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  • 1
    Electronic Resource
    Electronic Resource
    Oral β-stimulants can inhibit passive cutaneous anaphylaxis in rats through an indirect inhibitory mechanism: possible involvement of afferent and efferent nervous system via gastric β 2-adrenoceptor stimulation (2000)
    Springer
    Inflammation research 49 (2000), S. 714-719 
    Details
    ISSN: 1420-908X
    Keywords: Key words: Ephedrine – Stomach – Passive cutaneous anaphylaxis – Adrenergic nerve – Adrenoceptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Objective and Design: We previously demonstrated that oral l-ephedrine exerts an extremely rapid (within 20 s) inhibition of 48-h passive cutaneous anaphylaxis reaction (PCA) in rats by a possibly unidentified mode of action. In the present experiments, we elucidated the mechanism of the PCA inhibition by l-ephedrine using adrenoceptor agonists and antagonists.¶Materials: Rat antiserum was prepared with dinitrophenylated Ascaris suum extract + Bordetella pertussis.¶Treatment: Passively skin-sensitised Wistar rats were mainly used. l-Ephedrine, and adrenoceptor agonists and antagonists were orally administered immediately before PCA provocation. Catecholamine depleting (6-hydroxydopamine, 6-OH-DA), amine depleting (reserpine) or ganglion blocking (hexamethonium) agent was intraperitoneally or intravenously administered before the provocation.¶Methods: The effects of the drugs on PCA were assessed by inhibition of the dye leakage.¶Results: β-(propranolol) and β 2-(butoxamine) blocking agents reduced the inhibition of PCA by l-ephedrine, while the inhibition was not altered by either an α-blocking agent (phentolamine) or a β 1-(atenolol) selective antagonist. On the other hand, β-(isoproterenol) and β 2-selective (salbutamol) agonists showed extremely rapid inhibition of PCA. However, the β 1-selective agonist (dobutamine) had no effect on the reaction. The pretreatment with hexamethonium, reserpine or 6-OH-DA substantially attenuated the inhibitory effect of l-ephedrine on PCA.¶Conclusions: The results strongly suggest that β 2-adrenoceptors locate in the stomach and that their receptor excitement finally may lead to the inhibition of PCA via the stimulation of the central and peripheral nervous systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000110050651
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  • 2
    Electronic Resource
    Electronic Resource
    l-Ephedrine is a major constituent of Mao-Bushi-Saishin-To, one of the formulas of Chinese medicine, which shows immediate inhibition after oral administration of passive cutaneous anaphylaxis in rats (2000)
    Springer
    Inflammation research 49 (2000), S. 398-403 
    Details
    ISSN: 1420-908X
    Keywords: Key words: Ephedrine - Ephedra herb - Passive cutaneous anaphylaxis - Mast cell - Histamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: Objective and Design: Whether Mao-Bushi-Saishin-To (MBST), one of the formulas of classical Chinese medicine, is effective on 48-h passive cutaneous anaphylaxis (PCA) in rats and which substance in the formula is responsible for its inhibitory action were examined.¶Treatment: In the studies on PCA, MBST (hot water extract of the whole herbal formula), extracts of Ephedra herb (Mao), l-ephedrine and other reference drugs were orally administered immediately or at various times before or 5 min after the antigen challenge. In the experiments on anaphylactic histamine release from rat peritoneal mast cells, l-ephedrine and d-pseudoephedrine were added at 10-4-10-7 g/ml at 30, 10, 3 or 0 min before antigen provocation.¶Results: The time course study indicated that MBST produced a prompt and long lasting inhibition of PCA. Among the constituents of Mao, l-ephedrine exerted this prompt inhibitory activity, but d-pseudoephedrine did not. Neither pseudoephedrine nor l-ephedrine prevented the anaphylactic histamine release from isolated peritoneal mast cells.¶Conclusions: It is strongly emphasised that the rapid suppression of PCA by orally administered l-ephedrine must be exerted by a mechanism distinct from that of suppression produced following gastrointestinal absorption of the drug, because the time required for the inhibition was extraordinarily short. However, direct inhibition of anaphylactic histamine release from isolated mast cells was excluded in this inhibition of PCA.¶
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000110050607
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  • 3
    Electronic Resource
    Electronic Resource
    Immediate inhibition by oral l-ephedrine of passive cutaneous anaphylaxis of rats: indirect inhibition of anaphylactic chemical mediator release from the mast cell (2000)
    Springer
    Inflammation research 49 (2000), S. 553-559 
    Details
    ISSN: 1420-908X
