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  • 1995-1999  (5)
  • Amylase release  (2)
  • Phorbol myristate acetate  (2)
  • Key words Smooth muscle cell  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Gene expression of the human prostaglandin E receptor EP4 subtype: differential regulation in monocytoid and lymphoid lineage cells by phorbol ester (1996)
    Springer
    Journal of molecular medicine 74 (1996), S. 333-336 
    Details
    ISSN: 1432-1440
    Keywords: Prostaglandin E receptor ; EP4 subtype ; THP-1 ; Cyclic AMP ; Phorbol myristate acetate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We isolated a cDNA clone encoding the human prostaglandin (PG) E receptor EP4 subtype and examined the gene expression in human blood cells. Northern blot analysis revealed that the EP4 gene is expressed at a high level in peripheral blood mononuclear cells, and at lower levels in cultured human blood cell lines, THP-1 and U937 (monocytoid cell lines), MOLT-4 and Jurkat (T-cell lines), and Raji (B-cell line). To examine regulation of the EP4 gene expression in the immune system, we studied the effects of phorbol 12-myristate 13-acetate (PMA) on these cell lines. Gene expression was upregulated in THP-1, U937, and Raji cells by PMA, and was downregulated in MOLT-4 and Jurkat cells. In THP-1 cells the effects of PMA were further analyzed, and the upregulation of the EP4 gene was shown to be followed by an increase in PGE2 binding sites and in PGE2-induced cAMP accumulation. In the striking contrast, other PGE receptor subtypes (EP1, EP2 and EP3) and other prostanoid receptors (IP and DP) were shown not to be upregulated by PMA. Therefore, this is the first demonstration of a highly specific upregulation of the EP4 subtype in THP-1 cells treated with PMA, suggesting the importance of the EP4 subtype in the immune system. In the present study we also clarified that EP4 gene expression is regulated differently among human monocytoid and lymphoid lineage cells, thus leading to the better understanding of the regulatory mechanisms for the human EP4 gene expression in the immune system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00207510
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Gene expression of the human prostaglandin E receptor EP4 subtype: differential regulation in monocytoid and lymphoid lineage cells by phorbol ester (1996)
    Springer
    Journal of molecular medicine 74 (1996), S. 333-336 
    Details
    ISSN: 1432-1440
    Keywords: Key words Prostaglandin E receptor ; EP4 subtype ; THP-1 ; Cyclic AMP ; Phorbol myristate acetate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  We isolated a cDNA clone encoding the human prostaglandin (PG) E receptor EP4 subtype and examined the gene expression in human blood cells. Northern blot analysis revealed that the EP4 gene is expressed at a high level in peripheral blood mononuclear cells, and at lower levels in cultured human blood cell lines, THP-1 and U937 (monocytoid cell lines), MOLT-4 and Jurkat (T-cell lines), and Raji (B-cell line). To examine regulation of the EP4 gene expression in the immune system, we studied the effects of phorbol 12-myristate 13-acetate (PMA) on these cell lines. Gene expression was upregulated in THP-1, U937, and Raji cells by PMA, and was downregulated in MOLT-4 and Jurkat cells. In THP-1 cells the effects of PMA were further analyzed, and the upregulation of the EP4 gene was shown to be followed by an increase in PGE2 binding sites and in PGE2-induced cAMP accumulation. In the striking contrast, other PGE receptor subtypes (EP1, EP2 and EP3) and other prostanoid receptors (IP and DP) were shown not to be upregulated by PMA. Therefore, this is the first demonstration of a highly specific upregulation of the EP4 subtype in THP-1 cells treated with PMA, suggesting the importance of the EP4 subtype in the immune system. In the present study we also clarified that EP4 gene expression is regulated differently among human monocytoid and lymphoid lineage cells, thus leading to the better understanding of the regulatory mechanisms for the human EP4 gene expression in the immune system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001090050034
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Myosin light chain diphosphorylation is enhanced by growth promotion of cultured smooth muscle cells (1996)
    Springer
    Pflügers Archiv 432 (1996), S. 7-13 
    Details
    ISSN: 1432-2013
    Keywords: Key words Smooth muscle cell ; Myosin light chain mono and diphosphorylation ; Phosphatase ; Protein kinase C
