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

Yoshioka, Masahiro; Erickson, Roger H.; Woodley, John; Gulli, Rocco; Guan, Difu; Kim, Y. S.

doi:10.1152/ajpgi.1987.253.6.g781

Cited by 29 publications

(24 citation statements)

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“…As discussed, ACE is present in many different tissues, including the gastrointestinal tract, where some epithelia express high levels of somatic ACE (Yoshioka et al, 1987). Although the precise function of ACE in this location is not fully understood, the nonspecificity of ACE peptide cleavage suggests the hypothesis that it may play a role in the digestion of peptides (Rivière et al, 2004).…”

Section: Digestionmentioning

confidence: 99%

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

et al. 2012

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Section: Digestionmentioning

confidence: 99%

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

et al. 2012

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“…The role of ACE in transport functions of these epithelial cells is not clear yet. In the small intestine, ACE may cleave off dipeptides of digested protein fragments that are then easily absorbed by enterocytes (34,37).…”

Section: Resultsmentioning

confidence: 99%

Naturally occurring active N-domain of human angiotensin I-converting enzyme.

Deddish

Wang

Michel

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Angiotensin I-converting enzyme (ACE, kininase II) is a single-chain protein containing two active site domains (named N-and C-domains according to position in the chain). ACE is bound to plasma membranes by its C-terminal hydrophobic transmembrane anchor. Deal fluid, rich in ACE activity, obtained from patients after surgical colectomy was used as the source. Column chromatography, including modified affinity chromatography on lisinopril-Sepharose, yielded homogeneous ACE after only a 45-fold purification. N-terminal sequencing of ileal ACE and partial sequencing of CNBr fragments revealed the presence of an intact N terminus but only a single N-domain active site, ending between residues 443 and 559. Thus, ileal-fluid ACE is a unique enzyme differing from the widely distributed two-domain somatic enzyme or the single C-domain testicular (germinal) ACE. The molecular mass of ileal ACE is 108 kDa and when deglycosylated, the molecular mass is 68 kDa, indicating extensive glycosylation (37% by weight). In agreement with the results reported with recombinant variants of ACE, the ileal enzyme is less C1-dependent than somatic ACE; release of the C-terminal dipeptide from a peptide substrate was optimal in only 10 mM Cl. In addition to hydrolyzing at the C-terminal end of peptides, ileal ACE efficiently cleaved the protected N-terminal tripeptide from the luteinizing hormone-releasing hormone and its congener 6-31 times faster, depending on the Cl concentration, than the C-domain in recombinant testicular ACE. Thus we have isolated an active human ACE consisting of a single N-domain. We suggest that there is a bridge section of about 100 amino acids between the active N-and C-domains of somatic ACE where it may be proteolytically cleaved to liberate the active N-domain. These findings have potential relevance and importance in the therapeutic application of ACE inhibitors.

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“…The highest ACE2 mRNA expression levels were detected in the intestine epithelium. Like rat intestinal ACE, which is stimulated by high-protein-feeding, 29,30 ACE2 may act as a final proteolytic enzyme in nutrient degradation. The other major ACE2-expressing tissue was the placenta, suggesting that ACE2 may be involved in mother/fetus interactions, which is interesting regarding a potential role of ACE2 in fetal programming and pregnancy.…”

Section: Discussionmentioning

confidence: 99%

Angiotensin-Converting Enzyme 2 (ACE2) and ACE Activities Display Tissue-Specific Sensitivity to Undernutrition-Programmed Hypertension in the Adult Rat

et al. 2005

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Abstract-Human epidemiological studies have shown that low birth weight is associated with hypertension in adulthood.Rodent models of intrauterine growth retardation (IUGR) support these findings because offspring from undernourished dams develop hypertension. Angiotensin-converting enzyme 2 (ACE2) is a newly described renin-angiotensin system (RAS) component that competes with ACE for angiotensin peptide hydrolysis and therefore may modulate blood pressure. However, ACE2 potential participation in hypertension programming remains unknown, although RAS alterations were reported in IUGR models. Hence, we first investigated the tissue distribution of ACE2 and ACE in the rat and then whether hypertension programming differentially affects both enzymes. Using multiplex RT-PCR and in situ hybridization, we show that ACE2 mRNA is widely expressed and coregionalized with ACE. Moreover, tissues involved in blood pressure homeostasis (lung, heart, and kidney) express high levels of both enzymes. Enzymatic assays reveal that ACE2 and ACE are coactive in these tissues. Adult (4-month-old) offspring from 70% food-restricted dams throughout gestation (FR30 rats) present mild hypertension, impaired renal morphology, as well as elevated plasma angiotensin II and aldosterone, suggesting alterations of the systemic RAS. In FR30 rats, we show that ACE2 and ACE activities are increased only in the lung, whereas their mRNA expression is not significantly altered, showing that the enzymes display tissue-specific sensitivity to programming. Our results indicate that ACE2 and ACE are coexpressed in numerous rat tissues and that their increased activity in the lung of FR30 rats may participate in hypertension programming.

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

Cited by 29 publications

References 0 publications

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

Naturally occurring active N-domain of human angiotensin I-converting enzyme.

Angiotensin-Converting Enzyme 2 (ACE2) and ACE Activities Display Tissue-Specific Sensitivity to Undernutrition-Programmed Hypertension in the Adult Rat

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