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)

Elevation of serum-angiotensin-converting enzyme (serum ACE) in patients with active sarcoidosis was confirmed in a total of 64 subjects with a mean serum ACE of 15.76+/-7.4 units compared with 6.05+/-2.0 units in 194 patients with other types of respiratory disease. Resolution of the sarcoidosis disease state or therapeutic control with adequate doses of corticosteroids (15 mg prednisone daily) brought the elevated serum ACE levels down into the normal range. A longitudinal study of serum ACE activity was found to be an effective way of judging the therapeutic efficacy of various steroid dosage levels. No other disease state involved in the differential diagnosis of sarcoidosis was found to have elevations of serum ACE activity. However, 6 patients with Gaucher's disease did have elevated serum ACE activity that ranged well above the usual level seen even in patients with sarcoidosis. The two diseases could be readily distinguished in the laboratory by elevated serum acid phosphatase activity in most cases of Gaucher's disease. It would appear that detection of elevated serum ACE levels can be a useful procedure for confirming a diagnosis of active sarcoidosis and for judging the therapeutic response.
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PMID:The specificity and nature of serum-angiotensin-converting enzyme (serum ACE) elevations in sarcoidosis. 18 94

A statistically highly significant elevation of serum ACE was found in a group of 58 patients with sarcoidosis (serum ACE was elevated in 34% of patients), as compared with normal controls and patients with tuberculosis and various other common diseases. The results suggest that serum ACE is a useful aid for the diagnosis of sarcoidosis when elevated, but that a normal value does not rule out the condition and may occur in more than one-half of monitored patients. There is a trend to diminution of serum ACE with increasing duration of disease with or without steroid therapy, perhaps correlating with the total body mass of active granulomas, as indirectly suggested in preliminary data by correlation of serum ACE with serum globulin in 16 sarcoidosis patients. It is not yet clear whether there is any significant steroid effect on serum ACE, but a significant number of patients on steroid therapy for more than 2-4 yr have elevated serum ACE values, which in some instances are extremely high. There was a 12-fold elevation in ACE to specific activities generally exceeding those of normal lung in granulomatous lymph nodes of 14 patients with sarcoidosis, suggesting that sarcoid granulomas may be actively synthesizing ACE and resulting in elevation of serum ACE. Extensively fibrotic sarcoid lymph nodes had normal or slightly elevated ACE, suggesting that obliteration of granulomas in sarcoid lymph nodes diminishes their ACE content and that this obliteration may be related to the tendency to diminution of serum ACE with time. ACE was not elevated in one tuberculous lymph node or in experimental granulomas, suggesting that elevation of ACE may have some specificity for the granuloma of sarcoidosis rather than being a characteristic of all granulomas. The catalytic and physical properties of ACE in serum and lymph nodes in sarcoidosis were generally similar to normal ACE with respect to pH activity, modulators, polyacrylamide-gel electrophoresis, and Sephadex G-200 gel filtration. However, sarcoid lymph node ACE appeared to be more heat labile than normal lung or lymph node ACE, suggesting the possibility that an abnormal ACE may be present in sarcoidosis. If an abnormal enzyme is indeed present, it might be coded for by a host gene that is not normally expressed or a nonhost gene or it might be a normal ACE that has been altered. No ACE activity was found in circulating white blood cells in sarcoidosis or in control subjects, suggesting that circulating white blood cells may not contain the epithelioid cell precursor or that ACE synthesis (or less likely, uptake) may be turned on at a later stage in the transformation. Lysozyme activity was also elevated in sarcoid lymph nodes. Serum ACE and serum lysozyme were significantly positively correlated in 16 sarcoidosis patients, suggesting a relationship between the two...
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PMID:Elevation of angiotensin-converting enzyme in granulomatous lymph nodes and serum in sarcoidosis: clinical and possible pathogenic significance. 18 95

ACE activity of the serum of 52 normal pregnant women was measured in vitro under conditions of substrate saturation with Hip-His-Leu as substrate. The product His-Leu was measured by fluorimetry after reaction with o-phthaldehyde. ACE activity (nmol/min/ml serum) was 30.6 +/- 7.8, 28.8 +/- 7.4, and 30.9 +/- 8.2 for the first, second, and third trimester of pregnancy, respectively. No statistically significant differences (p greater than 0.05) in ACE activity were detected among the three trimesters of normal pregnancy with either serum volume or serum protein as reference value. These values are within the range reported by Friedland and Silverstein13 for 51 male and seven female healthy blood bank donors. We conclude that the evolution of normal pregnancy does not significantly modify the levels of ACE in peripheral blood serum.
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PMID:Angiotensin-converting enzyme: serum levels during normal pregnancy. 22 54

