Cellular localization of gastric intrinsic factor in the rat

1964 ◽  
Vol 206 (4) ◽  
pp. 783-786 ◽  
Author(s):  
Agna Boass ◽  
T. Hastings Wilson
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Cellular Localization ◽  
Tumor Tissue ◽  
Intrinsic Factor ◽  
Close Correlation ◽  
Carbonic Anhydrase Activity ◽  
Frozen Sections ◽  
Gastric Glands ◽  
Rat Gastric Mucosa

The distribution of carbonic anhydrase, pepsinogen, and intrinsic factor (IF) was studied in frozen sections of rat gastric mucosa using the method of Holter and Linderstrøm-Lang. Carbonic anhydrase activity was greatest in the sections nearest to the surface of the mucosa and less in the deeper regions of the glands. In contrast, the levels of both IF and pepsinogen were low at the surface and continued to increase to a maximum at the base of the gastric glands. The close correlation between the distribution of the concentrations of pepsinogen and IF suggests that the chief (zymogenic) cell may be the source of IF in the stomach of the rat. No IF was detected in human carcinoid tumor tissue. This absence of IF is consistent with the view that the argentaffine cell is not the source of IF.

Variation in the pattern of carbonic anhydrase activity in the cells of the gastric glands

1974 ◽  
Vol 39 (4) ◽  
pp. 289-300 ◽  
Author(s):  
William B. Winborn ◽  
Leonard L. Seelig ◽  
Charles M. Girard
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Gastric Glands

scholarly journals Carbonic anhydrase, ultrastructural localization in the mouse gastric mucosa and improvements in the technique.

1980 ◽  
Vol 28 (6) ◽  
pp. 511-525 ◽  
Author(s):  
N Sugai ◽  
S Ito
Keyword(s):  
Electron Microscopy ◽  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Picric Acid ◽  
Ultrastructural Localization ◽  
Carbonic Anhydrase Activity ◽  
Cobalt Sulfide ◽  
Ultrastructural Studies ◽  
Mucosal Cells ◽  
Erythrocyte Carbonic Anhydrase

The ultrastructural localization of carbonic anhydrase activity in mouse gastric mucosal cells as revealed by the cobalt bicarbonate histochemical method of Hansson has been made. In addition the effects of fixatives used for ultrastructural studies have been evaluated for reduction of carbonic anhydrase activity; exogenous erythrocyte carbonic anhydrase has been localized in tissues; acetazolamide and potassium cyanate inhibition of activity demonstrated; and an improved method for the osmication of reacted tissues for electron microscopy has been developed. The results indicate that the glutaraldehyde, formaldehyde, picric acid fixative, which retains about 5% of the original carbonic anhydrase activity, is distinctly better for histochemical studies than formaldehyde fixation, which retains about 32% activity. Acetazolamide at 10(-5) M consistently inhibits histochemical reaction, as does 20 mM KCNO, in the incubation medium. Exogenous carbonic anhydrase is readily visualized by the histochemical technique. Electron microscopy of gastric mucosa reacted for carbonic anhydrase activity indicates the focal deposition of the cobalt sulfide reaction product in the cores of microvilli lining the intracellular canaliculi, in the basal and lateral cell folds of parietal cells, and in the microvilli as well as the cytoplasm between mucous granules in the surface mucous cells. In addition, some reaction product was found in the mitochondrial cristae and in some nuclei and intercellular spaces.

scholarly journals CELLULAR LOCALIZATION OF CARBONIC ANHYDRASE IN AVIAN TISSUES BY LABELED INHIBITOR AUTORADIOGRAPHY

1973 ◽  
Vol 21 (8) ◽  
pp. 693-702 ◽  
Author(s):  
CAROL V. GAY ◽  
WERNER J. MUELLER
Keyword(s):  
Carbonic Anhydrase ◽  
Cellular Localization ◽  
Carbonic Anhydrase Activity ◽  
The Body ◽  
Interstitial Tissue ◽  
Light Microscope Level ◽  
Freeze Dried ◽  
Collecting Tubules ◽  
Columnar Cells ◽  
Lymphoid Nodules

