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  • 1
    Electronic Resource
    Electronic Resource
    Improved Suspension Technique for Quantitative Infrared Analysis of Insoluble Solids. (1963)
    s.l. : American Chemical Society
    Analytical chemistry 35 (1963), S. 931-933 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60200a051
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  • 2
    Electronic Resource
    Electronic Resource
    Glucagon-like peptide-1 but not glucagon-like peptide-2 stimulates insulin release from isolated rat pancreatic islets (1985)
    Springer
    Diabetologia 28 (1985), S. 704-707 
    Details
    ISSN: 1432-0428
    Keywords: Glucagon-like peptide-1 ; glucagon-like peptide-2 ; insulin release ; glucose dependency ; isolated islets
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Glucagon-like peptide-1 and glucagon-like peptide-2 are encoded by the m-RNA of pancreatic preproglucagon. They show high conservation in different species and substantial sequence homology to glucagon. Because no definite biological activity of these peptides has been reported, we investigated the effect of synthetic C-terminally amidated glucagon-like peptide-1 [1–36] and synthetic human glucagon-like peptide-2 [1–34] with a free C-terminus on insulin release from isolated precultured rat pancreatic islets in the presence of glucose. Glucagon-like peptide-1 stimulates insulin release at 10 and 16.7 mmol/l glucose in a dose-dependent manner. Significant stimulation starts at 2.5 nmol/l in the presence of 10 mmol/l glucose and near maximal release is observed at 250 nmol/l, with approximately 100% increase over basal at both glucose concentrations. The peptide reaches 63% of the maximal stimulatory effect of glucagon. No stimulation occurs in the presence of 2.8 mmol/l glucose. Glucagon-like peptide-2 has no effect on insulin secretion at any glucose concentration tested. It is concluded that glucagon-like peptide-1, in contrast to glucagon-like peptide-2, exhibits a glucose-dependent insulinotropic action on isolated rat pancreatic islets similar to that of glucagon and gastric inhibitory polypeptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00291980
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  • 3
    Electronic Resource
    Electronic Resource
    Morphological and functional changes of pancreatic B cells in cyclosporin A-treated rats (1984)
    Springer
    Diabetologia 27 (1984), S. 416-418 
    Details
    ISSN: 1432-0428
    Keywords: Cyclosporin A ; B cell changes ; pancreatic insulin content ; insulin levels ; hyperglycaemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Cyclosporin A (50 mg/kg orally for 7 days) produced severe degranulation and hydropic degeneration of islet B cells in rats. These changes were accompanied by hyperglycaemia and hypoinsulinaemia, while the pancreatic insulin content decreased by 75%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00304861
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  • 4
    Electronic Resource
    Electronic Resource
    The neuropeptide PACAP upregulates expression and release of cytokines and cell adhesion molecules in human microvascular endothelial cells via VPAC type 1 receptor (2004)
    Oxford, UK; Malden, USA : Blackwell Publishing Ltd/Inc
    Experimental dermatology 13 (2004), S. 0 
    Details
    ISSN: 1600-0625
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Pituitary adenylate cyclase-activating peptide (PACAP) and vasoactive intestinal peptide (VIP) belong to the same superfamily of neuropeptides which exert their effects by activating G-protein-coupled receptors defined as PACAP. So far, three receptor subtypes exist (PAC1R, VPACR-1 and VPACR-2). Because, PACAP appears to play a crucial role in cutaneous inflammation and vasoregulation, we examined the expression and biological effects of this peptide in primary human dermal microvascular endothelial cells (HDMECs). We detected the expression of PACAP and VPAC type 1 receptor at RNA and protein level by RT-PCR and immunohistochemistry, indicating an autocrine regulatory mechanism. cAMP assays revealed VPAC1R to be functional in these cells. RT-PCR showed upregulation of IL-8 in a time- and dose-dependent manner. ELISA experiments confirmed release of IL-8 by HDMEC cells. We also investigated cell adhesion molecule expression after stimulation with PACAP. ICAM-1 mRNA was upregulated at 3 and 6 h after treatment with PACAP, while VCAM was only upregulated maximally at 6 h after PACAP stimulation, indicating the regulation of cell adhesion molecule expression in human dermal endothelial cells via VPAC1R. Immunoreactivity for VPAC-1R was enhanced in microvascular endothelial cells of patients with atopic dermatitis and urticaria, indicating upregulation of this receptor in endothelial cells during cutaneous inflammation. In summary, VIP and PACAP may play an important role in cutaneous neurogenic inflammation by activating VPAC-1R on dermal microvascular endothelial cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0906-6705.2004.0212bw.x
