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)

The activity of LDG, ACE and CE was determined in the lumbar CSF and blood serum of patients with sustained mild concussion of the brain. As compared to healthy persons the diseased demonstrated a significant rise of the LDG activity in the CSF while the mounting activity of 2 other enzymes, observed in individual instances in the CSF, lacked statistical significance. It was found that in functional upsets without any marked morphological lesions there may be encountered changes in the enzymatic activity that should be considered as a consequence of deranged metabolism.
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PMID:[Activity of the enzymes of cerebrospinal fluid and blood serum in patients with the concussion syndrome]. 116 37

Cerebrospinal fluid angiotensin converting enzyme (CSF-ACE) level was measured in two patients considered to have neurosarcoidosis, three patients with possible neurosarcoidosis and in 38 control patients suffering from prolapsed intervertebral discs. Both neurosarcoidosis patients had elevated levels (1.8 and 5.4 mumol/l/min) while the possible neurosarcoidosis patients had values similar to the control patients (mean 0.59 +/- 0.42 mumol/l/min). We suggest that CSF-ACE values may be of use in some patients as a diagnostic test for neurosarcoidosis and provide a reference range of normal controls.
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PMID:Cerebrospinal fluid angiotensin converting enzyme levels in the diagnosis of neurosarcoidosis. 166 71

Three different molecular forms of angiotensin converting enzyme (ACE) (approximately Mr 150,000, 80,000 and 40,000, respectively), have been recovered from human cerebrospinal fluid. All three enzymes were inhibited by captopril and enalapril and their activity was potentiated by chloride ions. They were capable of degrading Leu-enkephalin-Arg6 and substance -P, but gave no conversion of neurokinin A. In all these aspects, the CSF enzymes were identical with the human pulmonary enzyme. The Mr 40,000 form of ACE is the smallest active form of the enzyme hitherto reported and is likely to represent a fragment of the C-terminal part of native ACE, where its active center is located.
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PMID:Molecular heterogeneity of angiotensin converting enzyme in human cerebrospinal fluid. 171 7

Conversion of the octapeptide dynorphin (Dyn) A-(1-8) to Leu5-enkephalin (LE) by endopeptidase EC 3.4.24.15 (EP-24.15) in vivo was examined using the technique of ventriculocisternal perfusion. Peptides were administered intracerebroventricularly in the presence or absence of the EP-24.15 inhibitor N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate (cFPAAF-pAB) via cannulae placed into the lateral ventricle of urethane-anesthetized rats. The concentration of Dyn-like peptides and LE within the CSF was monitored by radioimmunoassay in samples of CSF taken from a second cannula placed in the cisterna magna. In the absence of inhibitor, less than 5% of the Dyn A-(1-8) administered was recovered in CSF. Immunoreactive LE, which is normally not found in CSF, increased rapidly in content following Dyn A-(1-8) infusion, an observation suggesting that the larger peptide is converted to LE. When the inhibitor cFPAAF-pAB was coadministered with Dyn A-(1-8), the concentration of immunoreactive Dyn A-(1-8) after 5 min was 40 times higher than that found in the absence of inhibitor. The angiotensin converting enzyme inhibitor captopril reduced the degradation of Dyn A-(1-8) to a much lesser degree. The inhibitor of EP-24.15 also afforded some protection of other Dyn-like peptides. No EP-24.15 activity was found in rat CSF, whereas high activity was found in the choroid plexus. Taken together, these data clearly indicate that an ectoenzyme form of EP-24.15 rapidly converts intracerebroventricularly administered Dyn-like peptides to LE.
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PMID:An inhibitor of endopeptidase-24.15 blocks the degradation of intraventricularly administered dynorphins. 197 55

Incubation of various authentic peptides with rat CSF in vitro and analysis of their products by HPLC demonstrated the presence in CSF of a peptidyl dipeptidase [peptidyl dipeptide hydrolase; angiotensin I converting enzyme (ACE); kininase II; EC 3.4.15.1] which sequentially degraded bradykinin (BK) by liberating the carboxy-terminal dipeptides and converted angiotensin I to angiotensin II. This CSF enzyme was gel-chromatographed by means of HPLC, and the molecular weight was estimated. The susceptibility to various peptidase inhibitors of the rat CSF enzyme, as well as the effect of NaCl on the degradation of BK and Hip-His-Leu catalyzed by it, was also determined. These properties were compared with those of ACE or kininase II from brain or other tissues, as described in the literature. NaCl was shown to exert specific and concentration-dependent effects on each step of the sequential degradation of BK, via BK(1-7) to BK(1-5), catalyzed by the enzyme. In addition, the enzyme system for metabolism of BK appears to differ between rat CSF and blood, the former containing exclusively kininase II, whereas the latter contains both kininase I (carboxypeptidase N; EC 3.4.12.7) and kininase II.
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PMID:Some characteristics of a peptidyl dipeptidase (kininase II) from rat CSF: differential effects of NaCl on the sequential degradation steps of bradykinin. 217 62

