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  • 1
    Electronic Resource
    Electronic Resource
    Breakdown of hypothalamic peptides by hypothalamic neutral endopeptidase (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb00395.x
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  • 2
    Electronic Resource
    Electronic Resource
    Distribution of a neurospecific cardioactive protein-hormonal complex in rats with experimental myocardial ischemia (1990)
    Springer
    Bulletin of experimental biology and medicine 109 (1990), S. 177-179 
    Details
    ISSN: 1573-8221
    Keywords: protein-hormonal complex ; cardioactive antigen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00841663
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of the hypothalamic cardioactive protein-hormonal complex on choline sensitivity of the small intestine and contraction of the vas deferens in rats (1995)
    Springer
    Bulletin of experimental biology and medicine 119 (1995), S. 270-272 
    Details
    ISSN: 1573-8221
    Keywords: noradrenergic transmitter ; cardioactive protein-hormonal complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A cardioactive protein-hormonal complex capable of increasing the sensitivity of the small intestine to acetylcholine about 2.5 times was isolated from magnocellular nuclei of the hypothalamo-neurohypophyseal system. Moreover, this complex enhanced contraction of the vas deferens caused by transmural stimulation, exogenous noradrenalin, and phenylephrine. The findings indicate release of transmitters from cholinergic and adrenergic neurons under the influence of the complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02445832
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  • 4
    Electronic Resource
    Electronic Resource
    Correlation between the inhibition of phosphorylation in platelet myosin light chains and the inhibition of platelet aggregation by a new calcium and calmodulin antagonist (1996)
    Springer
    Bulletin of experimental biology and medicine 122 (1996), S. 684-686 
    Details
    ISSN: 1573-8221
    Keywords: platelet aggregation ; phosphorylation of myosin light chains ; calmodulin antagonists
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The recently synthesized compound [1,2,5-trimethyl-4-phenyl-4-β-(N-methyl-N-4′-methoxybenzyl)-ethylamino]piperidine dihydrochloride (AR-3), which is a derivative of [1,2,5-trimethyl-4-phenyl-4-β-(N,N-disubstituted-ethylamino)]piperidines, was tested for its effects on platelet aggregation and phosphorylation of light myosin chains isolated from platelets. AR-3 caused 50% inhibition of platelet aggregation in concentrations of 25.5 to 32.2 μM (depending on the aggregation inducer used) and 50% inhibition of light myosin chain phosphorylation in a concentration of 70 μM or, when 1 μM calmodulin was added, 120 μM. The good correlation found between the inhibitory effects of AR-3 on platelet aggregation and the phosphorylation of light myosin chains from platelets indicates that this compound inhibits platelet aggregation largely by inhibiting the Ca2+-calmodulin-dependent phosphorylation of platelet myosin light chains, acting in this respect similarly to the well-known calmodulin antagonist W-7.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02446022
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  • 5
    Electronic Resource
    Electronic Resource
    Regulation of multiple forms of cyclic nucleotide phosphodiesterase from bovine hypothalamus: New factors modulating enzyme activity (1985)
    Springer
    Neurochemical research 10 (1985), S. 1467-1481 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Studies of bovine hypothalamic cyclic nucleotide phosphodiesterase (PDE) indicate the presence of several peaks of PDE activity, distinguishable by DEAE-cellulose column chromatography, displaying different substrate specificities, kinetic behavior, and regulatory properties. Evidence is presented that chromatographically separated forms of PDE activity are subject to control by Ca2+-calmodulin, cyclic nucleotides, limited proteolysis, reagents affecting sulfhydryl groups, and neurohormone “C”—one of several new cardioactive compounds isolated from hypothalamic magnocellular nuclei of animals—in a complex substrate-specific and concentration-dependent manner. Of particular interest is the finding that each of the forms of cGMP PDE, being Ca2+/calmodulin-dependent, possesses sensitivity to activation by cAMP, especially under conditions favoring the oxidation of thiol groups of PDE, resulting in a loss in responsiveness of the enzyme to the activation by calmodulin. This effect appears to be relatively stable but readily reversible by sulfhydryl reducing reagents, which restore both the cGMP PDE sensitivity to competitive inhibition by cAMP and the responsiveness of the enzyme to activation by calmodulin. A reinterpretation of the regulatory properties of multiple forms of PDE is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00988860
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  • 6
    Electronic Resource
    Electronic Resource
    Regulation of multiple forms of cyclic nucleotide phosphodiesterase from bovine hypothalamus: New factors modulating enzyme activity (1985)
    Springer