Carbonic anhydrase was localized at the light microscope level using labeled inhibitor autoradiography. Laying hens, 10-day-old chicks and adult female Japanese quail received injections of 1-25 µC 3H-acetazolamide/g body weight. After 3 hr (quail) and 24 hr (hen and chick), 2-mm3 pieces of tissue were removed under anesthesia, frozen at –160°C, freeze-dried, fixed with OsO4 vapor, embedded in Epon, sectioned at 1 µ and covered with NTB-2 emulsion. The following results validate the method: (a) the concentration of acetazolamide was 100 times greater in red blood cells than in plasma 24 hr after injection in the hen, indicating that free and loosely bound acetazolamide was rapidly cleared from the body; (b) no significant amounts of label were found in muscle, cartilage, adipose tissue and nuclei, which have no carbonic anhydrase activity; (c) except for the pancreas, there was good agreement among the grain counts for the different classes of birds; and (d) the autoradiographic localizations were in general agreement with concepts of tissue function. Carbonic anhydrase was localized in: the proximal, distal, collecting tubules and the mesangium of the kidney; the acinar, but not the centroacinar, cells of the pancreas; the tubular glands and the columnar cells of the shell gland; the lining cells, but not the zymogenic cells, of the proventriculus; erythrocytes; erythroblasts; heterophils; and lymphoid nodules, but not in fat and interstitial tissue of bone marrow.

Cyclooxygenase-2 selective inhibition meloxicam-induced is correlated with gastric mucosa carbonic anhydrase activity

2000 ◽  
Vol 118 (4) ◽  
pp. A1296-A1297
Author(s):  
Ioan Puscas ◽  
Adrian Maghiar ◽  
Marcela Coltau ◽  
Teodor Maghiar ◽  
Ioan I. Puscas ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Selective Inhibition ◽  
Carbonic Anhydrase Activity ◽  
Cyclooxygenase 2

Distribution of smg p25A and smg p21s, ras p21-like guanine nucleotide-binding proteins, in the rat stomach

1992 ◽  
Vol 262 (1) ◽  
pp. G69-G73
Author(s):  
K. Matsuda ◽  
C. Sakamoto ◽  
O. Nakano ◽  
Y. Konda ◽  
T. Matozaki ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Binding Proteins ◽  
Nucleotide Binding ◽  
Guanine Nucleotide ◽  
Gastric Glands ◽  
Rat Gastric Mucosa ◽  
Ras P21 ◽  
Guanine Nucleotide Binding ◽  
Nucleotide Binding Proteins ◽  
Guanine Nucleotide Binding Proteins

Existence and distribution of small guanine nucleotide binding proteins (G proteins) such as smg p25A, smg p21s, and ras p21s were examined in the rat gastric mucosa. By immunoblot analysis using the specific monoclonal antibodies against smg p25A and ras p21 and the anti-smg p21 antiserum, smg p25A and smg p21s were detected in the gastric mucosa, while ras p21s were not detected. In immunocytochemical studies, moderate fluorescence of smg p25A was homogenously seen in the cytoplasmic portions of chief cells and surface epithelial cells. smg p21 immunoreactivity was detected in glandular cells and submucosal muscle layer in the mucosa. On the other hand, the cells constituting gastric glands were unstained with the anti-ras p21 monoclonal antibody, RASK-4. These results suggest that smg p25A and smg p21s exist as in other tissues and might exert their specific actions in the rat gastric mucosa.

Effect of Sympathectomy and Vagotomy on Carbonic Anhydrase Activity, Oxidative Phosphorylation, High Energy Phosphates Content and Electrolytes Content of the Gastric Mucosa

1958 ◽  
Vol 192 (3) ◽  
pp. 476-478 ◽  
Author(s):  
Takeshi Yakushiji ◽  
Tetsuya Kikuchi ◽  
Junichi Yamamoto ◽  
Kaname Kuriaki
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Oxidative Phosphorylation ◽  
High Energy ◽  
Carbonic Anhydrase Activity ◽  
High Energy Phosphates

Sympathectomy enhanced carbonic anhydrase activity, increased the rate of oxidative phosphorylation and the ATP and potassium contents of the canine gastric mucosa. Vagotomy was essentially without effect.

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