Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A series of marker enzymes for brush borders, basolateral membrane, and lysosomes were assayed in mucosal biopsy specimens from patients with untreated and treated coeliac disease and from controls. The brush border enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, and leucyl-beta-naphthylamidase showed reduced activities in the untreated state and complete or partial normalization during treatment. The lysosomal marker enzyme acid phosphatase increased in activity in untreated coeliac disease and was normalized by treatment. The brush border enzyme gamma-glutamyl transferase was nearly normal in untreated patients and slightly increased in treated patients. The basolateral membrane marker, 5'-nucleotidase, was reduced both in untreated and treated patients, whereas the lysosomal marker N-acetyl-beta-glucosaminidase was normal in the untreated state and decreased during treatment. The possible pathogenetic role of the three latter enzymes in coeliac disease is discussed. The patterns of the other enzymes are suggested to be attributable to the morphologic changes in the mucosa.
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PMID:Jejunal mucosal enzymes in untreated and treated coeliac disease. 667 55

Rectal biopsy specimens from control subjects, patients with either active or quiescent ulcerative colitis, and patients with Crohn's colitis were examined histologically and assayed for marker enzymes associated with tissue organelles. They were catalase (peroxisome); neutral alpha-glucosidase (endoplasmic reticulum); alkaline phosphatase (plasma membrane); malate dehydrogenase (mitochondria); lactate dehydrogenase (cytosol). There was no significant change in these enzyme activities in patient samples compared with controls. Activities of three acid hydrolases (lysosomal enzymes), beta-glucuronidase, acid phosphatase, and N-acetyl-beta-glucosaminidase, were also assayed in the biopsy samples. Decreased activities of all three enzymes were noted in ulcerative colitis, particularly in active disease. Normal values were obtained in Crohn's colitis. Measurement of lysosomal integrity by assays of latent N-acetyl-beta-glucosaminidase activity revealed similar results in control and colitic subjects. It is suggested that the lysosomal changes reflect a specific tissue release of enzyme and may be implicated in the pathogenesis of the tissue damage.
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PMID:Organelle pathology in ulcerative and Crohn's colitis with special reference to the lysosomal alterations. 671 88

Muscle hypertrophy was induced in the soleus muscle of young rats by tenotomy of the gastrocnemius and plantaris muscles. Three and 7 days afterwards the sciatic nerve was sectioned. The loss of weight of muscles subjected to this combined procedure three days after denervation was 30-40%. Lysosomal enzyme activities (acid phosphatase, alpha-glucosidase, beta-galactosidase and N-acetyl-beta-D-glucosaminidase) and energy enzyme activities (lactate dehydrogenase, LDH, triose-3-phosphate dehydrogenase, TPDH , D-hexokinase, HK and citrate synthase, CS) were determined 3 days after denervation, 3, 7 and 10 days after hypertrophy had been induced and 3 days after denervation of hypertrophying muscles on day 3 and 7. Normal non-operated rats of corresponding body weight served as controls and their enzyme activities were estimated on the same day. In the course of muscle hypertrophy, the 4 lysosomal enzyme activities increased progressively. Although 3 days' denervation of control muscles did not alter lysosomal enzyme activities, denervation of hypertrophying muscles greatly enhanced the activity of these enzymes. Enzymes of energy metabolism were affected to a lesser degree. The results suggest that denervation of hypertrophying muscles causes more extreme changes in muscle weight and lysosomal enzyme activities than denervation alone. The possible implications of this finding are discussed in relation to the rapid atrophy.
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PMID:Lysosomal and energy enzyme activities in hypertrophied rat soleus muscle after denervation. 671 25

The activity of acid hydrolases was studied in serum from patients with mucolipidosis (II and III) and other lysosomal disorders. In mucolipidosis II and III all hydrolases examined except alpha-glucosidase, beta-glucosidase and acid phosphatase were greatly increased. High values for beta-galactosidase were seen in mucopolysaccharidosis types I and II, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. N-Acetyl-beta-glucosaminidase activity was high in mucopolysaccharidosis types I, II, III and Gaucher's disease. The activity of beta-glucuronidase was increased in mucopolysaccharidosis types I, II and III, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. Acid phosphatase had increased activity only in Gaucher's disease. In several lysosomal storage disorders no increased values could be found. It is suggested that high values in serum from patients with lysosomal storage disorders (not including mucolipidosis II and III) may depend upon liver cell damage, which disturbs the clearing of acid hydrolases from serum.
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PMID:Acid hydrolases in serum from patients with lysosomal disorders. 676 92