    Keywords: Key words: Ephedrine - Passive cutaneous anaphylaxis - Mast cell - Vascular permeability - Histamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: Objective and Design: We previously reported that oral l-ephedrine showed extraordinarily rapid inhibition of 48-h passive cutaneous anaphylaxis (PCA) in rats. In the present study, in vivo and in vitro experiments were performed to elucidate a possible mechanism for the inhibition.¶Materials: Rat antiserum was prepared with dinitrophenylated Ascaris suum extract + Bordetella pertussis.¶Treatment: Wistar rats were passively skin-sensitised, actively sensitised or non-sensitised. l-Ephedrine immediately before provocations was orally or intravenously administered in in vivo experiments. In in vitro experiments, the drug was added at various time and concentrations before the challenge.¶Methods: The intensity of PCA was assessed by dye leakage method. Histamine and serotonin released in vitro or retained in the skin in vivo by anaphylaxis were assayed fluorometrically.¶Results: Oral l-ephedrine rapidly inhibited the PCA by inhibiting the release of histamine and serotonin from the reaction site, whereas anaphylactic histamine and serotonin releases from skin fragments were not affected by the drug. Furthermore, the orally administered drug influenced neither the histamine- nor serotonin-induced cutaneous vascular permeability.¶Conclusions: These results were strongly indicative that the prompt suppression of the PCA by oral l-ephedrine was not exerted following the drug was absorbed from the gastrointestinal tract. Thus, the result may be from an indirect inhibition of chemical mediator release, possibly through an unidentified stimulation of the nervous system, but not from the inhibition of chemical mediator release by the direct interaction of drug to mast cells and not from the decreased vascular permeability.¶
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000110050631
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  • 4
    Electronic Resource
    Electronic Resource
    Involvement of Smad proteins in the differentiation of pancreatic AR42J cells induced by activin A (1999)
    Springer
    Diabetologia 42 (1999), S. 719-727 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Beta-cell ; insulin ; differentiation ; activin A ; Smad.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aims/hypothesis. Activin A induces differentiation of amylase-secreting pancreatic AR42J cells into endocrine cells. This study assesses the role of Smad proteins in the actions of activin A in AR42J cells. Methods. The expression of Smad proteins was determined by northern blotting. Phosphorylation and translocation of Smad2 was measured by transfecting flag-tagged Smad2. Involvement of Smad2 was examined by transfecting cDNA encoding N-terminal and C-terminal domains of Smad2. Results. The mRNAs for Smad2 and Smad4 were abundantly expressed whereas the expression of mRNA for Smad1 and Smad3 was very low. Activin A induced serine-phosphorylation and the subsequent accumulation of the Smad2 in nuclei. Transfection of the N-terminal domain of Smad2, which acts as a dominantly negative mutant (Smad2-N), blocked the morphological changes induced by activin A whereas the C-terminal domain of Smad2, which acts as a constitutively active mutant (Smad2-C), reproduced the activin-induced morphological changes. Similarly, Smad2-N blocked apoptosis induced by activin A and Smad2-C induced apoptosis. Activin A converted AR42J into insulin-secreting cells in the presence of hepatocyte growth factor and introduction of Smad2-N inhibited the differentiation. Smad2-C, however, did not induce differentiation in the presence of hepatocyte growth factor. Conclusions/interpretation. Activation of the Smad2 pathway is necessary and sufficient to induce apoptosis and morphological changes. Although activation of the Smad2 pathway is required, it is not solely sufficient for the differentiation of AR42J into endocrine cells. [Diabetologia (1999) 42: 719–727]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051220
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  • 5
    Electronic Resource
    Electronic Resource
    Role of mitogen-activated protein kinase and phosphoinositide 3-kinase in the differentiation of rat pancreatic AR42J cells induced by hepatocyte growth factor (1999)
    Springer
    Diabetologia 42 (1999), S. 450-456 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Insulin ; beta cell ; differentiation ; hepatocyte growth factor ; MAP kinase.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aims/hypothesis. Pancreatic AR42J cells express both exocrine and neuroendocrine properties. When exposed to activin A, approximately 50 % of the cells die within 3 days by apoptosis. Addition of hepatocyte growth factor prevents apoptosis induced by activin A and induces differentiation into insulin-producing cells. The present study was conducted to examine the role of mitogen-activated protein kinase and phosphoinositide 3-kinase in the action of hepatocyte growth factor. Methods. The role of mitogen-activated protein kinase was assessed by using 2-(2 ′-amino-3 ′-methoxyphenol)-oxanaphthalen-4-one (PD098 059). Cells were also transfected with cDNA for mitogen-activated protein kinase phosphatase and constitutively active mutant of mitogen-activated protein kinase kinase. Results. Hepatocyte growth factor induced sustained activation of the mitogen-activated protein kinase, which was inhibited by PD098 059. PD098 059 completely blocked the differentiation and also blocked the prevention