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  • 5
    Electronic Resource
    Electronic Resource
    Interferone und Nukleosidanaloga Neue Perspektiven in der Therapie chronischer Virushepatitiden (1998)
    Springer
    Der Internist 39 (1998), S. 95-104 
    Details
    ISSN: 1432-1289
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001080050148
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  • 6
    Electronic Resource
    Electronic Resource
    PACAP induces bradycardia in guinea-pig heart by stimulation of atrial cholinergic neurones (1996)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 354 (1996), S. 424-430 
    Details
    ISSN: 1432-1912
    Keywords: PACAP ; Acetylcholine release ; Guinea-pig heart ; ω-conotoxin ; Patch-clamp technique ; cAMP ; Phosphorylation ; Chronotropy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Based on previous studies which indicated that pituitary adenylate cyclase activating peptide (PACAP) acts as a positive inotropic and chronotropic substance in different species via the cAMP signal transduction pathway, the objective of the present work was to investigate cAMP-regulated myocardial key proteins in response to PACAP in isolated ventricular cells of the guinea pig. Surprisingly, the two molecular forms of PACAP, PACAP(1–27) and PACAP(1–38), showed no effect on intracellular cAMP-levels, L-type Ca2+ channel current or phosphorylation of troponin inhibitor (TnI) and phospholamban (PLB). Additionally, inotropy of isolated guinea-pig ventricular strips was not affected by the neuropeptide. However, in isolated spontaneously beating guinea-pig atria, PACAP(1–27) and PACAP(1–38), but not VIP induced severe bradycardia in a dose-dependent manner. This effect could be prevented by preincubation with the PACAP receptor antagonist PACAP(6–38), by atropine and by ω-conotoxin, a blocker of neuronal N-type Ca2+channels. PACAP stimulates release of [3H]-labelled acetylcholine. Only preparations showing an increase in [3H]acetylcholine release developed bradycardia, indicating a causal relationship between both phenomena. It was concluded that PACAP exerts no influence on guinea-pig ventricular tissue, but induces negative chronotropic effects in isolated guinea-pig atria by stimulation of acetylcholine release from parasympathetic neurons via PACAP type 1 receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00168432
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  • 7
    Electronic Resource
    Electronic Resource
    PACAP induces bradycardia in guinea-pig heart by stimulation of atrial cholinergic neurones (1996)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 354 (1996), S. 424-430 
    Details
    ISSN: 1432-1912
    Keywords: Key words PACAP ; Acetylcholine release ; Guinea-pig heart ; ω-conotoxin ; Patch-clamp technique ; cAMP ; Phosphorylation ; Chronotropy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Based on previous studies which indicated that pituitary adenylate cyclase activating peptide (PACAP) acts as a positive inotropic and chronotropic substance in different species via the cAMP signal transduction pathway, the objective of the present work was to investigate cAMP-regulated myocardial key proteins in response to PACAP in isolated ventricular cells of the guinea pig. Surprisingly, the two molecular forms of PACAP, PACAP(1–27) and PACAP(1–38), showed no effect on intracellular cAMP-levels, L-type Ca2+channel current or phosphorylation of troponin inhibitor (TnI) and phospholamban (PLB). Additionally, inotropy of isolated guinea-pig ventricular strips was not affected by the neuropeptide. However, in isolated spontaneously beating guinea-pig atria, PACAP(1–27) and PACAP(1–38), but not VIP induced severe bradycardia in a dose-dependent