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

In crude homogenates prepared from freeze-dried cryostate sections of various rat organs the Km and Vmax of acid and neutral alpha-glucosidase as well as the effect of the pH, substrate and enzyme concentration and the incubation time on the activity were determined fluorometrically with 4-methylumbelliferyl- and 2-naphthyl alpha-d-glucoside as substrates. On the basis of the biochemical data 2 assays were developed for the microchemical measurement of both alpha-glucosidases in groups of epithelial cells isolated from freeze dried cryostate sections of the epididymis, jejunum, ilium, liver and kidney of suckling and adult rats. The rate of hydrolysis of 2-naphthyl and 4-methylumbelliferyl alpha-d-glucoside differs moderately. However, due to the higher sensitivity of 4-methylumbelliferone the methylumbelliferyl derivative is preferable especially for the evaluation of alpha-d-glucosidases in cells with low enzyme activity.
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PMID:[Microchemical investigation of alpha D-glucosidases using 4-methylumnelliferyl- and 2-naphthyl-alpha-d-glucoside (author's transl)]. 1 80

Plasma membrane fractions from the brush border (BBM) and antiluminal (ALM) surfaces of the dog's renal proximal tubule cell were separated using free-flow electrophoresis. Rabbits immunized with BBM rapidly produced antibody, but rabbits immunized with ALM did not respond. Indirect immunofluorescence and immunoferritin studies showed that the antibody reacts with the brush border of the proximal tubules in the normal kidney of the adult dog. It also reacts with the surface membranes of certain other absorptive and secretory epithelia, such as gall bladder, small intestine, epididymis, and lacrimal gland. The antibody has affinity for the membrane maltase without affecting its catalytic activity, but does not appear to have affinity for the membrane alkaline phosphatase or the high affinity binding site for phlorizin present in the BBM. Polyacrylamide electrophoresis of solubilized BBM showed approximately 37 protein bands and four glycoproteins. We conclude that the proximal tubule cell is immunologically polarized with respect to the distribution of antigenic proteins, and that the BBM is highly antigenic. The antigenic components appear to be high molecular weight glycoproteins present in the glycocalyx.
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PMID:Immunologic characterization of plasma membranes from the renal proximal tubule of the dog. 89 9

The serum concentrations of FSH, LH, prolactin, testosterone, and estradiol and the enzymatic activities of hyaluronidase, glucosidases (alpha-glucosidase, beta-glucosidase, alpha-mannosidase, N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and beta-galactosidase), lactate dehydrogenase and its isoenzymes (LDH1, LDH2, LDH3, LDH-X, LDH4), and total proteins were measured in the semen of 69 subjects (8 normozoospermic controls, 7 secretory, and 54 excretory azoospermic subjects). FSH levels rose with the deterioration in spermatogenesis and served to differentiate the secretory from the excretory azoospermias. The only source of hyaluronidase and LDH-X in the ejaculate is the spermatozoa. alpha-Glucosidase activity essentially originates in the epididymis. The seminal determination of alpha-glucosidase and, to a lesser extent, alpha-mannosidase and N-acetyl-beta-D-glucosaminidase helps rapidly, sensitivity, reliably, and noninvasively to differentiate secretory azoospermias (with higher enzymatic activity) from the excretory type (less enzymatic activity) and may be of use in identifying with a certain degree of reliability the site of obstruction in the male genital tract.
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PMID:Enzyme and hormonal markers in the differential diagnosis of human azoospermia. 153 Mar 67

Epididymal function was evaluated in normozoospermic men and men with asthenoteratozoospermia using alpha-glucosidase as a secretory parameter. No difference was observed in the total quantity of the enzyme secreted into the ejaculate in spite of major differences between the two groups in the proportion of spermatozoa exhibiting progressive motility and normal morphology. In general, the secretion of alpha-glucosidase was positively correlated with the sperm concentration in the normozoospermic group, but not in asthenozoospermic subjects. The total enzyme contents of the ejaculate were significantly greater in men with asthenoteratozoospermia (sperm concentrations, greater than 35 x 10(6)/ml) than in subjects with severe oligoasthenoteratozoospermia (sperm concentrations less than 10 x 10(6)/ml, P less than 0.01) indicating a higher incidence of epididymal occlusion and/or dysfunction in the latter group. Within normozoospermic individuals, extremes in progressive motility or abnormal morphology could not be related to the quantities of enzyme when expressed per million sperm cells. It is concluded that if alpha-glucosidase is a reliable parameter of human epididymal secretory function, variation in the secretory function of the epididymis cannot explain the poor sperm quality observed in asthenoteratozoospermic individuals.
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PMID:Epididymal secretory function in men with asthenoteratozoospermia. 175 25

