Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.15.1 (ACE)
18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sarcoidosis is a disease of unknown etiology that is characterized by the generalized formation of granulomas and is accompanied by elevation in the serum in less than half the patients of angiotensin converting enzyme, a dipeptidyl carboxypeptidase that catalyzes the conversion of the decapeptide, angiotensin I, to the pressor octapeptide, angiotensin II, and L-histidyl-L-leucine. Mean activity of angiotensin converting enzyme was elevated generally more than 10-fold in granuloma-containing lymph nodes, but not in lung in which normally it is abundant, in 19 of 20 patients with sarcoidosis. Angiotensin converting enzyme in lymph nodes from subjects with sarcoidosis was similar to the enzyme from normal lung and lymph node with respect to activity as a function of pH, inhibition of activity by EDTA and o-phenanthroline, gel filtration on Sephadex G-200, and requirement for chloride for activity, but appeared to be more heat labile. The data suggest that the granulomas in sarcoidosis may be the source of the elevated serum enzyme and that cells of the granulomas, particularly the epitheloid cells which appear by electron microscopy to have active protein biosynthesis, may be actively synthesizing the enzyme.
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PMID:Markedly elevated angiotensin converting enzyme in lymph nodes containing non-necrotizing granulomas in sarcoidosis. 0 63

Using hippuryl-L-histidyl-L-leucine as a substrate analogue, serum angiotensin converting enzyme (ACE) was spectrophotometrically estimated in patients with bronchial asthma. The mean level of asthmatic patients was significantly lower than that of the control subjects. The reduced serum ACE activities did not change during an acute asthmatic attack. Significantly lower levels of serum ACE occurred in patients with chronic asthma than in those who only suffered with occasional asthma. Serum ACE activity was not reduced when the patients were taking steroids. Serum ACE activity could not be correlated with either the systolic blood pressure or the diastolic blood pressure of our asthmatic patients. However, serum ACE activity was correlated with the serum beta-globulin fraction in asthmatic patients.
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PMID:Serum angiotensin converting enzyme level in bronchial asthma. 7 63

In adult chronic non-neuronopathic (Type 1) Gaucher's disease significant (p less than 0.001) elevations of angiotensin converting enzyme in serum (93.3 +/- 14.8 nmol/min/ml; number elevated, 8/11; normal control 32.2 +/- 1.30, n = 58) and spleen (5.62 +/- 0.35 nmol/min/mg protein, n = 2; control, 0.431 +/- 0.101, n = 4) and serum lysozyme (15.6 +/- 3.37 mug/ml; number elevated, 4/5) were observed. The KM for hippuryl-L-histidyl-L-leucine of Gaucher (1.31 mM) and normal (1.23 mM) serum angiotensin converting enzyme were similar. The increased angiotensin converting enzyme (ACE) in Gaucher's disease may be related to the genetic defect resulting in increased ACE synthesis in Gaucher cells, or perhaps generally, while high lysozyme may reflect an increased body mass of reticuloendothelial cells. These enzyme elevations may be of use in suggesting the possible presence of Gaucher's disease and perhaps in assessing the magnitude of pathologic involvement.
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PMID:Elevated serum and spleen angiotensin converting enzyme and serum lysozyme in Gaucher's disease. 18 66

Using hippuryl-L-histidyl-L-leucine as a substrate analog, serum angiotensin converting enzyme (ACE) was spectrophotometrically estimated in patients with bronchial asthma. There were significantly low activities of serum ACE in 115 patients with bronchial asthma irrespective of the presence or absence of acute attack. The activity of serum ACE was reduced more markedly in the chronic type of bronchial asthma than in the paroxysmal type.
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PMID:Serum angiotensin converting enzyme activity in human bronchial asthma. 19 59

The activity of serum angiotensin converting enzyme (ACE), assayed fluorometrically with the substrate hippuryl-L-histidyl-L-leucine was significantly higher in 116 patients with sarcoidosis than in 415 patients with other diseases--pulmonary and nonpulmonary--and in 58 normal subjects. Serum ACE was elevated in 59% of 46 recently diagnosed, untreated patients with sarcoidosis and was significantly reduced following steroid therapy in three patients with sarcoidosis, but in only one of four patients treated with placebos. The results suggest that elevated serum ACE activity is a valuable, although not absolutely specific, diagnostic indicator of sarcoidosis. It should be stressed that a normal value does not rule out the disease, and that steroid therapy tends to reduce the serum ACE activity.
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PMID:Increased serum angiotensin converting enzyme activity in sarcoidosis. 20 93

The activity of angiotensin converting enzyme, which transforms the relatively inactive decapeptide angiotensin I to the active octapeptide angiotensin II by removal of an L-histidyl-L-leucine residue, has been assayed in numerous region of the calf brain and of the brains of humans with Huntington's chorea and controls. In calf brain there are pronounced regional variations in enzyme activity, with highest activity in the globus pallidus and area postrema. In human brain, enzyme activity is highest in the corpus striatum, with similar levels in the caudate, putamen, and globus pallidus. Converting enzyme activity is reduced by 83 to 92% in the globus pallidus in Huntington's chorea. The caudate and putamen of choreic patients display 62 to 69% reductions in enzyme activity. Converting enzyme activity in two cerebral cortical regions from choreic brains is not significantly different from control.
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PMID:Huntington's chorea: selective depletion of activity of angiotensin coverting enzyme in the corpus striatum. 21 22

