rat cardiac ventricular myocytes. PKC activity was measured in cytosolic and particulate fractions prepared from control myocytes and those treated with either phorbol ester (phorbol 12-myristate 13-acetate, PMA) or a permeant synthetic diacylglycerol analog (1-oleoyl-2-acetylglycerol, OAG) in the absence or presence of an inhibitor of diacylglycerol kinase activity, compound R59022. Preliminary studies detected no Ca2+-/phospholipid-dependent histone kinase activity in either subcellular fraction. To reproducibly observe Ca2+-/phospholipid-dependent protein kinase activity, partial purification using a MonoQ HR 5/5 column and the presence of the peptide inhibitor of the cAMP-dependent protein kinase were essential. MonoQ chromatography of cytosolic and particulate fractions resulted in three peaks of Ca2+/phospholipid-dependent protein kinase activity. In the cytosolic fraction a large peak of activity eluted at 230-300 mM NaCl. Isoform-specific antisera indicated both PKCα and PKCβ were present. In the particulate fraction two peak of Ca2+-/phospholipid-dependent protein kinase activity, both containing PKCa immunoreactivity, were observed. The larger peak eluted at 230-300 mM NaCl. In addition, a peak eluting at lower salt concentrations contained a Ca2+-/phospholipid-independent histone kinase activity. This peak of kinase activity contained PKCα immunoreactive bands of 80- and 50-kDa. The 80-kDa band was the holoenzyme of PKCα whereas the band of lower molecular mass was likely a proteolytic fragment. In both cytosolic and particulate fractions, the peak of kinase activity eluting at 230-300 mM NaCl contained PKCα in the form of an 80-kDa doublet; this suggested the presence of autophosphorylated PKC. Incubation of the myocytes with PMA, but not OAG, resulted in translocation of PKC from the cytosolic to the particulate fraction. Curiously, a transient decrease in PKC activity was observed in both subcellular fractions following treatment with either OAG or ethanol (1%). Results from this study show that freshly isolated adult rat cardiac ventricular myocytes contain both PKCα and PKCβ, and that these isoforms translocate to the particulate fraction in response to treatment with PMA, but not OAG. (Mol Cell Biochem 166: 11-23, 1997)
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006861011857
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  • 10
    Electronic Resource
    Electronic Resource
    A non-specific Ca2+ (or Mg2+)-stimulated ATPase in rat heart sarcoplasmic reticulum (1990)
    Springer
    Molecular and cellular biochemistry 96 (1990), S. 175-182 
    Details
    ISSN: 1573-4919
    Keywords: rat heart ; sarcoplasmic reticulum ; ATPase ; non-specific ; regulationwcalmodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract ATPase activity in rat heart sarcoplasmic reticulum was stimulated in a concentration-dependent manner by both Ca2+ and Mg2+ in the complete absence of the other cation. Increasing concentrations of Mg2+ produced an apparent inhibition of the Ca2+-dependent ATP hydrolysis. CDTA (trans-1,2-diaminocyclohexane-N,N,N′,N′-tetraacetate) had no effect on these responses. The results indicate the presence of a low affinity non-specific divalent cation-stimulated ATPase in rat heart sarcoplasmic reticulum. However, sarcoplasmic reticulum vesicles transported Ca2+ with a high affinity (K0.5 Ca2+ = 0.41 μM) suggesting the presence of a high affinity Ca2+-transporting ATPase. Calmodulin did not stimulate rat heart sarcoplasmic reticulum ATPase activity over a range of Ca2+ and Mg2+ concentrations and failed to stimulate membrane phosphorylation and Ca2+ transport into sarcoplasmic reticulum vesicles. Calmodulin antagonists trifluoperazine and compound 48180 did not affect the ATPase activity. Catalytic subunit of cAMP-dependent protein kinase was also ineffective in stimulating the ATPase activity. These results suggest the presence of an ATPase activity in rat heart sarcoplasmic reticulum with different properties from the high affinity Ca2+-pumping ATPase previously characterized in dog heart and other species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420909
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