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

---

Query: EC:3.1.1.7 (acetylcholinesterase)
28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.
...
PMID:Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 0 44

The role of intercellular pathways in the ADH-dependent water transport was studied on the frog urinary bladder by means of acetylcholine (AC) and other cholinergic compounds. AC (10(-3) M) was found to cause a strong suppression of the pituitrin-stimulated water flow. Analogous effect was produced by AC on the osmotic flow stimulated by cyclic adenosine monophosphate (cAMP) and theolin. The antipituitrin effect was not reproduced either by nicotine, nor by potent M-cholinomimetic agents (methylfurmetide and F-2268), and was not prevented by M- and N-cholynolytic drugs (atropine, metacin, flaxedil, hexamethonium). However, the antipituitrin effect of AC was completely removed by the anticholinesterase drugs with different mode of action (eserine, proserine, armin, acridine iodmethylate, GD-42) in concentrations of 10(-6)--10(-3) M. It was concluded that the smooth muscles contraction with the subsequent closure of the intercellular spaces was not responsible for the antipituitrinic action of AC. This effect appears to be connected with cholinesterase activation. A possible role of the phosphoinositides in the water permeability regulation of the urinary bladder wall is discussed.
...
PMID:[Effect of acetylcholine on the pituitrin induced osmotic flow of water through the wall of the frog urinary bladder]. 8 Oct 76

The epithelial cells in the taste buds of C. jacchus and C. penicillata show a moderate amount of ribonucleic acid an a concentration of a PAS-positive diastase-resistant material at their apical part. These cells are devoid of UDPG-GT, phosphorylases, G-6-PA, alanyl aminopeptidase, leucine aminopeptidase, cholinesterase and MAO; they present a weak reaction of F-1, 6-P Ald, LDH, SDH, MDH, cytochrome oxidase, beta-OHBDH, nonspecific esterase and acid phosphatase and a stronger reaction to ADH, NADPH2-TR, ATPases, alpha-GPDH, alkaline phosphatase, 5-nucleotidase and GDH. Although some enzymes (alkaline phosphatase, 5-nucleotidase and ATPases) have an almost uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller taste buds of the fungiform papillae. As a rule the apical part of the cells shows a stronger enzymatic reactivity. The taste buds of the marmosets are penetrated by acetylcholinesterase positive nerve fibers whereas the autonomic ganglia in the connective tissue contain both-acetyl and butyrylcholinesterase.
...
PMID:Histochemical observations on the taste buds of the marmosets (Callithrix jacchus and Callithrix penicillata). 15 39

The structure and histochemistry of the palmar and plantar skin were studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). In this skin there exist well-developed epidermal ridges, to which are attached one or two ducts of sweat glands. A thick stratum corneum can be seen in the epidermis, while a distinct stratum lucidum cannot be isolated from the other layers. The stratum granulosum is constituted by one or three layers of cells containing keratohyalin granules. Melanin granulations are mainly concentrated in the basal cells of the epidermal ridges. Dendritic melanocytes and amelanotic melanocytes containing alkaline phosphatase are found among the epidermal cells. Glycogen, UDPG-GT and phosphorylases are mainly present in the middle and lower Malpighian cells of the epidermal ridges. Alkaline phosphatase, ATPase, alanyl amino-peptidase and leucine aminopeptidase were absent in the epidermal cells. SDH, cytochrome oxidase, MAO and a certain number of NAD-dependent dehydrogenases (LDH, ADH, MDH, alpha-GPDH, beta-OHBDH and GDH) showed a stronger reactivity in the basal cells and Malpighian layer. The NADP-dependent enzymes (G-6-PDH, 6-PGDH, cis-aconistase and ICDH) were more reactive in the upper Malpighian layer and stratum granulosum. The stratum corneum showed some acid phosphatase and nonspecific esterase reactivity. The collagenous fibers intertwined with a small number of very thin elastic ones and a larger amount of reticular fibers run almost parallel to the epidermal ridges in the papillary body. In the reticular dermis some fibers are disposed transversely to the epidermal ridges. Meissner corpuscles reactive to butyrylcholinesterase, acetylcholinesterase, nonspecific esterase and G-6-PA are disposed at regular intervals and frequently at each side of the epidermal ridges. Pacinian corpuscles were found only in the hypodermis. The eccrine sweat glands contain glycogen, UDPG-GT and phosphorylase in their secretory, ductal and myoepithelial cells. The secretory part shows a uniform reactivity for every dehydrogenase because it contains only one type of cells (clear cells). The intraepidermal segment of the ducts shows a stronger reactivity to nonspecific esterase and NADP-dependent dehydrogenases than the epithelial cells around it.
...
PMID:The skin of the palms and soles of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 86