The method of chemical assay of angiotensin I-converting enzyme described is a modification of the previously published spectrophotometric assay based on quantitation of hippuric acid released from hippuryl-L-histidyl-L-leucine. The new procedure involves extraction of hippuric acid with ethylacetate, evaporation to dryness of the extract, solubilization of the residue with 1 mol/l NaCl and purification with petroleum ether before measurements of the absorbance at 228 nm of the aqueous phase. Under these conditions, hippuric acid insoluble in petroleum ether remains in the aqueous phase, whereas other A228-absorbing materials, readily soluble in the ether and able to interfere with the assay, are eliminated.
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PMID:[Spectrophotometric assay of angiotensin I-converting enzyme (author's transl)]. 22 23

The pulmonary and hepatic clearances of the synthesized angiotensin converting enzyme (ACE) substrate, hippuryl-L-histidyl-L-leucine (HHL) were evaluated by applying the multiple sites of input method and the recirculation pharmacokinetic model. Rats received a constant rate infusion via the carotid artery, jugular vein or portal vein in the absence or presence of the ACE inhibitor, captopril. Blood samples were collected from the femoral artery. The organ extraction ratio was calculated from the steady-state plasma concentrations and the mean organ transit time was computed as the difference in the mean residence times for various administration routes. Pronounced elimination in the lung and liver was observed in the absence of captopril. Pulmonary metabolism was completely depressed in the presence of captopril while the hepatic elimination was little affected. This suggests that the pulmonary elimination was entirely ascribed to ACE while there exists an alternative elimination process in the liver. The mean cardiopulmonary transit time was very short, indicating the pulmonary elimination of HHL may take place on the surface of the vascular endothelium. The evaluation of the pulmonary elimination of HHL described in this paper indicates a simple in vivo method for assessing the pharmacological effect of ACE inhibitors. The present pharmacokinetic approach will be useful for the quantification of drug disposition in individual organs in vivo.
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PMID:Pulmonary and hepatic disposition of hippuryl-L-histidyl-L-leucine. 164 13

Kininase II (EC 3.4.15.1) (KII) and kininase I (KI) (EC 3.4.12.7) activities of rat plasma were characterized by the hydrolysis of hippuryl-L-histidyl-L-leucine (HHL), hippuryl-L-arginine (HLA) [expressed as carboxypeptidase N1 (CN1) activity] and hippuryl-L-lysine (HLL) [expressed as carboxypeptidase N2 (CN2) activity]. Using a spectrophotometric assay, biochemical characteristics of the three enzymes were investigated. The Michaelis-Menten constants were as follows: KII: Km 2.55 +/- 0.22 mM, Vmax 0.357 +/- 0.017 mumol/min/mL; CN1: Km 6.93 +/- 0.32 mM, Vmax 0.748 +/- 0.019 mumol/min/mL; and CN2: Km 35.8 +/- 1.52 mM, Vmax 13.11 +/- 0.40 mumol/min/mL. EDTA and O-phenanthroline inhibited the three enzyme assays at the same Ki, whereas captopril and 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid (MERGETPA), allowed for the demonstration of the specificity of each assay. Furthermore, Ki values of MERGETPA against both CN1 (4.75 microM) and CN2 (2.36 microM) activities do not support the hypothesis that KI activity may be accounted for by the presence of isoenzymes in rat plasma.
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PMID:A micromethod for the determination of the activities of kininases in rat plasma. Kinetics and inhibitory characteristics. 184 16

This study was undertaken to verify the activity of plasma kininases in hypertension. Male Wistar rats (WIS) were used and three models of experimental hypertension were studied: spontaneously hypertensive rats (SHR), renal hypertensive rats, made according to the method of Goldblatt, DOCA-salt hypertensive rats. Normal Wistar rats, nephrectomized rats and sodium-loaded rats were used as control groups. Plasma from these animals was used to evaluate the kininase activities: kininase II activity (KII) was measured by the hydrolysis of hippuryl-L-histidyl-L-leucine (HHL); kininase I activity (KI) was measured by the hydrolysis of hippuryl-L-arginine (HLA) (CN1 activity) and of hippuryl-L-lysine (HLL) (CN2 activity). The three enzyme activities were characterized by their kinetic constants and the inhibitory pattern of various inhibitors. In normal WIS rats, hydrolysis of HHL proceeds with a Km of 2.55 +/- 0.22 mM and at a Vmax of 0.357 +/- 0.017 mumol/min/ml; the enzyme is inhibited by EDTA, 0-phenanthroline and captopril. HLA has a Km of 6.93 +/- 0.32 mM and a Vmax of 0.748 +/- 0.019 mumol/min/ml while the Km and Vmax values of HLL are 35.8 +/- 1.52 mM and 13.11 +/- 0.40 mumol/min/ml. The hydrolysis of both substrates is inhibited by EDTA, 0-phenanthroline and MERGETPA. KII activity is decreased in WKY and SHR rats (Vmax = 0.241 +/- 0.014 and 0.262 +/- 0.011 mumol/min/ml, respectively). In renal hypertensive rats and DOCA-salt hypertensive rats, the KII activity remained unchanged. CN1 activity was increased in 1K, 1C hypertensive animals (Vmax = 0.866 +/- 0.221 mumol/min/ml) and in DOCA-salt hypertensive rats (Vmax = 1.119 +/- 0.049 mumol/min/ml).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Activity of plasma kininase I and kininase II in hypertensive rats]. 217 85


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