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The characteristics of actively growing smooth muscle cells (a variant, SM-3) were compared with those of growth-arrested cells with regard to response of myosin light chain (MLC) phosphorylation. Augmented MLC phosphorylation, in particular diphosphorylation, was observed in actively growing cells when stimulated with 30 μM prostaglandin F2α (PGF2α). The maximum level of diphosphorylation in growing cells was significantly higher than that in growth-arrested cells. The MLC diphosphorylation was sensitive to protein kinase C down-regulation by phorbol dibutylate and pretreatment by the protein kinase inhibitors, staurosporine (30 nM) and isoquinoline sulphonamide HA1077 (20 μM). The actively growing cells contained larger amounts of protein kinase C than growth-arrested cells. The phosphorylation sites of mono- and diphospho-MLC were determined to be MLC kinase-dependent sites (Thr18, Ser19). The PGF2αconcentration/response curves of MLC diphosphorylation were shifted to the left and upwards in the presence of the protein phosphatase inhibitor calyculin A. These results suggest that PGF2αstimulation of actively growing SM-3 cells augments MLC kinase-dependent MLC diphosphorylation. Protein kinase C is involved indirectly in this reaction, possibly through MLC phosphatase-sensitive regulatory mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050099
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Effects of saturated fatty acids on amylase release from exocrine pancreatic segments of sheep, rats, hamsters, field voles and mice (1996)
    Springer
    Journal of comparative physiology 166 (1996), S. 305-309 
    Details
    ISSN: 1432-136X
    Keywords: Key words Exocrine pancreas ; Fatty acids ; Amylase release ; Sheep ; Rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Stimulatory effects of saturated fatty acids consisting of 4 (butyrate), 8 (octanoate), 12 (laurate) and 16 (palmitate) carbon atoms, as well as acetylcholine on pancreatic amylase release were assessed in tissue segments isolated from sheep, rats, hamsters, field voles and mice. The amount of amylase release induced by the fatty acids (1 μmol ⋅ l-1 to 10 mml ⋅ l-1) and by acetylcholine (10 nmol ⋅ l-1 to 100 μmol ⋅ l-1) increased in a concentration-dependent manner, and the maximum response in response to the fatty acids was obtained at the maximal dose used. The maximum increase in amylase release in response to butyrate or octanoate was highly and significantly (r=0.974, P〈0.001) dependent on the log value of the mean body mass in the following order: sheep〉rats〉hamsters〉field voles〉mice. On the other hand, the response to laurate and palmitate was variable among animal species. Addition of atropine (1.4 μmol ⋅ l-1) to the medium did not reduce the responses to octanoate stimulation, but significantly reduced acetylcholineinduced responses, implying that the effects of the fatty acids were not mediated through activation of muscarinic acetylcholine receptors. Reduction of calcium ion concentration in the medium significantly inhibited the responses induced by the fatty acids and acetylcholine, suggesting that amylase release depends on extracellular calcium ions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003600050012
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of saturated fatty acids on amylase release from exocrine pancreatic segments of sheep, rats, hamsters, field voles and mice (1996)
    Springer
    Journal of comparative physiology 166 (1996), S. 305-309 
    Details
    ISSN: 1432-136X
    Keywords: Exocrine pancreas ; Fatty acids ; Amylase release ; Sheep ; Rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Stimulatory effects of saturated fatty acids consisting of 4 (butyrate), 8 (octanoate), 12 (laurate) and 16 (palmitate) carbon atoms, as well as acetylcholine on pancreatic amylase release were assessed in tissue segments isolated from sheep, rats, hamsters, field voles and mice. The amount of amylase release induced by the fatty acids (1 μmol·l−1 to 10 mml·l−1) and by acetylcholine (10 nmol·l−1 to 100 μmol·l−1) increased in a concentration-dependent manner, and the maximum response in response to the fatty acids was obtained at the maximal dose used. The maximum increase in amylase release in response to butyrate or octanoate was highly and significantly (r=0.974,P〈0.001) dependent on the log value of the mean body mass in the following order: sheep 〉 rats 〉 hamsters 〉 field voles 〉 mice. On the other hand, the response to laurate and palmitate was variable among animal species. Addition of atropine (1.4 μmol·l−1) to the medium did not reduce the responses to octanoate stimulation, but significantly reduced acetylcholine-induced responses implying that the effects of the fatty acids were not mediated through activation of muscarinic acetylcholine receptors. Reduction of calcium ion concentration in the medium significantly inhibited the responses induced by the fatty acids and acetylcholine, suggesting that amylase release depends on extracellular calcium ions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02439916
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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