It was found that acetylcholine (ACh) at the concentration of 10(-3) M inhibited ADH-stimulated water transport through the wall of amphibian urinary bladder. This effect was suggested to be caused by an interaction of ACh with acetylcholinesterase (AChE) rather than by a stimulation of the M- or N-cholinoreceptor. The inhibitory action of ACh was completely suppressed in the presence of various AChE inhibitors (physostigmine, proserine, armine, Gd-42, acridine-iodmethylate), while an inhibitor of butyrylcholinesterase (BuChE), AD-4, failed to affect it. In accord with this observation the activity of AChE (but not of BuChE) was demonstrated in the urinary bladder epithelium. Since, in addition to the hydrosmotic effects of pituitrine, 8-arginine-vasopressin or oxytocin, ACh blocked also effects of forskolin or cyclic AMP, one may conclude that it acts at some post-cyclic AMP production stage. AChE-dependent inhibition of the ADH-stimulated water transport decreased significantly when the serosal pH was raising from 7.2 to 8.0, but was augmented by serosal acidification (pH 6.8), whereas such pH alterations did not affect the activity of the epithelium AChE. The effect of ACh under consideration was suppressed by adding amiloride (10(-4) M) to the serosal solution. Similarly, the ACh effect was blocked by an inhibitor of Ca-dependent K+ channels, 4-aminopyrdine, which in addition prevented the inhibition of the ADH-stimulated water transport by the serosal acidification. It was noteworthy that some other K+ channel blockers (Ba2+, Cs+, tetraethylammonium, apamine, quinine) did not affect either the water transport or the antipituitrine effect of ACh. In conclusion, we suggest that the inhibitory action of ACh on the ADH-stimulated water transport in the urinary bladder is mediated through the intracellular acidification resulting from ACh interaction with AChE. It is unlikely that the acidification is merely a consequence of the ACh hydrolysis, rather the ACh-AChE interaction induces directly an increase in the proton conductivity of the basolateral membrane of the urinary bladder epithelium.
...
PMID:[Acetylcholinesterase and the ADH-dependent transport of water in the amphibian bladder]. 181 71

Brain dead donor can not be maintained the systemic circulation more than 48 hours despite rather large dosage of catecholamine. The combined administration of arginine vasopressin (ADH) and catecholamine (epinephrine or dopamine) succeeded in long-term circulatory maintenance after brain death. We examined the renal and hepatic function by the method of circulatory maintenance. Twenty brain dead patients were randomly separated into two groups. Ten patients were maintained the systemic blood pressure with ADH and epinephrine (Group E). And the other ten were maintained with ADH and dopamine (Group D). Circulation was maintained with a small dosage of catecholamine at least six days in all donors. Urine output was well controlled, and serum BUN and creatinine were normal for 14 days. Daily creatinine clearance was always normal in both groups. Serum GPT, cholinesterase and alkaliphosphatase were the same in both groups, but total bilirubin was lower in group D than in group E on the seventh day. The combination of ADH and catecholamine preserved the kidney and liver after brain death for more than a week. This method will be of great value in organ transplantation from brain dead organ donors.
...
PMID:[Organ preservation with the combination of vasopressin and catecholamine in brain dead donors]. 188 89

