Purification and characterization of human converting enzyme (kininase II)

Stewart, T.A.; Weare, John A.; Erdös, Ervin G.

doi:10.1016/s0196-9781(81)80027-7

Cited by 66 publications

(17 citation statements)

References 32 publications

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“…Converting enzyme from hupian lung and kidney differ in their sialic acid content (14). Lung contains more acid forms, which confirms our findings.…”

Section: Resultssupporting

confidence: 90%

Influence of Neuraminidase Treatment on the Electrophoretic Behaviour of Angiotensin Converting Enzyme from Human Tissues

Sande¹,

Hendriks²,

Kasahara³

1986

Clinical Chemistry and Laboratory Medicine

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Angiotensin converting enzyme (dipeptidyl carboxypeptidase, kininase II; EC 3.4.15.1), is a membrane bound glycoprotein, playing an impqrtant role in the renin-aldosterone system. The enzyme contains a carbohydrate moiety, consisting of fucose, mannose, galactose, N-acetylglucosamine and Nacetylneuraminic acid. Treatment with nenraminidase (EC 3.2.1.18) removes sialic acid from the molecule. The influence of this treatment on the electrophoretic mobility of the enzyme was studied in 29 human tissues and body fluids. Results obtained showed differences in the sialic acid content of the enzyme in the tissues examined.

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“…Converting enzyme from hupian lung and kidney differ in their sialic acid content (14). Lung contains more acid forms, which confirms our findings.…”

Section: Resultssupporting

confidence: 90%

Influence of Neuraminidase Treatment on the Electrophoretic Behaviour of Angiotensin Converting Enzyme from Human Tissues

Sande¹,

Hendriks²,

Kasahara³

1986

Clinical Chemistry and Laboratory Medicine

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“…Human lung and kidney CE were purified to homogeneity as previously described [41,42]. Human kidney CE was also purified…”

Section: Methodsmentioning

confidence: 99%

Angiotensin-Converting Enzyme in Epithelial and Neuroepithelial Cells

Defending¹,

Zimmerman

Weare³

et al. 1983

Neuroendocrinology

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147

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Angiotensin-converting enzyme (CE) occurs in three types of cell:endothelial, epithelial, and neuroepithelial. In all three, it appears to be bound to plasma membrane. With antisera to the human enzyme, CE is demonstrated in paraffin sections on the apical surface of epithelial cells in the proximal tubule of the kidney, the mucosa of the small intestine, the syncytial trophoblast of the placenta, and the choroid plexus. Epithelial CE is characteristically found on microvillous surfaces in contact with an effluent, well placed to act on substrate in flux. In the brain, CE occurs in nerve fibers and terminals, mainly mesiobasally and in basal ganglia. Mesiobasal CE coincides with other components of the renin-angiotensin system (RAS) in the choroid/ventricular fluid, the subfornical organ, and the magnocellular neurosecretory system of the hypothalamus. Extrapyramidal CE, however, may not be related to the RAS. In the substantia nigra and the globus pallidus, the enzyme has the same cellular distribution as two putative neuromodulators, substance P and enkephalin, the latter a known substrate of CE.

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“…(4) The physiological concentrations of kinins in the heart tissue are below the K m values of the competing enzymes NEP and ACE and thus lower than those used in our in vitro experiments. Because BK has a higher affinity for ACE than for NEP, 23,24 we measured the degradation of BK by the cardiac membranes at a substrate concentration of 100 nmol/L, which is well below the K m values of both enzymes. At this concentration, the hydrolysis of BK follows first-order kinetics, that is, the substrate affinity may substantially affect the reaction kinetics.…”

Section: Role Of Ace In Bradykinin Metabolismmentioning

confidence: 99%

Kallidin- and Bradykinin-Degrading Pathways in Human Heart

et al. 1999

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Background-Since kinins kallidin (KD) and bradykinin (BK) appear to have cardioprotective effects ranging from improved hemodynamics to antiproliferative effects, inhibition of kinin-degrading enzymes should potentiate such effects. Indeed, it is believed that this mechanism is partly responsible for the beneficial effects of angiotensin-converting enzyme (ACE) inhibitors. In the heart, enzymes other than ACE may contribute to local degradation of kinins. The purpose of this study was to investigate which enzymes are responsible for the degradation of KD and BK in human heart tissue. Methods and Results-Cardiac membranes were prepared from the left ventricles of normal (nϭ5) and failing (nϭ10) hearts. The patients had end-stage congestive heart failure as the result of coronary heart disease or idiopathic dilated cardiomyopathy. Heart tissue was incubated with KD or BK in the presence or absence of enzyme inhibitors. We found no difference in the enzymes responsible for kinin metabolism or their activities between normal and failing hearts. Thus KD was mostly converted into BK by the aminopeptidase M-like activity. When BK was used as substrate, it was converted into an inactive metabolite BK-(1-7) mostly (80% to 90%) by the neutral endopeptidase (NEP) activity, with ACE unexpectedly playing only a minor role. The low enzymatic activity of ACE in the cardiac membranes, compared with that of NEP, was not due to chronic ACE inhibitor therapy, because the cardiac ACE activities of patients, whether receiving ACE inhibitors or not, and of normal subjects were all equal. Conclusions-The present in vitro study shows that in human cardiac membranes, the most critical step in kinin metabolism, that is, inactivation of BK, appears to be mediated mostly by NEP. This observation suggests a role for NEP in the local control of BK concentration in heart tissue. Thus inhibition of cardiac NEP activity could be cardioprotective by elevating the local concentration of BK in the heart. (Circulation. 1999;99:1984-1990.)

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Purification and characterization of human converting enzyme (kininase II)

Cited by 66 publications

References 32 publications

Influence of Neuraminidase Treatment on the Electrophoretic Behaviour of Angiotensin Converting Enzyme from Human Tissues

Influence of Neuraminidase Treatment on the Electrophoretic Behaviour of Angiotensin Converting Enzyme from Human Tissues

Angiotensin-Converting Enzyme in Epithelial and Neuroepithelial Cells

Kallidin- and Bradykinin-Degrading Pathways in Human Heart

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