The present study examines the role of cardiac lysosomal enzymes in the pathogenesis of the cardiomyopathy that develops in genetically diabetic C57BL/KsJ db+/db+ mice. Db+/db+ mice and littermate controls were sacrificed as age-matched pairs between 5-26 weeks of age. C57BL/6J ob/ob mice and littermates served as other controls. The hearts were excised, homogenized, and the following enzymatic activities measured: N-Acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosaminidase, aryl sulphatase, alpha-mannosidase, alpha-glucosidase, beta-galactosidase, beta glucosidase, total p-nitrophenyl phosphatase, acid phosphatase and 5'-phosphodiesterase type IV. There is a progressive decrease in cardiac lysosomal enzyme activities of db+/db+ mice for the period 5-21 weeks of age. All enzyme activity is depressed significantly during the 9-21 week interval with beta-glucuronidase, aryl sulphatase and beta-glucosidase decreased about 40-50%. The decrease in lysosomal enzyme activity can explain the accumulation of large residual bodies and interstitial material in the myocardium of the db+/db+ animals
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PMID:Lysosomal enzymes in experimental diabetic cardiomyopathy. 678 Feb 37

Several short- or long-term and longitudinal or cross-sectional studies have been conducted to ascertain the effect of vasectomy on circulating levels of gonadotropic and gonadal hormones and the function of assessory sex organs. Vasectomy does not cause noticeable changes in pituitary testicular axis. Changes, when they occur, are marginal and the hormone levels are still within normal physiological limits. The secretory function of both the prostate and the epididymis are changed as a result of vasectomy. There is a 2-fold increase in acid phosphatase in semen after vasectomy, indicating hyperfunction of the prostate. Both prostatic secretions and epididymal secretions decrease after vasectomy. 1 group of 12 men vasectomized for 1 week to 8 years were reanastomized and followed up for 12 months. Semen volume, seminal critic acid, maltase, glycerophosphorylcholine, prolactin, zinc, and magnesium returned to normal levels within 6 months, some within 1 month.
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PMID:Endocrine and accessory sex organ function after vasectomy and vasovasostomy. 679 97

The activities of various enzymes involved in detoxication and carbohydrate metabolism in the liver and the gastrointestinal tract of germfree (GF) and conventional (CV) rats, 8 and 40 weeks' old, were measured in relationship to intestinal microflora and aging. In 8-week-old rats, the activities of nitroreductase (NR) and aniline hydroxylase (AH) in the liver, and of alkaline phosphatase (ALP), maltase and lactase in the duodenum were higher in GF than in CV rats, but the activities of arginosuccinate synthetase (ASS) and lactate dehydrogenase (LDH) in the liver were higher in CV than in GF rats. In 40-week-old rats, the activities of NR and glucose-6-phosphatase dehydrogenase (G-6-PDH) of the liver and ALP, maltase and lactase of the duodenum were higher in GF than in CV rats, but those of ASS, UDP-glucuronyl transferase (UDP-GT), AH, beta-glucuronidase, and LDH of the liver were higher in CV than in GF rats. Compared between 8- and 40-week-old rats the activities of NR, beta-glucuronidase, LDH, and acid phosphatase increased with aging in both GF and CV rats. The specific activities of ASS in CV and UDP-GT and AH in GF rats decreased with aging. The total activities of ASS and AH in GF rats also decreased with aging. The activities of ALP, maltase and lactase decreased with aging in both GF and CV rats. Thus, these data suggested that there are influences of indigenous intestinal microflora and aging on the activities of various enzymes in the liver and gastrointestinal tract.
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PMID:Intestinal microflora and aging: age-related change of enzymes in the liver and the small intestine of germ-free and conventional rats. 679 85

Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.
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PMID:Alkaline phosphatase and acid lysosomal hydrolases in pancreatic juice and fibroblast cell cultures of patients with chronic calcifying pancreatitis. 680 85

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

This report describes a female patient with childhood form of acid maltase deficiency who survived till fifteen years old. Although acid alpha-1,4-glucosidase was deficient in the liver, kidney, skeletal and cardiac muscles, neutral alpha-1,4-glucosidase was present in normal concentrations in those organs. On light microscopic examination, numerous intracytoplasmic vacuoles containing acid phosphatase positive granules and PAS positive materials were present in both type 1 and 2 A fibers, predominantly in the latter. The striking finding in the present case was a selective type 2 fiber atrophy with type 2 B fiber deficiency believed to result from type 2 motor neuron dysfunction in the spinal cord. Electron microscopic study revealed extensive glycogen particle accumulation, autophagic vacuoles and myelin figures in the muscle fibers.
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PMID:Vacuolar myopathy with type 2 A fiber atrophy and type 2 B fiber deficiency. A case of childhood form acid alpha-1,4-glucosidase deficiency. 681 87


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