Radiation inactivation is a method to determine the apparent target size of molecules. In this report we examined whether radiation inactivation of various enzymes and brain receptors is influenced by the preparation of samples preceding irradiation. The apparent target sizes of endogenous acetylcholinesterase and pyruvate kinase from rat brain and from rabbit muscle and benzodiazepine receptor from rat brain were investigated in some detail. In addition the target sizes of alcohol dehydrogenase (from yeast and horse liver), beta-galactosidase (from Escherichia coli), lactate dehydrogenase (endogenous from rat brain), and 5-HT2 receptors, acetylcholine muscarine receptors, and [35S] butyl bicyclophosphorothionate tertiary binding sites from rat brain were determined. The results show that apparent target sizes are highly influenced by the procedure applied for sample preparation before irradiation. The data indicate that irradiation of frozen whole tissue as opposed to lyophilized tissue or frozen tissue homogenates will estimate the smallest and most relevant functional target size of a receptor or an enzyme.
...
PMID:The apparent target size of rat brain benzodiazepine receptor, acetylcholinesterase, and pyruvate kinase is highly influenced by experimental conditions. 284 37

Ethylcholine mustard aziridinium ion (AF64A, MEChMAz) has been proposed as a cholinergic neuron-specific neurotoxin. We report that in further studies on its mechanism of action incubation of the cholinergic neuroblastoma X glioma cell line, NG-108-15, with 100 microM AF64A resulted in a rapid decrease in cellular choline acetyltransferase (ChAT) activity which preceded cytotoxicity. Thus, a 60-85% decrease in ChAT activity was measured within 5 h of AF64A exposure, whereas cell lysis (measured as the release of the cytosolic enzyme lactate dehydrogenase into the medium) did not become apparent until 18 h of AF64A exposure. This led us to examine the effects of AF64A on partially purified ChAT. We report a concentration- and time-dependent inhibition of partially purified ChAT by AF64A that could not be reversed by dialysis but could be prevented by coincubation of the enzyme and AF64A with choline but not with acetyl-coenzyme A. We present kinetic evidence that choline and AF64A compete for the same site on the enzyme. In addition, thiosulfate, which inactivates the aziridinium ion, eliminated AF64A's capacity to inhibit the enzyme. AF64A also irreversibly inhibited partially purified choline kinase and acetylcholinesterase but not lactate dehydrogenase, alcohol dehydrogenase, carboxypeptidase A, or chymotrypsinogen, enzymes that do not use choline as a substrate or product. Thus, the data suggest that AF64A acts as an irreversible active site directed inhibitor of ChAT and possibly other enzymes recognizing choline.
...
PMID:AF64A: an active site directed irreversible inhibitor of choline acetyltransferase. 383 98

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
...
PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

1. Neurones in the supraoptic nucleus were examined for their responsiveness to microiontophoretically applied monoamines and cholinomimetic agents. One hundred and sixty-one of the 749 neurones recorded were antidromically identified as neurosecretory cells.2. The monoamines, dopamine, noradrenaline and serotonin, reduced the activity of all cells which responded.3. Reduction in activity following noradrenaline administration was antagonized by the beta-adrenergic blocking agent MJ-1999 and potentiated by desmethylimipramine.4. Acetylcholine produced either a decrease or an increase in activity of responsive cells with depression the predominant result. Both the depressant and the excitatory response to acetylcholine were seen in individual neurosecretory cells which were depressed by noradrenaline.5. Application of acetyl-beta-methylcholine and carbaminoylcholine consistently resulted in depression of all responsive cells, while nicotine excited the majority of responsive cells. Both types of response were observed on the same neurosecretory cell.6. The depressant response was antagonized by the muscarinic blocking agent atropine while the excitatory response was antagonized by the nicotinic blocking agent dihydro-beta-erythroidine. Responses to acetylcholine were potentiated by the acetylcholinesterase inhibitor physostigmine.7. The data indicate that noradrenaline-containing terminals on these neurosecretory cells are likely to inhibit their discharge rate, while the presumed cholinergic terminals might function as either excitatory or inhibitory, depending on the receptor activated.8. These results support the hypothesis that ADH release is related to the neuronal activity of the supraoptic neurosecretory cell.
...
PMID:Noradrenaline and acetylcholine responses of supraoptic neurosecretory cells. 439 77


1 2 Next >>

---