Biomaterial Database

Effect of alloxan-induced diabetes on intestinal peptidases in the rat. 1978

C Arvanitakis, and J Folscroft, and G Stitt

Intestinal transport of amino aicds, similar to sugar absorption, is enhanced in experimental diabetes. Because peptidases play a significant role in peptide digestion, we examined the effect of diabetes on intestinal peptidases. Leucyl-naphthylamidase and leucyl-glycine hydrolase (brush border peptidases) and prolyl-glycine hydrolase (cytosol peptidase) were assayed in the brush border and cytosol fraction in diabetic rats 7 days after alloxan administration. Mucosal weight, protein concentration, and total and specific activity of leucyl-naphthylamidase and leucyl-glycine hydrolase were significantly increased in diabetes in the brush border but not in cytosol fraction. By contrast, prolyl-glycine hydrolasw was not affected in cytosol fraction or brush border. These data indicate that brush border peptidases are increased in experimental diabetes. This adaptive response of the small intestinal mucosa is similar to disaccharidase elevation and alteration in the intestinal absorptive function which occurs in experimental diabetes.

UI	MeSH Term	Description	Entries
D007422	Intestines	The section of the alimentary canal from the STOMACH to the ANAL CANAL. It includes the LARGE INTESTINE and SMALL INTESTINE.	Intestine
D007931	Leucyl Aminopeptidase	A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.	Cytosol Aminopeptidase,Leucine Aminopeptidase,L-Leucylnaphthylamidase,Methoxyleucine Aminopeptidase,Peptidase S,Zinc-Manganese-Leucine Aminopeptidase,Aminopeptidase, Cytosol,Aminopeptidase, Leucine,Aminopeptidase, Leucyl,Aminopeptidase, Methoxyleucine,Aminopeptidase, Zinc-Manganese-Leucine,Zinc Manganese Leucine Aminopeptidase
D008297	Male		Males
D008871	Microvilli	Minute projections of cell membranes which greatly increase the surface area of the cell.	Brush Border,Striated Border,Border, Brush,Border, Striated,Borders, Brush,Borders, Striated,Brush Borders,Microvillus,Striated Borders
D010447	Peptide Hydrolases	Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.	Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D003600	Cytosol	Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.	Cytosols
D003921	Diabetes Mellitus, Experimental	Diabetes mellitus induced experimentally by administration of various diabetogenic agents or by PANCREATECTOMY.	Alloxan Diabetes,Streptozocin Diabetes,Streptozotocin Diabetes,Experimental Diabetes Mellitus,Diabete, Streptozocin,Diabetes, Alloxan,Diabetes, Streptozocin,Diabetes, Streptozotocin,Streptozocin Diabete
D004150	Dipeptidases	EXOPEPTIDASES that specifically act on dipeptides. EC 3.4.13.
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D051381	Rats	The common name for the genus Rattus.	Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus