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)

To further document the effect of insulin on intestinal maturation, suckling rats were treated either with exogenous insulin (12.5 mU.g body wt, intraperitoneally, twice daily) or with saline from d 8 to 12 postpartum. Sucrase activity in brush border membrane extracts was precociously induced by insulin, whereas the activities of other brush border membrane enzymes (maltase, aminopeptidase, and neutral lactase) were enhanced (+ 30 to + 131%, p less than 0.01 versus controls). The lysosomal enzyme, N-acetyl-beta-glucosaminidase, which normally declines at weaning was significantly (p less than 0.025) decreased in both villus (-51%) and crypt cells (-57%) isolated from the jejunum of insulin-treated rats. The microsomal enzyme, sulfatase C, and the cytosolic enzyme, lactate dehydrogenase, were also sensitive to insulin with decreases in activity ranging from -37 to -63% (p less than 0.05) compared to saline-treated control rats. Insulin at doses of 0.5 or 12.5 mU did not influence plasma total corticosterone levels, which were about 9-fold lower in suckling than in 25-d-old weaned rats. In weaned rats (from d 25 to 32) insulin treatment (12.5 mU) failed to influence the activity of brush border membrane hydrolases or of lysosomal, microsomal, and cytosolic enzymes. The synthesis rate of mature sucrase-isomaltase, measured in weaned rats (32 d) by the incorporation of 14C-leucine into the enzyme precursor protein, was equivalent in both groups. These data demonstrate that the immature enterocyte of the suckling rat is responsive to insulin, whereas the mature enterocyte of the weaned rat is unresponsive.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Hormonal regulation of the rat small intestine: responsiveness of villus and crypt cells to insulin during the suckling period and unresponsiveness after weaning. 217 34

The purpose of the present study was to determine the role of cardiac lysosomal enzymes in the pathogenesis of the cardiomyopathy that develops in the genetically diabetic C57BL/KsJ db+/db+ mice. Db+/db+ mice and littermate controls were sacrificed as age-matched pairs between 5 and 26 weeks of age. C57BL/6J ob/ob mice and littermates served as other controls. Following anesthesia, the hearts were excised, homogenized, and the following enzymatic activities measured: N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosaminidase, aryl sulfatase, alpha-mannosidase, alpha-glucosidase, beta-galactosidase, beta-glucosidase, total rho-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 to 21 weeks of age. All enzyme activity is depressed significantly during the 9- to 21-week interval: alpha-glucosidase, beta-glucosidase, alpha-mannosidase, beta-galactosidase, acid phosphatase, N-acetyl-beta-galactosaminidase, 5'-phosphodiesterase type IV, and total rho-nitrophenyl phosphatase are reduced approximately 10 to 20 per cent, whereas beta-glucosaminidase, aryl sulfatase, and N-acetyl-beta-glucosaminidase are decreased almost 40 to 50 per cent. In contrast, cardiac lysosomal enzymic activity in the ob/ob mice does not differ significantly from controls aside from aryl sulfatase (20 per cent decrease) and beta-glucosidase (10 per cent decrease). This decrease in lysosomal enzyme activity can explain the accumulation of large residual bodies and interstitial material that occurs in the myocardium of the db+/db+ animals as part of the cardiomyopathy.
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PMID:Lysosomal enzymes in the heart of the genetically diabetic mouse. 742 Nov 26