of apoptosis. Transfection of the cells with cDNA for mitogen-activated protein kinase phosphatase reproduced the effect of PD098 059. Conversely, transfection with cDNA for the constitutively active mutant of mitogen-activated protein kinase kinase reproduced the effect of hepatocyte growth factor. In contrast, addition of wortmannin or transfection of the dominantly negative form of the p85 subunit of the phosphoinositide 3-kinase did not affect differentiation induced by hepatocyte growth factor. Instead, wortmannin enhanced the increase in the insulin content of the differentiated AR42J cells. Conclusion/interpretation. The MAP kinase pathway is necessary and sufficient for the action of HGF on differentiation of AR42J cells. [Diabetologia (1999) 42: 450–456]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051178
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  • 6
    Electronic Resource
    Electronic Resource
    Inducing effect of feprazone on hepatic drug-metabolizing enzymes in man (1986)
    Springer
    European journal of clinical pharmacology 31 (1986), S. 117-118 
    Details
    ISSN: 1432-1041
    Keywords: feprazone ; drug-metabolizing enzyme ; enzyme induction ; 6β-hydroxycortisol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The inducing effect of feprazone, a pyrazolone anti-inflammatory agent, on hepatic drug-metabolizing enzymes has been studied in healthy volunteers. The ratio of 6β-hydroxycortisol (6β-OHF) to 17-hydroxycorticosteroids (17-OHCS) in urine, used as an indicator of oxidative drug-metabolizing enzyme activity, was increased up to 1.6-times the original level after 5 days of oral treatment with feprazone 300 mg/day. This indicates that feprazone induces hepatic drug-metabolising enzymes in man as does phenylbutazone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00870999
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  • 7
    Electronic Resource
    Electronic Resource
    Blood-to-plasma distribution of cyclosporin A in a renal transplant recipient (1988)
    Springer
    European journal of clinical pharmacology 35 (1988), S. 443-444 
    Details
    ISSN: 1432-1041
    Keywords: cyclosporin A ; kidney transplants ; blood-to-plasma distribution ; case report
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00561382
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  • 8
    Electronic Resource
    Electronic Resource
    Crystal-Grain Refinement of Materials under an Ultra-Strong Gravitational Field (2006)
    s.l. ; Stafa-Zurich, Switzerland
    Advanced materials research Vol. 15-17 (Feb. 2006), p. 639-642 
    Details
    ISSN: 1662-8985
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: In this study, we investigate the crystalline states and conditions for thegrain-refinement of Bi70Sb30 (at.%) alloy. It was considered under an ultra strong gravity field, thecrystals were fine-grained from the primary grain sizes of several mm to several tens of mm, andthe crystal growth followed with formation of graded-composition structure due to sedimentationof atoms along the direction of gravity. It was found that for the crystal-grain refinement inBi70Sb30 alloy the minimum gravitational field and the minimum time duration were at least160,000 G and 10 hours, respectively at about 200 ºC
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/01/39/transtech_doi~10.4028%252Fwww.scientific.net%252FAMR.15-17.639.pdf
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  • 9
    Electronic Resource
    Electronic Resource
    Crystallization of the alanine dehydrogenase from Phormidium lapideum (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 407-408 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Amino-acid dehydrogenases catalyse the interconversion of their respective amino acids to the corresponding keto acid, with concomitant reduction of NAD or NADP. The enzymes phenylalanine, glutamate, leucine and valine dehydrogenase all share a similar three-dimensional subunit structure and a high degree of sequence similarity, indicating that they belong to an enzyme superfamily related by divergent evolution. In contrast, alanine dehydrogenase shows no sequence similarity with any of these enzymes despite catalysing a reaction with the same chemistry and thus it is predicted that it possesses a different three-dimensional structure. The alanine dehydrogenase from Phormidium lapideum has been crystallized in space group R32, cell dimensions a = b = 123.1 and c = 184.8 Å, with a monomer in the asymmetric unit. The structure determination of this enzyme will shed light on how nature has evolved two different systems to carry out the same reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997011578
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  • 10
    Electronic Resource
    Electronic Resource
    Evidence that protein kinase C may not be involved in the insulin action on cAMP phosphodiesterase: Studies with electroporated rat adipocytes that were highly responsive to insulin
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 285 (1991), S. 97-104 
    Details
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-9861(91)90333-E
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