We examined the effects of omeprazole and SDZ CO-611 (an orally active somatostatin analog) alone and in combination, on ulcer healing, gastric acid secretion and the serum gastrin level in rats.Two or 4-wk' treatment with oral omeprazole significantly enhanced spontaneous healing and/or prevented delayed healing (caused by indomethacin) of acetic acid ulcers, with the inhibition of gastric acid secretion and hypergastrinemia.While oral SDZ CO-611 had no effect on spontaneous ulcer healing, it significantly prevented delayed ulcer healing.On SDZ CO-611 treatment, gastric acid secretion was significantly inhibited but basal gastrin level remained unchanged.Hypergastrinemia induced by a single treatment with oral omeprazole was markedly suppressed by SDZ CO-611 for >12 h.SDZ CO-611, administered together with omeprazole for 2 or 4 wk, did not affect the enhanced ulcer healing or the antisecretory effect of omeprazole, despite a greater than 60% decrease.We conclude that omeprazole-induced hypergastrinemia does not contribute to the mechanism by which omeprazole enhances ulcer healing.

01 Jun 1996·NeuropharmacologyQ2 · MEDICINE

Localization and pharmacological characterization of somatostatin recognition sites in the human cerebellum

Q2 · MEDICINE

Article

Author: D. Hoyer ; A. Probst ; V.S. Thoss ; C. Piwko

Radioligand binding studies were performed in membranes of human cerebellum using [125I][Tyr3]octreotide also known as [125I]204-090, [125I]LTT-SRIF-28 ([Leu8, D-Trp22, 125I-Tyr25]SRIF-28) and [125I]CGP 23996 ([125I]c[Asu-Lys-Asn-Phe-Trp-Lys-Thr-Tyr-Thr-Ser]) to characterize the nature of cerebellar somatostatin receptors. Saturation experiments performed with [125I]204-090 suggest the presence of a single class of binding sites with high affinity: Bmax = 55.7 +/- 9.7 fmol/mg protein, pKd = 9.57 +/- 0.04. The pharmacological profile of [125I]204-090 and [125I]LTT-SRIF-28 labelled sites in human cerebellar membranes was overlapping (correlation coefficient r = 0.998) and correlated very significantly with that of recombinant human sst2 receptors (r = 0.987). By contrast, there was very little correlation with those of recombinant human sst3 (r = 0.208) or human sst5 receptors (r = 0.547). In contrast to [125I]204-090 or [125I]LTT-SRIF-28 binding, [125I]CGP 23996 binding (in 5 mM MgCl2 buffer) in cerebellar membranes was heterogeneous as indicated by biphasic competition curves produced by sst2 receptor selective ligands such as seglitide or octreotide. The pharmacological profile of the major component was closely correlated with that of human sst2 receptors (r = 0.989), whereas the minor component correlated equally well with human sst1 or sst4 receptors (r = 0.902 and 0.941, respectively). In vitro autoradiographic studies performed in cerebellar slices using [125I]204-090 and [125I]LTT-SRIF-28 demonstrated the presence of binding sites predominantly in the molecular layer, whereas weaker labelling was detected in the granular layer. The distribution of sites labelled by both radioligands was very similar. Using [125I]CGP 23996 (in 120 mM NaCl buffer), no clear difference between labeling of the molecular and granular layers was detectable; the dentate nucleus demonstrated binding sites for [125I]CGP 23996, in contrast to the very low level of binding observed with both, [125I]204-090 and [125I]LTT-SRIF-28. Together, the present data demonstrate the presence of SRIF receptors in the adult human cerebellar cortex which are, for the major population, best characterized as sst2. The SRIF receptors in the minor populations of the cerebellar cortex and the dentate nucleus most probably represent sst1 and/or sst4 sites.

01 Jan 1996·XenobioticaQ4 · MEDICINE

Biotransformation of a somatostatin analogue in precision-cut liver and kidney slices from rat, dog and man

Q4 · MEDICINE

Article

Author: Larrauri, A. ; Dannecker, R. ; Vickers, A. E. M. ; Brendel, K. ; Nufer, R. ; Connors, M. S.

1. Cleavage of the glucopyranosyl moiety of the somatostatin analogue SDZ CO 611 results in the formation of the major metabolite, SDZ CO 610, in liver and kidney slices of rat, dog and man, as well as in liver S9 and cytosol of rat and man. 2. The rates of SDZ CO 610 formation (nmol/h/mg slice protein) for all three species were determined in liver slices for 24 h and the relative order was: rat (0.12) > dog (0.096) = man (0.095). The rates of SDZ CO 610 formation (nmol/h/mg slice protein) for all three species in kidney were determined, and the relative order was: rat (0.29) > dog (0.16) > man (0.10). 3. SDZ CO 610 was rapidly formed by rat gut contents in the absence of NADPH, possibly by disaccharide-splitting enzymes. 4. Biotransformation of SDZ CO 611 to SDZ CO 610 in human and rat liver S9 and cytosol was similar to that found in liver slices cultures indicating that cleavage of the glucopyranosyl moiety of SDZ CO 611 could occur in the presence and in the absence of cytochrome P450, possibly by glucosidases in liver cytosol. 5. Rat intestinal homogenate also formed SDZ CO 610 but metabolism was dependent upon NADPH, suggestive of a cytochrome P450-dependent reaction.

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