Histamine and acute haemorrhagic lesions in rat gastric mucosa: Prevention of stress ulcer formation by (+)-catechin, an inhibitor of specific histidine decarboxylase in vitro

1977 ◽  
Vol 7 (1) ◽  
pp. 69-73 ◽  
Author(s):  
H. -J. Reimann ◽  
W. Lorenz ◽  
M. Fischer ◽  
R. Frölich ◽  
H. -J. Meyer ◽  
...  
1988 ◽  
Vol 66 (8) ◽  
pp. 1139-1143 ◽  
Author(s):  
Gary B. Glavin ◽  
Lorne J. Brandes

N,N-Diethyl-2-[4-(phenylmethyl)-phenoxy]-ethanamine hydrochloride (DPPE) is a para-diphenylmethane derivative that binds selectively and with high affinity to the microsomal antiestrogen binding site (AEBS). Recent studies with DPPE indicate that AEBS is closely related to a lower affinity non-H1, non-H2 histamine site that may be associated with calcium channels; the DPPE–AEBS site is different from that which verapamil binds, however. DPPE, but not verapamil, demonstrates antiproliferative effects in vitro and is antiestrogenic in vivo. We now show that DPPE profoundly inhibits restraint and cold stress and ethanol-induced gastric ulcer formation, accelerates ulcer healing, attenuates the stress-induced rise in plasma corticosterone level, and significantly reduces basal and H2 agonist (dimaprit)-stimulated and, to a lesser extent, bethanechol-stimulated gastric acid output in conscious rats. A nonulcerogenic but prostaglandin-depleting dose of indomethacin completely blocks the inhibitory effects of DPPE on stress ulcer formation. Conversely, verapamil only slightly attenuates dimaprit-stimulated gastric acid secretion and exacerbates ethanol-induced gastric ulcers; its anti-stress ulcer effects are only partially attenuated by indomethacin. These findings support the likelihood that the site of action of DPPE is different from that of verapamil, and that an effect on prostaglandins may, at least in part, contribute to its antiulcer and apparent cytoprotective effects.


1994 ◽  
Vol 79 (5) ◽  
pp. 647-659 ◽  
Author(s):  
MA Miller ◽  
NW Bunnett ◽  
HT Debas

1982 ◽  
Vol 205 (2) ◽  
pp. 405-412 ◽  
Author(s):  
A Savany ◽  
L Cronenberger

The heterogeneity of histidine decarboxylase from rat gastric mucosa was studied. The partially purified enzyme was fractionated by preparative isoelectric focusing on a flat-gel bed by using narrow pH-range carrier ampholytes and a short focusing time. The activity was resolved, with about 95% recovery, into three forms, designated I, II and III, with pI values of 5.90, 5.60 and 5.35 respectively. These three forms exhibited similar molecular weights, indicating that the forms were not the result of different degrees of polymerization. By preparative refocusing each form refocused as a single peak of enzyme activity with reproducible pI, but a high loss of activity occurred with repeated focusing. Forms I, II and III were purified by the combined use of preparative isoelectric focusing and gel chromatography and other fractionation methods. The active forms could be distinguished by electrophoresis and isoelectric focusing on polyacrylamide gels and displayed protein heterogeneity. These forms were found in the crude extract and in the partially purified preparations in the presence or absence of proteinase inhibitors. Form II had the highest specific activity, but all three forms had the same optimum pH and Km value for histidine.


1978 ◽  
Vol 15 (6) ◽  
pp. 955-967 ◽  
Author(s):  
B.J.R. Whittle ◽  
N.K. Boughton-Smith ◽  
S. Moncada ◽  
J.R. Vane

1995 ◽  
Vol 58 (4) ◽  
pp. 421-424 ◽  
Author(s):  
Craig A. Miller ◽  
Masanobu Nakashima ◽  
George K. Gittes ◽  
Halle T. Debas

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