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Author(s): Naim HY
Title: Secretion of human intestinal angiotensin-converting enzyme and its association with the differentiation state of intestinal cells
Source: BIOCHEMICAL JOURNAL 316: 259-264
Date: 1996 MAY 15
Document Type: Journal : Article
DOI:
Language: English
Comment:
Address:
Reprint: Naim, HY, UNIV DUSSELDORF,INST MICROBIOL,PROT SECRET GRP,UNIV STR
1,D-40225 DUSSELDORF,GERMANY. E-mail:
Author Keywords:
KeyWords Plus: MEMBRANE GLYCOPROTEIN SYNTHESIS; EPITHELIAL-CELLS; O-GLYCOSYLATION;
ALKALINE-PHOSPHATASE; SURFACE MEMBRANE; BIOSYNTHESIS; PROTEINS;
LOCALIZATION; EXPRESSION; HYDROLASE
Abstract: Human angiotensin I-converting enzyme (ACE) exists in intestinal epithelial cells as a membrane-bound (ACEm) and secretory glycoprotein (ACEsec). The electrophoretic mobilities of ACEsec and ACEm on SDS/polyacrylamide gels are similar; the N-deglycosylated ACEsec and ACEm, in contrast, display slight differences in their apparent molecular masses, indicating that the carbohydrate contents of ACEsec and ACEm are different. Moreover, ACEsec is solely N-glycosylated whereas ACEm is N-and O-glycosylated, assessed by lectin binding studies. Spontaneous release of ACEsec is achieved by incubation of brush border membranes at 37 degrees C. Aprotinin, leupeptin and EDTA partly inhibit the generation of ACEsec, strongly suggesting that ACEsec is generated from ACEm by proteolytic cleavage. The expression levels of ACEsec in the intestine may be associated with the differentiation state of mucosal cells. Thus ACEsec is more abundant than ACEm in immature nonepithelial crypt cells of patients with coeliac disease. Well-differentiated epithelial cells, by contrast, contain predominantly ACEm. The variations in the proportions of cleaved ACEsec in differentiated and non-differentiated cells may be due to varying levels of the cleaving protease. Alternatively, because epithelial cell differentiation is accompanied by alterations in the levels of oligosaccharyltransferases, the results suggest a critical role for the glycosylation pattern of ACEm in its susceptibility to the putative cleaving protease.
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