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.

Regulation of rat stomach histidine decarboxylase activity by the serum gastrin concentration

1973 ◽  
Vol 3 (3) ◽  
pp. 178-179 ◽  
Author(s):  
R. Håkanson ◽  
G. Liedberg ◽  
J. Oscarson ◽  
J. F. Rehfeld ◽  
F. Stadil
Keyword(s):  
Histidine Decarboxylase ◽  
Serum Gastrin ◽  
Decarboxylase Activity ◽  
Rat Stomach ◽  
Serum Gastrin Concentration ◽  
Histidine Decarboxylase Activity

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.

Rat stomach ECL-cell histidine decarboxylase activity is suppressed by ergocalciferol but unaffected by parathyroid hormone and calcitonin

1999 ◽  
Vol 79 (2-3) ◽  
pp. 131-139 ◽  
Author(s):  
Rebecca Gagnemo-Persson ◽  
Per Persson ◽  
Tomas Bryngelsson ◽  
Britt Greén ◽  
Rolf Håkanson
Keyword(s):  
Parathyroid Hormone ◽  
Histidine Decarboxylase ◽  
Decarboxylase Activity ◽  
Rat Stomach ◽  
Ecl Cell ◽  
Histidine Decarboxylase Activity

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.

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.

Comparison between activation of ornithine decarboxylase and histidine decarboxylase in rat stomach

1996 ◽  
Vol 270 (3) ◽  
pp. G476-G486 ◽  
Author(s):  
X. Q. Ding ◽  
D. Chen ◽  
E. Rosengren ◽  
L. Persson ◽  
R. Hakanson
Keyword(s):  
Food Intake ◽  
Ornithine Decarboxylase ◽  
Histidine Decarboxylase ◽  
Serum Gastrin ◽  
Oral Treatment ◽  
Somatostatin Analogue ◽  
Rat Stomach ◽  
Oxyntic Mucosa ◽  
Serum Gastrin Concentration ◽  
Fasted Rats

We compared the responses of rat stomach ornithine decarboxylase (ODC) and histidine decarboxylase (HDC) to food intake, oral treatment with antisecretagogues, NaHCO3, and hypertonic NaCl, antrectomy, intravenous infusion of gastrin-17, the selective cholecystokinin (CCK)-B/gastrin receptor antagonist L-365,260, and the somatostatin analogue RC-160. The serum gastrin concentration and oxyntic mucosal ODC and HDC activities were higher in freely fed rats than in fasted rats. Food intake in fasted rats raised the serum gastrin concentration and the ODC and HDC activities. Ranitidine, omeprazole, and NaHCO3 raised the serum gastrin concentration and activated ODC and HDC. Hypertonic NaCl raised the ODC activity 200-fold, whereas circulating gastrin and HDC activity were increased only moderately. Infusion of gastrin-17 activated HDC but not ODC. L-365,260 prevented the activation of HDC but not of ODC in response to food intake and treatment with omeprazole, NaHCO3, or hypertonic NaCl. Antrectomy prevented the food- and omeprazole-evoked rise in oxyntic mucosal HDC activity but not the rise in ODC activity. RC-160 suppressed HDC activity after food intake and treatment with omeprazole, NaHCO3, or NaCl. In contrast, RC-160 suppressed omeprazole- and NaHCO3-evoked ODC activation but not that evoked by food intake or NaCl. The results support the view that HDC in the oxyntic mucosa is activated by gastrin and suppressed by somatostatin. The induction of ODC is not mediated by gastrin; ODC activation appears to be related to acid inhibition per se or to mucosal maintenance and repair; somatostatin, or rather the lack of it, might contribute to the induction of ODC after acid blockade. The mechanism behind the activation of rat stomach ODC seems to differ depending on the type of stimulus.

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