Trophic effects of glicentin on rat small-intestinal mucosa in vivo and in vitro

1997 ◽  
Vol 32 (3) ◽  
pp. 300-305 ◽  
Author(s):  
Satoshi Myojo ◽  
Tomoyuki Tsujikawa ◽  
Masaya Sasaki ◽  
Yoshihide Fujiyama ◽  
Tadao Bamba
Keyword(s):  
Intestinal Mucosa ◽  
Small Intestinal Mucosa ◽  
Trophic Effects ◽  
Small Intestinal

scholarly journals Dietary Fiber and Phosphorylated Oligosaccharide Protect Small Intestinal Mucosa of Rat from Oxidative Damages in vitro.

1999 ◽  
Vol 46 (7) ◽  
pp. 487-490 ◽  
Author(s):  
Makiko KAWAGUCHI ◽  
Yuko FUJIOKA ◽  
Mikako KISHIMOTO ◽  
Toshiki MATSUURA ◽  
Tomio ICHIKAWA
Keyword(s):  
Dietary Fiber ◽  
Intestinal Mucosa ◽  
Small Intestinal Mucosa ◽  
Oxidative Damages ◽  
Small Intestinal

Mo2046 Sulforaphane Protects Small Intestinal Mucosa From Indomethacin-Induced Injury in Mice via Dual Beneficial Mechanisms In Vivo

2012 ◽  
Vol 142 (5) ◽  
pp. S-727-S-728
Author(s):  
Junya Sato ◽  
Atsushi Fukumoto ◽  
Yuhei Suzuki ◽  
Akinori Yanaka
Keyword(s):  
Intestinal Mucosa ◽  
Small Intestinal Mucosa ◽  
Small Intestinal

scholarly journals Influence of ethanol on the activity of glycosidases in rats exposed to cadmium (Cd2+).

1995 ◽  
Vol 42 (3) ◽  
pp. 297-299
Author(s):  
L P Arciuch ◽  
A Omasta ◽  
K Rostkowska ◽  
M Gałazyn-Sidorczuk ◽  
J Moniuszko-Jakoniuk ◽  
...  
Keyword(s):  
Small Intestine ◽  
Intestinal Mucosa ◽  
Small Intestinal Mucosa ◽  
Distinct Effect ◽  
Small Intestinal ◽  
Beta Galactosidase

Inhibition by ethanol of the activities of lysosomal exoglycosidases in stomach, small intestine, liver and brain of rats exposed to cadmium (Cd2+) was determined. Out of the glycosidases tested the most distinct effect of Cd2+ and ethanol administered to the rats in vivo was observed in the small intestinal mucosa in a decreasing order: N-acetyl-beta-hexosaminidase, beta-galactosidase and alpha-fucosidase.

Intestinal mucosa in diabetes: synthesis of total proteins and sucrase-isomaltase

1986 ◽  
Vol 250 (6) ◽  
pp. G788-G793 ◽  
Author(s):  
W. A. Olsen ◽  
E. Perchellet ◽  
R. L. Malinowski
Keyword(s):  
Protein Synthesis ◽  
Intestinal Mucosa ◽  
Total Protein ◽  
Specific Radioactivity ◽  
Small Intestinal Mucosa ◽  
Insulin Deficiency ◽  
Intestinal Protein ◽  
Streptozotocin Induced Diabetes ◽  
Small Intestinal

The effects of insulin deficiency on nitrogen metabolism in muscle and liver have been extensively studied with recent in vivo demonstration of impaired protein synthesis in rats with streptozotocin-induced diabetes. Despite the significant contribution of small intestinal mucosa to overall protein metabolism, the effects of insulin deficiency on intestinal protein synthesis have not been completely defined. We studied the effects of streptozotocin-induced diabetes on total protein synthesis by small intestinal mucosa and on synthesis of a single enzyme protein of the enterocyte brush-border membrane sucrase-isomaltase. We used the flooding-dose technique of McNurlan, Tomkins, and Garlick (Biochem. J. 178: 373–379, 1979) to minimize the difficulties of measuring specific radioactivity of precursor phenylalanine and determined incorporation into mucosal proteins and sucrase-isomaltase 20 min after injection of the labeled amino acid. Diabetes did not alter mucosal mass as determined by weight and content of protein and DNA during the 5 days after injection of streptozotocin. Increased rates of sucrase-isomaltase synthesis developed beginning on day 3, and those of total protein developed on day 5. Thus intestinal mucosal protein synthesis is not an insulin-sensitive process.

scholarly journals Enzyme studies on the esterification of vitamin D in rat tissues

1968 ◽  
Vol 109 (3) ◽  
pp. 457-467 ◽  
Author(s):  
D. R. Fraser ◽  
E. Kodicek
Keyword(s):  
Vitamin D ◽  
Pancreatic Juice ◽  
Intestinal Mucosa ◽  
Micellar Solution ◽  
Plasma Cholesterol ◽  
Esterification Reaction ◽  
Rat Tissues ◽  
Small Intestinal Mucosa ◽  
Small Intestinal

1. The mechanism of vitamin D esterification in the rat was studied with liver, small-intestinal mucosa, pancreatic juice and blood plasma as enzyme sources and [1−3H]cholecalciferol, [U−14C]ergocalciferol and [4−14C]cholesterol as substrates. 2. No esterification of vitamin D could be detected with liver preparations nor with homogenates or acetone-dried powder extracts of intestinal mucosa. 3. Pancreatic juice esterified [1−3H]cholecalciferol with oleic acid, and specificity studies indicated that a cholesterol-esterifying enzyme was using vitamin D as substrate. 4. Plasma cholesterol-esterifying enzyme also esterified vitamin D. 5. The specificity of the esterification reaction is discussed in relation to (a) the molecular structure of the substrates and (b) their availability, in a micellar solution, to the enzyme. 6. It is concluded that cholesterol-esterifying enzymes esterify vitamin D in vivo during absorption from the small intestine and while it is transported in blood.

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