It is easy to identify patients with neurosarcoidosis who have a lesion the neural lesion. However, it is be difficult if the patient has a preceding neural lesion or isolated CNS sarcoidosis in which the lesion is localized in CNS and the lesion in another organ hem regressed. The finding of generalized or localized cerebral edema and the shadow of tumor on CT, and the result of CSF examination which indicates an increase in cell count, protein or ACE activity (especially in meningitis type) are helpful for the diagnosis of the above disorder. Epidemiological studies on the basis of 21 patients with neurosarcoidosis in our center and 166 patients in our country indicated that this disorder was more common in females than in males (1.6/1). The age of patients showed predominance in the twenties in males, and the twenties, forties and fifties in females. Common pathological finding in our postmortem examinations (n = 2) and intracranial biopsy (n = 1) was lymphocytic phlebitis in central and peripheral neurons and in neurons with no clinical symptom.
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PMID:[Neurosarcoidosis]. 235 89

Serum and CSF angiotensin converting enzyme (ACE) were measured by a new inhibitor binding assay in 32 patients with sarcoidosis, 49 with neurologic diseases, and 38 controls. In neurosarcoidosis, 11 of 20 patients had high levels of CSF ACE. In systemic sarcoidosis without neurologic abnormality, only 1 of 12 patients had elevated CSF ACE. The highest value was observed in a patient with widespread meningeal sarcoidosis. High values were also observed in patients with bacterial meningitis or malignant tumors of the CNS. Fluctuation in successive analyses correlated to clinical course of neurosarcoidosis. CSF ACE analysis seems useful in diagnosis and follow-up of neurosarcoidosis.
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PMID:Angiotensin converting enzyme in cerebrospinal fluid: a new assay. 299 15

Cerebrospinal fluid enzyme levels of creatine kinase (CK), lactate dehydrogenase (LDH), glutamate oxaloacetate transaminase (GOT) and angiotensin converting enzyme (ACE) were studied in 40 acute stroke patients comprising 20 lacunar strokes and 20 cortical strokes. A marked elevation of at least one of the enzymes CK, GOT or LDH was seen in 80% of cases of cortical strokes. No elevation was seen in lacunar stroke with CK, GOT or ACE and only a slight elevation with LDH. Within the cortical group, there was a correlation between the site, size of infarction seen on CT scan and enzyme level. These findings may help to explain the previously noted unpredictability of rises in CSF enzymes in stroke patients. In certain instances, a study of CSF enzymes may be of use to distinguish cortical from lacunar stroke. A precise diagnosis of lacunar infarction is important for management purposes, entry into stroke treatment trials or description of new syndrome types.
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PMID:CSF enzymes in lacunar and cortical stroke. 630 Nov 13

We report two siblings with sarcoidosis; the younger sister had symptoms of central nervous system, and both sisters had subcutaneous mass lesions in the gluteal region. Case 1. A 30-year-old woman presented with two episodes of right leg paresis. On admission, neurological examination revealed right leg weakness, spasticity of both legs, increased deep tendon reflexes in all extremities, urinary disturbance and hearing loss of the right ear, but she had no meningeal signs. Serological studies were normal including angiotensin converting enzyme. Cerebrospinal fluid revealed elevated protein to 340 mg/dl, mild pleocytosis, decreased glucose. CSF culture was negative, and cytology showed no malignant cells. Enhanced MR imaging showed diffuse leptomeningeal enhancement in both the brain around basal meninges and the whole spinal cord. Case 2. A 34-year-old woman (the elder sister of Case 1) presented with visual disturbance. She had been diagnosed to have bilateral iritis at Hiroshima Red Cross Hospital before visiting our hospital. Neurological examination and serological studies were normal. In both cases, left gluteal subcutaneous mass was detected and its biopsy revealed characteristic sarcoid nodules and confirmed the diagnosis of sarcoidosis. A tendency of familial occurrence and positive associations of the specific HLA antigens in sarcoidosis have been reported. Though the diagnosis of neurosarcoidosis has been difficult without extraneurological signs, sarcoidosis should be considered as a differential diagnosis in all the patients with myelopathy, and enhanced MRI and measure of CSF angiotensin converting enzyme seem to be useful for diagnosis and evaluation of drug effect during the course of steroid therapy.
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PMID:[Two siblings with sarcoidosis diagnosed by younger sister's central nervous symptoms]. 904 58

The hemorphins are a family of recently identified opioid receptor binding peptides derived from the proteolytic processing of the beta, gamma, delta, and epsilon chains of hemoglobin. They have previously been identified at high concentration in human pituitary glands and in the CSF of patients with cerebral bleeding. Hemorphins are potent inhibitors of angiotensin converting enzyme and therefore possibly have a role to play in blood pressure regulation. We report the presence of four hemorphin peptides in extracts of normal adrenal tissue and in pheochromocytoma tumors. The hemorphins were quantified and structurally characterized using mass spectrometry. High concentrations of hemorphins were found in all samples, comparable with the levels reported in the literature for pituitary and brain tissue.
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PMID:Mass spectrometric identification and quantification of hemorphins extracted from human adrenal and pheochromocytoma tissue. 908 45


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