Immunolocalization of gastrin-dependent histidine decarboxylase activity in rat gastric mucosa during feeding

1998 ◽  
Vol 275 (4) ◽  
pp. G660-G667 ◽  
Author(s):  
Gordon V. Ohning ◽  
Min Song ◽  
Helen C. Wong ◽  
S. Vincent Wu ◽  
John H. Walsh
Keyword(s):  
Enzyme Activity ◽  
Histidine Decarboxylase ◽  
Gastric Gland ◽  
Decarboxylase Activity ◽  
Rapid Reduction ◽  
Oxyntic Mucosa ◽  
Ecl Cells ◽  
Rat Gastric Mucosa ◽  
Fasting And Refeeding ◽  
Atropine Treatment

The localization of histidine decarboxylase (HDC) activity in the enterochromaffin-like (ECL) cells of the oxyntic mucosa was studied during fasting and refeeding using monoclonal (CURE no. 44178) and polyclonal (CURE no. 94211) antibodies directed against the COOH terminus of HDC (HDC-CT). Changes in HDC immunostaining were correlated with mucosal HDC enzyme activity. Immunoneutralization of circulating gastrin and atropine treatment during refeeding were used to determine the relative importance of gastrin and cholinergic mechanisms in the regulation of HDC activity and immunostaining. Fasting caused a rapid reduction in the number of ECL cells immunostaining for HDC that was correlated with an almost complete loss of mucosal HDC enzyme activity. Refeeding restored both HDC immunostaining and enzyme activity within 2–4 h, and this response was inhibited by gastrin immunoneutralization but not by atropine treatment. Immunostaining was uniformly decreased and restored in the lower half of the oxyntic mucosa, which corresponds to the predominant area of ECL cells in the gastric gland. Histamine immunostaining and mucosal histamine content were not significantly changed during fasting and refeeding or by gastrin antibody and/or atropine treatment during refeeding. These findings indicate that HDC activity correlates with HDC-CT immunostaining and that both HDC activity and HDC-CT immunostaining are regulated by gastrin during refeeding.

Ornithine decarboxylase in rat small intestine: stimulation with food or insulin

1976 ◽  
Vol 231 (5) ◽  
pp. 1557-1561 ◽  
Author(s):  
DV Maudsley ◽  
J Leif ◽  
Y Kobayashi
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Ornithine Decarboxylase ◽  
Diamine Oxidase ◽  
Actinomycin D ◽  
Histidine Decarboxylase ◽  
Decarboxylase Activity ◽  
Adenosylmethionine Decarboxylase ◽  
Diamine Oxidase Activity ◽  
Similarities And Differences

Ornithine decarboxylase in the small intestine of starved rats was stimulated 3- to 10-fold by refeeding or administration of insulin. A peak is observed 3-5 h following treatment after which the enzyme activity rapidly declines. The rise in ornithine decarboxylase is reduced by actinomycin D or cycloheximide. The increase in enzyme activity occurs mainly in the duodenum and jejunum with less than a twofold change being observed in the ileum. A small (twofold) increase in S-adenosylmethionine decarboxylase activity in the small intestine was observed after food, but there was no change in diamine oxidase activity. Whereas pentagastrin and metiamide administration markedly stimulated histidine decarbosylase in the gastric mucosa, no consistent effect of these agents on ornithine decarboxylase in the small intestine was observed. The similarities and differences between histidine decarboxylase and ornithine decarboxylase are discussed.

Differentiation of the Gastric Mucosa I. Role of histamine in control of function and integrity of oxyntic mucosa: understanding gastric physiology through disruption of targeted genes

2006 ◽  
Vol 291 (4) ◽  
pp. G539-G544 ◽  
Author(s):  
Duan Chen ◽  
Takeshi Aihara ◽  
Chun-Mei Zhao ◽  
Rolf Håkanson ◽  
Susumu Okabe
Keyword(s):  
Gastric Mucosa ◽  
Histidine Decarboxylase ◽  
Parietal Cells ◽  
Oxyntic Mucosa ◽  
Mucosal Integrity ◽  
Ecl Cells ◽  
Gastric Physiology ◽  
Ecl Cell ◽  
Insight Into

Many physiological functions of the stomach depend on an intact mucosal integrity; function reflects structure and vice versa. Histamine in the stomach is synthesized by histidine decarboxylase (HDC), stored in enterochromaffin-like (ECL) cells, and released in response to gastrin, acting on CCK2 receptors on the ECL cells. Mobilized ECL cell histamine stimulates histamine H2 receptors on the parietal cells, resulting in acid secretion. The parietal cells express H2, M3, and CCK2 receptors and somatostatin sst2 receptors. This review discusses the consequences of disrupting genes that are important for ECL cell histamine release and synthesis (HDC, gastrin, and CCK2 receptor genes) and genes that are important for “cross-talk” between H2 receptors and other receptors on the parietal cell (CCK2, M3, and sst2 receptors). Such analysis may provide insight into the functional significance of gastric histamine.