Sarcoid uveitis is usually a presumptive diagnosis based on the simultaneous presence of uveitis and clinicoradiographic or histologic findings of sarcoidosis. The elevation of serum ACE in some patients with granulomatous uveitis is strongly presumptive of sarcoid uveitis even in the absence of these findings. Serum ACE may prove to be a useful indicator of ocular sarcoid in the absence of otherwise undetectable systemic disease.
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PMID:Uveitis associated with sarcoidosis and angiotensin converting enzyme. 23 84

Serum angiotensin converting enzyme activity was measured in 60 blood donors and 100 patients with sarcoidosis histologically confirmed using a spectrophotometric assay with hippurylhistidylleucine as substrate. Sex related differences in the enzyme activity could not be observed. ACE was found to be markedly raised above the normal range (the mean of the control subjects plus 2 standard deviations) in 53 (58.2%) out of 91 untreated patients. The distribution of the enzyme activities was significantly different as compared to the control group. Nine patients with sarcoidosis receiving steroids had a mean level within the normal range. ACE level in stage II group tended to be more elevated compared to stage I, but this difference was not significant. Extrapulmonary sarcoidosis (with and without pulmonary involvement) appeared to be associated with especially high ACE activities. The distribution of the enzyme activities within the groups of untreated patients failed to reveal statistically significant differences. Therefore it was not possible to determine the clinical state of the disease and to discriminate between the stages (I and II) of sarcoidosis by the measurement of serum ACE level. However as the results suggest serum ACE assays can be a useful aid in diagnosis of sarcoidosis. Further investigations may demonstrate the value of this in vitro method for the clinical management of the disease including prognosis and therapeutic effects.
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PMID:[Diagnostic value of serum angiotensin converting enzyme activity in sarcoidosis (author's transl)]. 23 24

The effect was followed up of 2-PAM and Toxogonin (T), reactivators of choline esterase, at a single muscular application on the activity of acetylcholine esterase (ES 3.1.1.7) (ACE) of whole blood (WB) and the myoneural synapses (MS) of an interrib muscle. It was found that a species-specific effect was produced by T and 2-PAM on ACE of WB and MS in lambs and sheep. Optimal doses of 50 and 80 mg/kg led to a slight drop in the activity of ACE at the 2nd hour following injection, after which it rose gradually up to values that were higher than the initial ones for more than ten days. 100 and 200 mg/kg led to a more sensitive and long-term drop in the activity of ACE (up to 48h--72nd hour), after which it likewise rose above the initial value, and came back to normal on the 13th day. With lambs the reaction was analogous, though weaker. In rats and rabbits there was no change in the activity of ACE of WB and MS following the use of oximes. The optimal nontoxic and inductoenzyme rates of the two oximes for lambs and sheep proved to be about 50 mg/kg. It was established that both for rats and for sheep and lambs T was almost twice as toxic as 2-PAM. Intoxication with T was characterized by severe hemorrhagic and necrotic nephroso-nephritis, acute toxic dystrophy of the liver, and ulcerous, necrotic enteritis. 2-PAM was found to potentiate the toxic effect of T.
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PMID:[Toxicity of oximes and their effect on acetylcholinesterase activity in the blood and myoneural synapses of animals]. 36 May 96

The effect of captopril (SQ 14,225) a potent inhibitor of angiotensin converting enzyme (ACE: kininase II) on the bronchoconstrictor response to bradykinin was studied in the anesthetized guinea pig. The i.v. administration of captopril caused a profound long lasting hypotension without affecting pulmonary resistance or dynamic compliance. Similarly, the i.v. administration of bradykinin caused small increases in pulmonary resistance and decreases in dynamic compliance which were not altered by the administration of captopril. However, after beta-receptor blockade with propranolol, bradykinin-induced changes in resistance and compliance were enhanced; additional captopril administration further potentiated the bradykinin effects. The prostaglandin synthetase inhibitor indomethacin antagonized the bradykinin-induced bronchoconstriction in beta-blocked animals and its potentiation by captopril. In the isolated perfused guinea pig lung, bradykinin caused a dose dependent release of a prostaglandin-like substance which was significantly increased by captopril and antagonized by indomethacin. These results suggest that bradykinin causes a prostaglandin-mediated bronchoconstriction. Captopril, a potent inhibitor of ACE, prevents the degradation of bradykinin thus potentiating the bradykinin-induced bronchoconstriction, an effect observed in intact animals only in the absence of pulmonary beta-receptor activation.
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PMID:The effects of captopril (SQ 14,225) on bradykinin-induced bronchoconstriction in the anesthetized guinea pig. 38 32