    Neurochemical research 10 (1985), S. 1467-1481 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Studies of bovine hypothalamic cyclic nucleotide phosphodiesterase (PDE) indicate the presence of several peaks of PDE activity, distinguishable by DEAE-cellulose column chromatography, displaying different substrate specificities, kinetic behavior, and regulatory properties. Evidence is presented that chromatographically separated forms of PDE activity are subject to control by Ca2+-calmodulin, cyclic nucleotides, limited proteolysis, reagents affecting sulfhydryl groups, and neurohormone “C”—one of several new cardioactive compounds isolated from hypothalamic magnocellular nuclei of animals—in a complex substrate-specific and concentration-dependent manner. Of particular interest is the finding that each of the forms of cGMP PDE, being Ca2+/calmodulin-dependent, possesses sensitivity to activation by cAMP, especially under conditions favoring the oxidation of thiol groups of PDE, resulting in a loss in responsiveness of the enzyme to the activation by calmodulin. This effect appears to be relatively stable but readily reversible by sulfhydryl reducing reagents, which restore both the cGMP PDE sensitivity to competitive inhibition by cAMP and the responsiveness of the enzyme to activation by calmodulin. A reinterpretation of the regulatory properties of multiple forms of PDE is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02430598
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Neurohormonal regulation of calcium in the cell (1988)
    Springer
    Neurochemical research 13 (1988), S. 493-498 
    Details
    ISSN: 1573-6903
    Keywords: Necrosis of myocardium ; neurohormone “C” ; mitochondrial proteins ; reticulum proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Neurohormone “C” (NC) is a glycopeptide isolated from bovine hypothalamus, which inhibits Ca-calmodulin (CaM)-dependent cAMP and cGMP phosphodiesterase (PDE) and is a regulator of Ca in the cell. Distribution of [45Ca]CaCl2 in the mitochondria and reticulum (SR) of heart and brain mitochondria and changes of Ca-binding proteins in these organelles under NC influence have been studied in the myocardium before and after isoproterenol-induced necrosis. Intraperitoneal administration of 80–100 mU of PDE inhibitory activity of NC to rats did not cause any noticeable changes in the protein content of intracellular organelles, but altered the affinity of certain proteins to45Ca2+. This property of NC was especially noticable after isoproterenol necrosis. Necrotic injury of the myocardium induced Ca2+ storage in the mitochondria and SR of brain, and decreased the Ca2+ concentration in myocardial mitochondria. NC injection to the animals with necrosis was followed by Ca2+ release from all the studied organelles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01268886
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  • 8
    Electronic Resource
    Electronic Resource
    A hypothalamic activator of calmodulin-dependent enzymes is thymosin β4 (1–39) (1992)
    Springer
    Neurochemical research 17 (1992), S. 773-777 
    Details
    ISSN: 1573-6903
    Keywords: Thymosin ; calcium-calmodulin ; myosin light chain kinase ; phosphodiesterase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A new class of stimulators of basal activity of a number of calmodulin-dependent enzymes have been previously isolated from bovine hypothalamus. One of these stimulators, denoted as C3, has been purified to homogeneity by reverse phase HPLC and tentatively identified as thymosin β4 (1–39) by mass spectrometry and Edman microsequence analysis. The stimulating effect of C3 on rabbit skeletal muscle MLCK basal activity was compared with that of thymosin α1 and thymosin β4 (16–38). Evidence is presented that all the indicated compounds are Ca2+-independent high-affinity MLCK stimulators. The potency of the stimulators in activating the enzyme was: C3〉β4〉(CaM+Ca2+〉α1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00969011
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  • 9
    Electronic Resource
    Electronic Resource
    Calcium- and calmodulin-independent modulation of calmodulin-sensitive hypothalamic cyclic nucleotide phosphodiesterase activity by the (11–19) fragment of thymosin β4 (1994)
    Springer
    Neurochemical research 19 (1994), S. 451-456 
    Details
    ISSN: 1573-6903
    Keywords: Affinity HPLC ; Thymosin β4 ; cAMP ; calmodulin ; phosphodiesterase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A fragment (11–19) of thymosin β4 was found to stimulate phosphodiesterase activity even in the absence of calcium and calmodulin. Half-maximal enzyme activation occurred with 10 nM peptide, and was further increased by phospholipids such as phosphatidylserine. The mechanism of stimulation is an increase in the Vmax of cAMP degradation without a substantial change in the Km for the substrate. In the presence of calcium ions and calmodulin the peptide was also stimulatory.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00967323
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  • 10
    Electronic Resource
    Electronic Resource
    Acid proteinase of hypothalamus (1978)
    Springer
    Neurochemical research 3 (1978), S. 89-99 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In a continuing study of the physiological role of protein breakdown in the hypothalamus, acid proteinase from bovine hypothalamus was purified about 1000-fold. The molecular weight of the enzyme was approximately 50,000. Maximal activity against hemoglobin was obtained at pH 3.2–3.5; serum albumin was split much more slowly. Hypothalamus acid proteinase was partially inhibited by β-phenyl pyruvate, or benzethonium Cl, and was completely inhibited by low concentrations of pepstatin. This proteinase splits somatostatin, substance P, and analogs of substance P. The probable sites of enzyme action on these peptides were determined by the end group dansyl technique. The enzyme, most likely cathepsin D, may play an important role in the formation and breakdown of peptide hormones in the hypothalamus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00964362
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