manner. This effect could be prevented by preincubation with the PACAP receptor antagonist PACAP(6–38), by atropine and by ω-conotoxin, a blocker of neuronal N-type Ca2+channels. PACAP stimulates release of [3H]-labelled acetylcholine. Only preparations showing an increase in [3H]acetylcholine release developed bradycardia, indicating a causal relationship between both phenomena. It was concluded that PACAP exerts no influence on guinea-pig ventricular tissue, but induces negative chronotropic effects in isolated guinea-pig atria by stimulation of acetylcholine release from parasympathetic neurons via PACAP type 1 receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00168432
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  • 8
    Electronic Resource
    Electronic Resource
    Pituitary adenylate cyclase activating peptide, a novel VIP-like gut-brain peptide, relaxes the guinea-pig taenia caeci via apamin-sensitive potassium channels (1992)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 346 (1992), S. 511-514 
    Details
    ISSN: 1432-1912
    Keywords: Gastrointestinal tract ; Non-adrenergic ; non-cholinergic transmitter ; PACAP receptors ; Smooth muscle ; Guinea-pig taenia caeci
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Effects of pituitary adenylate cyclase activating peptide (PACAP-(1-27)) and vasoactive intestinal polypeptide (VIP) on the guinea-pig taenia caeci were studied in the presence of guanethidine and scopolamine. Both peptides (1 nmol/1-1 μmol/1) concentration-dependently relaxed the smooth muscle of the taenia. PACAP-(1-27) and VIP were nearly equipotent. Apamin (30 nmol/1), a selective blocker of calcium-activated potassium channels, abolished the relaxation induced by PACAP-(1–27) whereas the effect of VIP remained unaffected. PACAP-(1–27) may be a candidate for the noncholinergic, non-adrenergic inhibitory neurotransmitter which induces apamin-sensitive relaxation in the intestinal tract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169005
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  • 9
    Electronic Resource
    Electronic Resource
    Light and electron microscopical immunocytochemical localization of pancreastatin-like immunoreactivity in porcine tissues (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 369-380 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Pancreastatin is a 49 amino acid comprising peptide isolated from porcine pancreas that is derived by proteolytic processing from chromogranin A. Using an antibody against the synthetic C-terminal fragment pancreastatin (33–49), we examined the light and electron microscopical immunocytochemical localization of this peptide in porcine tissues. Pancreastatin-like immunoreactivity (PLI) was found in pancreatic somatostatin-, insulin- and glucagon cells in varying intensities; pancreatic polypeptide cells were always negative. At the electron microscopical (EM) level the immunoreactivity was confined to the electron dense core of the secretory granules in the case of somatostatin and insulin cells or to the less electron dense “halo” of the glucagon granules. In the antrum PLI positive cells represented gastrin (G), somatostatin (D) and enterochromaffin (EC) cells, in the duodenum in addition to EC- and G-cells a small number of PLI positive cells showed a positive immunoreaction for glucagon-like peptide (GLP) I and secretin in serial sections. Both norepinephrine and epinephrine containing cells of the adrenal medulla exhibited a strong reaction for PLI. In the pituitary several cell populations stained with varying intensities, including gonadotrophs and thyrotrophs. PLI is present in a distinct and characteristic subpopulation of neuroendocrine cells in various organs. The subcellular localization may indicate a function in the granular concentration, packaging and storage of peptides and amines in the brain-gut endocrine system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315853
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  • 10
    Electronic Resource
    Electronic Resource
    Bücher- und Zeitschriftenschau (1930)
    Springer
    International journal of earth sciences 21 (1930), S. 314-338 
    Details
    ISSN: 1437-3262
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01813012
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    Paper (German National Licenses)
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