With only a few exceptions, in sarcoidosis the lung is virtually always, the liver mostly and the spleen only occasionally involved. Therefore, thorax-X-ray is the most important screening procedure. Histological verification by laparoscopy, bronchoscopy (transbronchial lung biopsy and bronchial mucosa biopsy) or mediastinoscopy is essential. In order to decide the therapeutic regimen, particularly the use of corticosteroids, the staging according to Wurm seems less suitable than pulmonary function testing (pneumotachograph, plethysmograph, CO-transfer, compliance). Futher clinical trials will have to find out, whether enzyme analysis (ACE) is apt to monitor progression of disease or to diagnose sarcoidosis in clinical routine use.
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PMID:[Diagnosis and treatment of sarcoidosis (author's transl)]. 54 3

Drug-membrane association of daunomycin, adriamycin and three of its derivatives, adriamycin-14-octanoate (AD-14-OCTA), adriamycin-14-acetate (AD-14-ACE) and N-trifluoroacetyladriamycin-14-valerate (AD32), was studied using phospholipid bilayers and human erythrocytes. The various drugs exhibited a differential affinity to membrane-lipid domains. Lipid-incorporated drugs exhibit a marked change in the shape of the emission spectrum which was utilized for the evaluation of the apparent dielectric constant, epsilon, of the environment surrounding the anthracycline moiety, as well as for the determination ofthe partitioning constant. By measuring the fluorescence polarization and the fluorescence lifetime of the incorporated drugs, rotational relaxation times of 4--8 ns were derived. These parameters provide a supportive evidence of the association of the fluorophore of the drugs with membrane-lipid domains. The anthracycline derivatives interact to a different degree with dipalmitoyl phosphatidylcholine and phosphatidylserine as reflected by changes in their thermotropic properties assessed by differential scanning calorimetry. Daunomycin was the most effective in decreasing the temperature of the phase transition and brought about a comparable reduction in the enthalpy of melting as AD32 and AD-14-OCTA. Adariamycin was the least potent of the series. AD-14-ACE and AD32 protected erythrocytes against hypotonic lysis, adriamycin and daunomycin had no significant effect on the susceptibility to hypotonic lysis, whereas AD-14-OCTA proved to be hemolytic even at low concentration (approx. 10(-7M).
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PMID:A differential interaction of daunomycin, adriamycin and their derivatives with human erythrocytes and phospholipid bilayers. 70 25

Analysis of carcinoembryonic antigen (CE)-reactive glycoproteins from liver metastasis of primary colon and breast tumors and from primary breast tumors has been carried out by affinity chromatography on concanavalin A (Con A)-Sepharose. Three CEA-reactive glycoproteins from colon tumors (liver metastasis) with different binding capacity to Con A have been separated and further purified by gel filtration. Of the 3 CEA-reactive glycoproteins, 1 of them did not bind to Con A. Both Con A-binding and nonbinding CEA-reactive glycoproteins were immunologically indistinguishable when tested with a reference goat anti-CEA (ACE, 67-70; Dr. C.W. Todd and Dr. M.L. Egan), as well as with a variety of rabbit anti-CEA and anti-CEA (nonbinding) prepared in this laboratory. Carbohydrate analysis showed that mannose content of different purified CEA preparations or nonbinding CEA did not differ appreciably. N-Acetylglucosamine content of purified CEA preparations, however, varied considerably, suggesting that this sugar may impart the specificity of binding of CEA to Con A. The purified CEA preparations differed in their ability to inhibit the binding of 125l-labeled CEA to goat anti-CEA. One of the purified CEA preparations had 3- to 8-fold greater inhibitory capacity when compared to other preparations and shared a partial identity with a glycoprotein present in the extracts of fetal colon. The glycoprotein extracts of primary breast tumors did not contain a CEA that was immunologically identical to CEA present in colon tumors, whereas the liver metastasis of primary breast tumors showed several CEA-reactive glycoproteins as judged by radioimmunoassay. However, these CEA-reactive glycoproteins did not have any antigenic relationship with CEA from colon tumors when tested by double diffusion and immunoelectrophoresis. In conclusion, when Con A affinity chromatography of tumor glycoproteins is carried out under defined conditions and with the use of appropriate antisera, it is possible to delineate the presence or absence of CEA in tumors of nonentodermal origin.
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PMID:Immunochemical studies on carcinoembryonic antigen-reactive glycoproteins from carcinomas of the colon and breast separated by concanavalin A affinity chromatography. 97 8


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