Dietary regulation of rat intestinal angiotensin-converting enzyme and dipeptidyl peptidase IV

1993 ◽  
Vol 264 (6) ◽  
pp. G1153-G1159 ◽  
Author(s):  
Y. Suzuki ◽  
R. H. Erickson ◽  
A. Sedlmayer ◽  
S. K. Chang ◽  
Y. Ikehara ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Fold Increase ◽  
Immunoblot Analysis ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Converting Enzyme ◽  
Brush Border Membranes ◽  
Dpp Iv

The small intestinal brush-border membrane contains several peptidases that are involved in the hydrolysis of dietary peptides containing proline. A high-proline (gelatin) diet was administered to one of several groups of rats to study its possible regulatory effect on levels of two prolyl peptidases, namely angiotensin-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP IV). Groups of rats were maintained on isocaloric diets containing either low (4%), normal (17%), or high (50%) protein (casein) or high (50%) gelatin. After 7 days, brush-border membranes and total RNA were prepared from the small intestine. ACE activity was 3- to 10-fold higher in brush-border membranes from the gelatin group compared with the low-protein group. DPP IV exhibited a three- to sixfold increase. Immunoblot analysis of brush-border membrane-associated ACE protein indicated a six- to eightfold increase in the high-gelatin group. There was also a 1.5- to 3-fold increase in steady-state levels of ACE and DPP IV mRNA. These results suggest that a diet high in proline (gelatin) is particularly effective in increasing intestinal levels of these two enzymes.

scholarly journals Investigation into the bioavailability of milk protein-derived peptides with dipeptidyl-peptidase IV inhibitory activity using Caco-2 cell monolayers

2017 ◽  
Vol 8 (2) ◽  
pp. 701-709 ◽  
Author(s):  
Isabelle M. E. Lacroix ◽  
Xiu-Min Chen ◽  
David D. Kitts ◽  
Eunice C. Y. Li-Chan
Keyword(s):  
Biological Activity ◽  
Brush Border ◽  
Inhibitory Activity ◽  
Milk Protein ◽  
Brush Border Membrane ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Cell Monolayers ◽  
Dpp Iv

The present study used Caco-2 cell monolayers to investigate the bioavailability of milk protein-derived peptides with DPP-IV inhibitory activity and showed that the susceptibility of the peptides to brush border membrane peptidases impacts their biological activity.

Angiotensin converting enzyme in brush-border membranes of avian small intestine

1988 ◽  
Vol 135 (1) ◽  
pp. 1-8
Author(s):  
B. R. Stevens ◽  
A. Fernandez ◽  
C. del Rio Martinez
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Brush Border ◽  
Physiological Role ◽  
Intestinal Epithelial ◽  
Converting Enzyme ◽  
Brush Border Membranes ◽  
Fluid Uptake ◽  
The Common ◽  
Kinetics Of ◽  
Hydrolysis Of

Angiotensin converting enzyme activity was identified in brush-border membranes purified from the small intestinal epithelium of the common grackle, Quiscalus quiscula. Angiotensin converting enzyme was enriched 20-fold in the membrane preparation, compared with intestinal epithelial cell scrapes, and was coenriched with the brush-border markers, alkaline phosphatase and aminopeptidase N. The kinetics of hydrolysis of N-[3-(2-furyl)acryloyl]-L-phenylalanylglycylglycine (FAPGG) gave a Vmax of 907 +/− 41 units g-1 and a Km of 55 +/− 6 mumol l-1. The avian intestinal angiotensin converting enzyme was inhibited by the antihypertensive drug, Ramipril, with a median inhibitory concentration (IC50) of 1 nmol l-1. In the light of previous studies on angiotensin converting enzyme in mammalian epithelia, these results may implicate a physiological role for angiotensin converting enzyme in regulating electrolyte and fluid uptake in bird small intestines.

Role of rat intestinal brush-border membrane angiotensin-converting enzyme in dietary protein digestion

1987 ◽  
Vol 253 (6) ◽  
pp. G781-G786 ◽  
Author(s):  
M. Yoshioka ◽  
R. H. Erickson ◽  
J. F. Woodley ◽  
R. Gulli ◽  
D. Guan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Angiotensin Converting Enzyme ◽  
Brush Border ◽  
Dietary Protein ◽  
Brush Border Membrane ◽  
Biologically Active ◽  
Converting Enzyme ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border

The role of rat intestinal angiotensin-converting enzyme (ACE; E.C 3.4.15.1) in the digestion and absorption of dietary protein was investigated. Enzyme activity was associated with the brush-border membrane fraction, with the highest activity in the proximal to midregion of the small intestine. Preliminary enzyme characterization studies were carried out using purified brush-border membrane preparations. When a variety of N-blocked synthetic peptides were used as potential substrates for ACE, activity was highest with those containing proline at the carboxy terminal position. The hydrolytic rates observed with these prolyl peptides were comparable to those observed when major digestive peptidases of the brush-border membrane such as aminopeptidase N and dipeptidyl aminopeptidase IV were assayed. When isolated rat jejunum was perfused in vivo with solutions of Bz-Gly-Ala-Pro, the dipeptide Ala-Pro was the main hydrolytic product detected in the perfusates. Absorption rates of the constituent amino acids, alanine and proline, depended on the concentration of peptide perfused. Captopril, an active site specific ACE inhibitor, significantly inhibited hydrolysis and absorption of constituent amino acids from Bz-Gly-Ala-Pro. These results show that intestinal brush-border membrane ACE functions as a digestive peptidase in addition to its role as a regulator of biologically active peptides in other tissues.

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