Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of the work was to specify the possibilities of the use of the enzymes of mediator metabolism: monoamine oxidase (MAO) of platelets, amine oxidase (AO) of serum and acetyl cholinesterase (ACE) of red blood cells to estimate the structure of depressions and to predict their therapeutic dynamics. 32 patients in the depressive phase of MDP were examined. There were 28 women and 4 men aged 22 to 50 years. The monopolar type was recorded in 28 patients, the bipolar one in 4 (all women). The total disease duration amounts to 0.5-17 years; depression may last from 2 months to 4 years. Depending on the type of the dominant affect the patients were distributed into 2 groups (10 persons had melancholic and 22 anxious depression). It has been shown that activity of platelet MAO and serum AO was significantly higher in anxious than in melancholic depression. An interrelationship was established between activity of these enzymes before treatment and prognosis of the treatment with tricyclic antidepressants. Activation of the enzymes during therapy was parallelled by positive clinical changes. Activity of platelet MAO turned out most significant in terms of prognosis. The data obtained are analyzed from the standpoint of regarding depression as a stressful condition, with the participation of the neurohormonal axis: the hypothalamus, pituitary, and adrenal cortex.
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PMID:[Significance of various enzymes of mediator metabolism for evaluation of depression and therapeutic prognosis]. 131 64

Endopeptidase-24.11 (sometimes referred to as 'enkephalinase') is a key cell-surface enzyme in the metabolism of neuropeptides. A previous immunohistochemical study mapped the enzyme in pig brain and indicated a striosomal ordering of the enzyme within the striatum. This point has now been confirmed by staining adjacent sections for acetylcholinesterase (by histochemistry) and endopeptidase-24.11 (by an immunoperoxidase method). While there were some general similarities in the mapping of these two hydrolases, e.g. in the caudate-putamen, globus pallidus, olfactory tubercle, substantia nigra and striatonigral tract, there were differences in intensity and in the microscopic distribution, e.g. as in striosomes for which acetylcholinesterase was diminished. Two other membrane peptidases, peptidyl dipeptidase A ('angiotensin converting enzyme') and aminopeptidase N, were also mapped by the same immunohistochemical method. Peptidyl dipeptidase A had some similarities with endopeptidase-24.11, e.g. in its concentration within the striatal nuclei, but clear differences were also apparent, in particular the absence of staining of the former in the globus pallidus and olfactory tubercle. Immunostaining for aminopeptidase N, in contrast to the other peptidases, was observed as a diffuse staining throughout the gray matter. At the microscopic level, two important differences were that staining for aminopeptidase N and peptidyl dipeptidase A was very intense throughout the vasculature of the brain and that striatal efferent bundles of unmyelinated fibres staining positively for endopeptidase-24.11 were depleted of the other two peptidases. All three peptidases were identified in the pia mater. Thus, endopeptidase-24.11, unlike peptidyl dipeptidase A and aminopeptidase N, is a marker for a set of striatal efferent fibres in pig brain.
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PMID:Endopeptidase-24.11 is striosomally ordered in pig brain and, in contrast to aminopeptidase N and peptidyl dipeptidase A ('angiotensin converting enzyme'), is a marker for a set of striatal efferent fibres. 290 57