Ischemia of rat stomach mobilizes ECL cell histamine

2005 ◽  
Vol 288 (5) ◽  
pp. G1084-G1090 ◽  
Author(s):  
Masayuki Kitano ◽  
Maria Bernsand ◽  
Yosuke Kishimoto ◽  
Per Norlén ◽  
Rolf Håkanson ◽  
...  
Keyword(s):  
Histidine Decarboxylase ◽  
Ischemia Reperfusion ◽  
Celiac Artery ◽  
Enzyme Linked Immunosorbent Assay ◽  
Decarboxylase Activity ◽  
Rat Stomach ◽  
Ecl Cells ◽  
Ecl Cell ◽  
Mucosal Lesions ◽  
Histidine Decarboxylase Activity

Microdialysis was used to study how ischemia-evoked gastric mucosal injury affects rat stomach histamine, which resides in enterochromaffin-like (ECL) cells and mast cells. A microdialysis probe was inserted into the gastric submucosa, and the celiac artery was clamped (30 min), followed by removal of the clamp. Microdialysate histamine was determined by enzyme-linked immunosorbent assay. In addition, we studied the long-term effects of ischemia on the oxyntic mucosal histidine decarboxylase activity in omeprazole-treated rats. Gastric mucosal lesions induced by the ischemia were enlarged on removal of the clamp. The microdialysate histamine concentration increased immediately on clamping (50-fold rise within 30 min) and declined promptly after the clamp was removed. In contrast, histidine decarboxylase activity of the ECL cells was lowered by the ischemia and returned to preischemic values 9 days later. Mast cell-deficient rats responded to ischemia-reperfusion much like wild-type rats with respect to histamine mobilization. Pretreatment with the irreversible inhibitor of histidine decarboxylase, α-fluoromethylhistidine, which is known to eliminate histamine from ECL cells, prevented the rise in microdialysate histamine. Pharmacological blockade of acid secretion (cimetidine or omeprazole) prevented the lesions induced by ischemia-reperfusion insult but not the mobilization of histamine. In conclusion, ischemia of the celiac artery mobilizes large amounts of histamine from ECL cells, which occurs independently of the gross mucosal lesions. The prompt reduction of the mucosal histidine decarboxylase activity in response to ischemia probably reflects ECL cell damage. The lesions develop not because of mobilization of histamine per se but because of ischemia plus reperfusion plus gastric acid.

scholarly journals Leukocyte Histidine Decarboxylase: Properties and Activity in Myeloproliferative Disorders

Blood ◽  
1968 ◽  
Vol 31 (6) ◽  
pp. 699-709 ◽  
Author(s):  
STEPHEN KRAUSS ◽  
HARRIET S. GILBERT ◽  
LOUIS R. WASSERMAN ◽  
Gertrude Lurinsky
Keyword(s):  
Enzyme Activity ◽  
Cellular Localization ◽  
Pyridoxal Phosphate ◽  
Histidine Decarboxylase ◽  
Myeloproliferative Disorders ◽  
Control Group ◽  
Acid Decarboxylase ◽  
Decarboxylase Activity ◽  
Myeloid Metaplasia ◽  
Histidine Decarboxylase Activity

Abstract 1. Histidine decarboxylase was assayed in extracts from human leukocytes and the properties of the enzyme studied. 2. Leukocyte histidine decarboxylase was found to be substrate-specific, to require pyridoxal phosphate as co-enzyme, and to be inhibited by alpha-hydrazino analog of histidine (MK 785), a selective inhibitor of the specific histidine decarboxylase occuring in rat tissue. A non-specific L-aromatic amino acid decarboxylase was also demonstrated in leukocyte extracts, which possessed little activity toward histidine. 3. Cellular localization studies revealed that mature neutrophils and basophils possessed most of the histidine decarboxylase activity exhibited by mixed leukocyte preparations. Mature eosinophils, small lymphocytes, and immature myeloid cells (myeloblasts and promyelocytes) showed little histidine decarboxylase activity. 4. In the clinical studies, patients with uncontrolled polycythemia vera, "spent" polycythemia, myelofibrosis with myeloid metaplasia, and chronic myelocytic leukemia, showed increased leukocyte enzyme activity when compared to a control group composed of normal subjects and patients with relative polycythemia. This increased activity appears to represent a true increase in enzyme activity per granulocyte, and is believed to account for the elevated leukocyte histamine content demonstrated in patients with myeloproliferative disorders.

