scholarly journals Proteolytic Activity of Human Gastric Mucosa. I

1951 ◽  
Vol 53 (3-4) ◽  
pp. 243-249 ◽  
Author(s):  
Mitsuhisa Hayakawa
Keyword(s):  
Gastric Mucosa ◽  
Proteolytic Activity ◽  
Human Gastric Mucosa

scholarly journals The isolation and properties of a non-pepsin proteinase from human gastric mucosa

1978 ◽  
Vol 169 (3) ◽  
pp. 617-624 ◽  
Author(s):  
N B Roberts ◽  
W H Taylor
Keyword(s):  
Bone Marrow ◽  
Gastric Mucosa ◽  
Gastric Adenocarcinoma ◽  
Proteolytic Activity ◽  
Structural Characteristics ◽  
Human Gastric Mucosa ◽  
Cathepsin E ◽  
Activity Curve ◽  
Rabbit Bone ◽  
Ph Range

1. A non-pepsin proteinase, proteinase 2, was successfully isolated free from pepsinogen (by repetitive chromatography on DEAE- and CM-celluloses) from the gastric mucosa of a patient with a duodenal ulcer and the uninvaded mucosa of a patient with a gastric adenocarcinoma. 2. Proteinases 1a and 1b, found in gastric adenocarcinoma, were not found in the gastic mucosa of these patients. 3. Proteinase 2 was shown to have an asymmetrical broad pH-activity curve with a maximum over the pH range 3.0-3.7. 4. Proteolytic activity of proteinase 2 was inhibited by pepstatin; the concentration of pepstatin giving 50% inhibition is of the order of 3nm. 5. Inhibition of proteolytic activity by carbenoxolone and related triterpenoids indicated that at pH 4.0 proteinase 2 possesses structural characteristics relating it to the pepsins and at pH 7.4 to the pepsinogens. 6. The sites of cleavage of the B-chain of oxidized insulin for proteinase 2 at pH 1.7 and pH 3.5 were shown to be similar to those previously established for human pepsin 3 and for the cathepsin E of rabbit bone marrow. 7. The non-pepsin proteinase 2 (cathepsin) of human gastric mucosa has properties more similar to cathepsin E than to the cathepsins D.

Sem Observations in Gastric Mucosa Exposed to Progressive Enzymatic Etching

1980 ◽  
Vol 38 ◽  
pp. 570-571
Author(s):  
C.A.E. Lemmi ◽  
D. Booth ◽  
G.E. Adomian
Keyword(s):  
Gastric Mucosa ◽  
Critical Point ◽  
Proteolytic Activity ◽  
Etching Process ◽  
Cellular Types

In order to enrich populations of homogeneous cellular types we dissociated gastric mucosa by enzymatic techniques. In addition, we used SEM to monitor the progressive etching of the mucosa. Two enzymes were tested: collagenase III with minimum proteolytic activity and Pronase with broader proteolytic effects. The gastric mucosa was exposed to the effect of the enzymes using everted stomach preparations. In this way the digestive action occured progressively from the lumen of the stomach toward the base of the glands. This “etching” process could be monitored conveniently by SEM. After incubation for periods varying from 30 to 210 minutes the tissues were stretched on dental wax, fixed in 2 % glutaralheyde, post-fixed in osmium, dehydrated, critical point dryed and coated with gold. A model MSM-5 “Mini-SEM” was used for observation. Gentle uncurling of the preparation before coating with gold produced fractures which revealed the structure of the gastric glandsin more detail.

H. pylori down-regulates TRAIL (DR4)-receptors in the human gastric mucosa, a possible mechanism for chronic persistence

2001 ◽  
Vol 120 (5) ◽  
pp. A81-A81
Author(s):  
B NEU ◽  
R RAD ◽  
M NEUHOFER ◽  
C TRAUTWEIN ◽  
M GERHARD ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Human Gastric Mucosa ◽  
H Pylori

scholarly journals Purification and Properties of Acid Deoxyribonucleases of Human Gastric Mucosa and Cervix Uteri

1974 ◽  
Vol 249 (12) ◽  
pp. 3884-3889 ◽  
Author(s):  
Masayoshi Yamanaka ◽  
Yoriaki Tsubota ◽  
Motoaki Anai ◽  
Koji Ishimatsu ◽  
Makoto Okumura ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Cervix Uteri ◽  
Human Gastric Mucosa ◽  
Purification And Properties

scholarly journals Relation of Helicobacter pylori to the human gastric mucosa in chronic gastritis of the antrum.

Gut ◽  
1990 ◽  
Vol 31 (11) ◽  
pp. 1230-1236 ◽  
Author(s):  
L L Thomsen ◽  
J B Gavin ◽  
C Tasman-Jones
Keyword(s):  
Helicobacter Pylori ◽  
Gastric Mucosa ◽  
Chronic Gastritis ◽  
Human Gastric Mucosa

Succinic and Malic Oxidase in Gastric Hydrochloric Acid Production

1956 ◽  
Vol 187 (3) ◽  
pp. 427-431 ◽  
Author(s):  
Joseph J. Vitale ◽  
Oscar M. Jankelson ◽  
Patricia Connors ◽  
D. Mark Hegsted ◽  
Norman Zamcheck
Keyword(s):  
Gastric Mucosa ◽  
Guinea Pig ◽  
Succinic Dehydrogenase ◽  
Titratable Acidity ◽  
Spectrophotometric Analysis ◽  
Parietal Cells ◽  
Human Gastric Mucosa ◽  
City Hospital ◽  
Malic Dehydrogenase ◽  
Oxidase System

Effect of histamine on the activity of succinic oxidase and malic dehydrogenase was studied in guinea pig and human gastric mucosa. Human tissue was obtained through the surgical services of the Boston City Hospital. Control value for the succinic oxidase system of the proximal half of the guinea pig stomach was approximately 480 ( Qo2 (N) (µl O2/mg nitrogen/hr.)). After histamine, this value rose to 550 in 30 minutes with a simultaneous rise in titratable acidity of the stomach contents. Animals fasted for 72 hours had a Qo2 (N) of approximately 500 and after histamine a Qo2 (N) of 700 was observed. Spectrophotometric analysis of succinic dehydrogenase and cytochrome oxidase activities, two of the major components of the succinic oxidase system, revealed that both components are increased following histamine administration. Malic dehydrogenase, however, was not affected by histamine treatment. Succinic dehydrogenase was demonstrated by histochemical localization and was concentrated below the superficial mucous layer where parietal cells were abundant. Succinic oxidase activity of human gastric mucosa was demonstrable only in those specimens containing abundant parietal cells. This study confirms the view that HCl production by parietal cells is associated with aerobic metabolism and is perhaps under enzymatic control. The study suggests that the succinic oxidase system may be involved in the production or secretion of HCl.

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