After twenty weeks of continuous dosing with Trichostrongylus colubriformis larvae substantial, but declining, numbers of worms had persisted in most of the lambs examined, although there were wide inter-individual variations. Mucosal lesions were found in the proximal small intestines of all the infected animals, their severity being directly related to worm burden. Representative brush border enzyme activities analysed in intestinal mucosal extracts from the same lambs showed differing responses. Alkaline phosphatase and glycyl-L-leucine dipeptidase were significantly depleted, whereas maltase activity was only marginally reduced, and leucine aminopeptidase activity was normal. Mucosal acetylcholinesterase activity was significantly elevated in the parasitised animals and, interestingly in view of the postulated role of this enzyme in nematode pathogenicity, the level of activity was directly correlated with individual worm burdens. Intestinal trypsin and chymotrypsin activities were unaffected and the level of superoxide dismutase, an enzyme associated with the inflammatory response, was normal. There were also no consistent changes in the mucosal activities of several enzymes including lactic dehydrogenase, creatine phosphokinase, aldolase, and glutamic oxaloacetate transaminase, whose leakage from damaged or necrotic tissues has been well defined in terms of the concomitant increase in their activity in the circulation. Lambs treated orally with fenbendazole five and/or ten weeks before slaughter either in the presence or absence of continued larval intake, had negligible worm burdens, and showed little evidence of intestinal damage at post mortem. Brush border enzyme levels, with the exception of alkaline phosphatase and, in two cases dipeptidase, were normal in these animals. The activity of alkaline phosphatase was approximately double that in the continuously infected, untreated lambs, but remained markedly lower than in the uninfected controls. The activities of the other enzymes studied, including acetylcholinesterase, were within the control range. In summary, in chronic trichostrongylosis even relatively low nematode burdens were associated with marked pathological and biochemical damage in the intestine with both lesion severity and mucosal acetylcholinesterase activity being directly related to worm numbers. Although morphological integrity was completely restored after anthelmintic treatment, the persistent low activity of brush border alkaline phosphatase coupled with the enzymological findings in untreated, infected animals suggests that recovery of the full functional capability of the intestinal mucosa may take longer.
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PMID:Intestinal enzyme activity in lambs chronically infected with Trichostrongylus colubriformis: effect of anthelmintic treatment. 634 11

A new method to determine ureteral motility by means of radioisotopes is presented. After administration of 99m-Tc-MDP or 99m-Tc-DTPA urine transport within the ureter is documented by functional way-time-matrices. The special resolution results of a series of 7 to 12 regions of interest covering the ureter out of which the information about its motility is extracted from a series of 300 to 480 single pictures. The time resolution is 1 to 2.5 seconds. The observation period varies between 5 and 20 minutes. Urine transport is outlined as an declined stripe in the matrix. Retroperistaltic waves or dyskinesies can also be detected with this method. 31 patients in whom radical surgery was performed for carcinoma of the cervix were examined by the described functional ureter test. The results show that changes in ureteral function like frequency or quality or even retroperistaltic contractions of the ureter can be observed by the urokinetogram, changes which can be traced neither by isotope renogram nor by intervenous pyelography. Similar observations could be made in 10 patients treated by radiotherapy. In 26 patients the influence of sympathico- and parasympathicomimetic agents on the ureteral motility was studied. The results show that an increase of contraction frequency can be obtained by alpha- and betamimetics and also by cholinesterase inhibitors. These results which are in consistance with the available literature will be analysed and discussed in detail. The urokinetogram opens new possibilities to get insights into the physiology of urine transport and is therefore of great interest as an addition to radiologic and urodynamic methods.
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PMID:[New aspects of registration and drug influence of ureteral motility ]. 675 Sep 29

Several mammalian enzymes are anchored to the outer surface of the plasma membrane by a covalently attached glycosyl-phosphatidylinositol (GPI) structure. These include acetylcholinesterase, alkaline phosphatase, membrane dipeptidase and 5'-nucleotidase. All GPI anchors determined to date have the conserved core structure ethanolamine-PO4-6Man alpha 1-2Man alpha 1-6Man alpha 1-4GlcNH2 alpha 1-6myo-inositol-1-PO4- lipid. In most mammalian GPI anchors the lipid is 1-alkyl-2-acyl-glycerol, although in porcine membrane dipeptidase it is diacylglycerol. Attached to the conserved core are various side chain residues that appear to be either protein- or tissue-specific. In addition to membrane attachment, a GPI anchor may confer additional properties on the protein, such as the susceptibility to cleavage by phospholipases and the potential to cluster in detergent-insoluble domains. GPI anchors can also act as intracellular targeting signals, in transmembrane signalling, in the clathrin-independent endocytic process of potocytosis and as hormone mediators. Thus, a GPI anchor can confer additional properties on enzymes that may be important in their physiological and pathophysiological functioning.
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PMID:Glycosyl-phosphatidylinositol anchored membrane enzymes. 943 83