Three hundred eight-nine healthy, infertile patients were studied to determine the effects of inflammation on genital tract organs. Clinically silent inflammation was diagnosed by measuring polymorphonuclear granulocyte (PMN) elastase in semen. Seminal vesicle, prostate, and epididymis functions were assessed by measuring fructose, citric acid, and neutral alpha-glucosidase in semen. There was a significant relationship between high PMN elastase levels and low citric acid levels in semen; fructose and neutral alpha-glucosidase were not related to PMN elastase. Semen samples with increased PMN elastase levels (greater than 250 and greater than 1,000 ng/ml) showed a high incidence of pathologic citric acid levels (67% and 73%, respectively). These biochemical data indicate that the prostate is the main target in clinically silent male genital tract inflammation.
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PMID:Impact of clinically silent inflammation on male genital tract organs as reflected by biochemical markers in semen. 176 69

It has been suggested that alpha-glucosidase may be a marker of epididymal patency and function. Spermatozoal ATP concentrations decrease during passage through the epididymis, indicating efficient maturation. We correlated sperm motility with seminal plasma alpha-glucosidase activity and spermatozoal ATP. The sperm motility correlation with alpha-glucosidase activity was significantly positive, and the sperm motility correlation with spermatozoal ATP was significantly negative. It appears that high-alpha-glucosidase activity and low-spermatozoal ATP were present in semen with good sperm motility and could possibly indicate efficient epididymal function.
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PMID:alpha-Glucosidase, sperm ATP concentrations, and epididymal function. 187 46

Low spermatozoal ATP concentration in the presence of high alpha-glucosidase activity may indicate efficient epididymal function. It was suggested that detached ciliary tufts (DCTs) originated from the epididymis. We compared the spermatozoal ATP concentration and alpha-glucosidase activity in semen of patients with DCTs to that of a control group. Higher ATP concentration and lower alpha-glucosidase activity were found in patients with DCTs in their semen compared to the control group. These results might probably point out impaired epididymal function and further support the proposed epididymal origin of these tufts.
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PMID:Impaired epididymal function in patients with detached ciliary tufts in semen: a preliminary report. 195 21

Short-term vasectomy was studied in adult male rats in order to ascertain whether cytosolic or lysosomal hydrolases were differently affected 100 days after vas ligation. The secretory form of alpha-1,4-glucosidase remained unchanged while the lysosomal form of the enzyme and also cathepsin D increased in the cytosol of both caput and cauda epididymis. This set of data demonstrates for the first time that a triggering mechanism which stimulates lysosomal activity is present all along the rat epididymis. Disposal of the continuous influx of spermatozoa from the testis could therefore require both an active and a passive process.
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PMID:Fate of alpha-1,4-glucosidases and cathepsin D in the rat epididymis after vasectomy. 210 99

The seminal marker of epididymal function alpha-1, 4-glucosidase was localized histochemically in the cytoplasm of the efferent duct epithelium and the brush border of the entire length of the human epididymis. Quantification using the specific inhibitor castanospermine revealed strongest activity in the corpus and cauda regions. Selective inhibition of the brush border enzyme activities by maltotriose identified these as the neutral isoenzymes. Despite detection of alpha-glucosidase in the renal tubules of all the animals studied, the enzyme was not detectable in epididymides of hamsters or mice. In rabbits and monkeys, it was absent from the entire brush border but present weakly in the cytoplasm of the proximal epididymides. An enzyme distribution pattern similar to that in the human epididymis was found in rats, except for the absence of histochemical staining at pH 6.5 from the initial segment and distal cauda epididymidis. Experiments in which endogenous testosterone was depleted in rats demonstrated the dependence of epididymal alpha-glucosidase on androgen, albeit with a low sensitivity. This study suggests the rat to be a suitable model for the investigation of the role of epididymal alpha-glucosidase in fertility.
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PMID:Histochemical localization and quantification of alpha-glucosidase in the epididymis of men and laboratory animals. 211 30

The literature pertaining to epididymal proteins and their functions in fertilization is reviewed. Animal studies have indicated that specific epididymal proteins may be involved in aspects of sperm motility, sperm-zona binding and the acrosome reaction. If analogous proteins in the human exist, use could be made of them in the andrology clinic. Currently, only one specific epididymal protein (alpha-glucosidase) is routinely measured for semen analysis. Glucosidase secretion, in addition to reflecting inflammation of the organ, is used in conjunction with other markers of human fertility to identify patients with ductal occlusion for whom bypass operations may be useful therapy. Glucosidase inhibitors have been used to improve the assay, by establishing true semen blank values, and to quantify histochemical activity in frozen tissue sections. From its localization in the human corpus and cauda epididymidis, neutral glucosidase can not be used to identify occlusion in the proximal regions of the duct. Other proteins may be valuable markers of these regions. In the future, other specific proteins of epididymal origin found in seminal fluid could well illuminate dysfunction of the organ in cases of infertility or be end-points of the disruptive action of drugs aimed at the epididymis.
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PMID:Secretory proteins from the epididymis and their clinical relevance. 213 67


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