Angiotensin I converting enzyme (kininase II) of the brush border of human and swine intestine

Ward, Patrick E.; Sheridan, Martha A.; Hammon, Katy; Erdös, Ervin G.

doi:10.1016/0006-2952(80)90603-6

Cited by 79 publications

(30 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ACE is localized to the luminal surface of vascular endothelial cells (2) and also occurs at other sites in tissues such as kidney (3), brain (4), and small intestine (5). Techniques for harvesting and culture of endothelial cells have been described (6), and the cultured cells have been shown to produce ACE in vitro (7).…”

Section: Introductionmentioning

confidence: 99%

Induction by Glucocorticoids of Angiotensin Converting Enzyme Production from Bovine Endothelial Cells in Culture and Rat Lung In Vivo

Mendelsohn¹,

Lloyd²,

Kachel³

et al. 1982

J. Clin. Invest.

130

View full text Add to dashboard Cite

A B S T R A C T The effect of corticosteroids on angiotensin converting enzyme was investigated in endothelial cell cultures and intact rat lung. Cultured endothelial cells from bovine aorta showed net production of angiotensin converting enzyme (ACE) over 2 d culture in serum-free medium. Dexamethasone (DM) increased cell ACE activity six-to sevenfold at 100 nM with a threshold effect at 0.3 nM. The effect of DM on ACE production was completely inhibited by actinomycin D or cycloheximide. Deoxycorticosterone (DOC) and aldosterone were markedly less active, with a threshold near 100 nM and significant (two to threefold) stimulation of ACE activity at 1 ,uM. In cells incubated in the presence of 10 nM DM, DOC (10 ,iM) significantly inhibited ACE production compared with 10 nM DM alone, suggesting that DOC is a partial agonist/partial antagonist in this enzyme system. Protein content of cells or medium was unchanged by steroids at all doses used.In vivo, adrenalectomized rats showed lower pulmonary ACE compared with intact controls, and when injected with DM (40 ,ug/d for 4 d) showed a significant (twofold, P < 0.002) increase in lung ACE over oil-injected, adrenalectomized controls; serum ACE did not change. Injection with DOC (40 jg/d) or aldosterone (10 jg/d) had no effect on lung or serum ACE. Over a range (0.6 to 2,000 jig) of concentrations of DM administered daily for 7 d, the dose-response curve of DM for induction of pulmonary ACE mirrored that for thymolysis; for both, half-maximal effects were seen at -6 jg DM/d, and plateau levels at 60 Ag/d.Received for publication 23 November 1981 and in revised form 18 May 1982. We conclude that glucocorticoids are potent inducers of ACE activity in endothelial cells in culture and in rat lung in vivo, and that the action of aldosterone and DOC reflects occupancy of glucocorticoid receptors. This effect may be of (patho)physiological relevance in regulating levels of ACE in local vascular beds, and thereby modulating local levels of the vasoactive peptides angiotensin II and bradykinin.

show abstract

Section: Introductionmentioning

confidence: 99%

Induction by Glucocorticoids of Angiotensin Converting Enzyme Production from Bovine Endothelial Cells in Culture and Rat Lung In Vivo

Mendelsohn¹,

Lloyd²,

Kachel³

et al. 1982

J. Clin. Invest.

130

View full text Add to dashboard Cite

show abstract

“…It has been identified in the luminal aspect of vascular endothelial cells in lung, where it plays an important role in the process of fluid extravasation in the context of the 'neurogenic inflammation' (Piedimonte et al, 1991), and in other areas, where it is implicated in vascular permeability changes (Caldwell et al, 1976). Membranebound ACE is also found in renal proximal tubules (Oshima et al, 1974;Schulz et al, 1988), in the gastrointestinal brush border (Ward et al, 1980), in brain structures (choroid plexuses, circumventricular structures) (Igic et al, 1977;Defendini et al, 1983), and in the testis and epididymis (Srittmaster & Snyder, 1984).…”

Section: Introductionmentioning

confidence: 99%

Angiotensin converting enzyme binding sites in human heart and lung: comparison with rat tissues

Vago

Bevilacqua

Conci

et al. 1992

British J Pharmacology

View full text Add to dashboard Cite

1Angiotensin converting enzyme (ACE), a dipeptidyl carboxypeptidase which catalyzes the final activation step in the formation of angiotensin II, was identified by radioligand studies in rat heart and lung. In this work we identified ACE binding sites in human left ventricle and lung by radioligand binding using the ACE inhibitor [3H]-ramiprilat, and compared its binding characteristics in human and rat tissues. 2 Binding of [3H]-ramiprilat in all tissues tested was saturable, temperature and zinc-dependent, and inhibited by EDTA. In human left ventricle homogenate we found a density of binding sites of 121 ± 15 fmol mg-' protein (n = 4) with an affinity (Kd) of 850 ± 55 pM, whereas in rat left ventricle the same values were 23 ± 4 fmol mg-' protein and 315 ± 30 pM, (n = 4), respectively. 3 [3H]-ramiprilat binding to rat (n = 4) and human lung (n = 4) showed a binding site density of 2132 ± 155 and 1085 ± 51 fmol mg-' protein respectively with an affinity of 639 ± 54 and 325 ± 22 pM. The lung:heart ratio of ACE binding site density was about 9:1 in man and 100:1 in rat. 4 The binding affinities of 13 ACE inhibitors were evaluated on human heart and lung: the drugs tested showed a wide range of affinities for the ACE binding sites in both tissues, and the affinity for lung was significantly greater than for heart for most of the drugs. 5 The greater potency of some ACE inhibitors in displacing [3H]-ramiprilat in human lung compared with the heart indicates differences between ACE binding sites in these tissues and suggests the possibility of a selective organ-targeted therapeutic approach.

show abstract

“…The same role has been suggested for ACE on the intestinal brush border. 43 In the choroid plexus where ACE faces the cerebrospinal fluid and in the subfornical organ, ACE may facilitate the production of angiotensin II, which is a potent dipsogen. In addition the choroid plexus may be the source of ACE in cerebrospinal fluid.…”

mentioning

confidence: 99%

Angiotensin I converting enzyme and the changes in our concepts through the years. Lewis K. Dahl memorial lecture.

1990

View full text Add to dashboard Cite

Angiotensin I converting enzyme (kininase II) of the brush border of human and swine intestine

Cited by 79 publications

References 18 publications

Induction by Glucocorticoids of Angiotensin Converting Enzyme Production from Bovine Endothelial Cells in Culture and Rat Lung In Vivo

Induction by Glucocorticoids of Angiotensin Converting Enzyme Production from Bovine Endothelial Cells in Culture and Rat Lung In Vivo

Angiotensin converting enzyme binding sites in human heart and lung: comparison with rat tissues

Angiotensin I converting enzyme and the changes in our concepts through the years. Lewis K. Dahl memorial lecture.

Contact Info

Product

Resources

About