Gastrin regulates histidine decarboxylase activity and mRNA abundance in rat oxyntic mucosa

1994 ◽  
Vol 267 (2) ◽  
pp. G254-G258 ◽  
Author(s):  
A. K. Sandvik ◽  
R. Dimaline ◽  
R. Marvik ◽  
E. Brenna ◽  
H. L. Waldum
Keyword(s):  
Enzymatic Activity ◽  
Histidine Decarboxylase ◽  
Serum Gastrin ◽  
Mrna Abundance ◽  
Decarboxylase Activity ◽  
Oxyntic Mucosa ◽  
Trophic Effect ◽  
Ecl Cell ◽  
Release Histamine ◽  
Different Doses

Gastrin release histamine from the oxyntic mucosa, stimulates the enzymatic activity of histidine decarboxylase (HDC), increases HDC mRNA abundance, and has a trophic effect on the enterochromaffin-like (ECL) cell. In the present study, we examined the effect of exogenous gastrin on HDC activity and mRNA and the time scale of increase and decline of HDC activity and mRNA. Rats received intravenous infusion of gastrin-(1-17) in different doses or periods of time. Oxyntic mucosal HDC activity and mRNA abundance increased significantly with serum gastrin concentrations in the physiological range. The onset of response was rapid and maximal for both parameters after 2 h. Poststimulatory decrease was maximal 2 h after cessation of gastrin infusion. Those observations suggest that HDC enzymatic activity and mRNA abundance are important in meal-to-meal regulation of gastric secretion. Furthermore, HDC enzymatic activity and mRNA abundance varied in parallel, indicating that HDC mRNA abundance is important in the overall regulation of gastric mucosal HDC activity.

scholarly journals Histamine-storing cells in the oxyntic mucosa of the rat stomach: a transmission electron microscopic study employing fixation with carbodiimide.

1993 ◽  
Vol 41 (9) ◽  
pp. 1405-1412 ◽  
Author(s):  
M J Nissinen ◽  
P Panula
Keyword(s):  
Gastric Mucosa ◽  
Endocrine Cells ◽  
Cell Types ◽  
Rat Stomach ◽  
Electron Microscopic ◽  
Oxyntic Mucosa ◽  
Ecl Cells ◽  
Transmission Electron ◽  
Basal Half ◽  
Rat Gastric Mucosa

We studied the distribution of histamine (HA) immunoreactivity in endocrine cells of the acid-producing mucosa in rat stomach with pre-embedding immunoelectron microscopy (IEM) using an antiserum against HA. Four fixation modifications were compared to optimize the ultrastructural morphology and staining pattern with the antisera produced against carbodiimide-conjugated HA. Fixation with 4% 1-ethyl-3(3-dimethyl-aminopropyl) carbodiimide (EDCDI) combined with both 4% paraformaldehyde and 0.1% glutaraldehyde gave superior results compared with EDCDI alone. Enterochromaffin-like (ECL) cells were easily distinguished from other endocrine cells in optimally fixed samples. The peroxidase end-product was distributed within the cytoplasm surrounding the vesicles of the ECL cells. ECL cells comprised about 75% of all endocrine cells, and about 90% of them were HA immunoreactive (HA-IR). No other HA-IR cell types were identified by EM in the basal half of the oxyntic region of rat gastric mucosa. The results suggest that a combination of EDCDI and aldehydes is suitable for IM demonstration of HA in cells. ECL cells from a predominant portion of endocrine cells in the oxyntic glands and may constitute the only significant non-mast cell store of HA in rat gastric mucosa.

Relationship of induced histidine decarboxylase activity and histamine synthesis to shock from stress and from endotoxin

1960 ◽  
Vol 198 (6) ◽  
pp. 1187-1192 ◽  
Author(s):  
Richard W. Schayer
Keyword(s):  
Enzyme Activity ◽  
Blood Vessels ◽  
Histidine Decarboxylase ◽  
Lethal Dose ◽  
Decarboxylase Activity ◽  
Living Animal ◽  
Histamine Synthesis ◽  
Mouse Tissues ◽  
Relationship Of ◽  
Histidine Decarboxylase Activity

The activity of histidine decarboxylase of various mouse tissues is increased by stress, by epinephrine and by endotoxins. Enzyme activity reaches a maximum in about 6 hours following a stimulus and returns essentially to normal within 1 day. In mice given a lethal dose of endotoxin, enzyme activity is at its highest observed level when the animals become moribund. Evidence is presented that the elevated enzyme activites reflect an increased rate of histamine synthesis in the living animal. The hypothesis of a homeostatic relationship between newly synthesized histamine and the catecholamines, which during intense stress can suffer imbalance, affords a reasonable explanation for the events observed in the small blood vessels during development of shock, for the damaging effects of epinephrine in endotoxin-treated animals and for a number of other phenomena related to shock.

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