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)

Brush-border membranes prepared from proximal and distal human small intestine were characterized with respect to lipid fluidity, lipid composition, and protein-lipid interactions. Steady-state fluorescence polarization and differential polarized phase fluorometry revealed that the "static" and "dynamic" rotational components of fluidity (assessed by r infinity values of 1,6-diphenyl-1,3,5-hexatriene and r values of 12-anthroylstearate, respectively) were greater in the distal membranes compared with their proximal counterparts. The lipid fluidity of distal brush-border membranes was also greater as measured by excimer/monomer fluorescence ratio intensities of pyrene decanoate. A lower molar ratio of cholesterol/phospholipid in the distal membranes was responsible for these regional fluidity differences. Lipid thermotropic transitions were detected at 26-28 degrees C using 1,6-diphenyl-1,3,5-hexatriene in proximal and distal membranes. Arrhenius plots of p-nitrophenylphosphatase and gamma-glutamyl transpeptidase activities demonstrated breakpoints in the vicinity of the lipid thermotropic transition temperatures (28-30 degrees C), whereas maltase and sucrase yielded a single activity slope over the range of 10-40 degrees C. Moreover, 50 mM benzyl alcohol fluidized proximal brush-border membranes and increased p-nitrophenylphosphatase activity in this membrane. This agent also shifted the phase transition temperature of the membrane and breakpoint temperature of this enzymatic activity from approximately 28 degrees C to 19 degrees C. These findings demonstrate that differences in human small intestinal brush-border membrane lipid fluidity and lipid composition exist between proximal and distal regions of this organ. Furthermore, alterations in fluidity and/or lipid composition modulate p-nitrophenylphosphatase and gamma-glutamyl transpeptidase but not sucrase or maltase activities in these membranes.
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PMID:Protein-lipid interactions in human small intestinal brush-border membranes. 259 11

Experiments were conducted, using a nonspecific lipid transfer protein, to vary the cholesterol/phospholipid molar ratio of rat proximal small intestinal microvillus membranes in order to assess the possible role of cholesterol in modulating enzymatic activities of this plasma membrane. Cholesterol/phospholipid molar ratios from 0.71 to 1.30 were produced from a normal value of 1.05 by incubation with the transfer protein and an excess of either phosphatidylcholine or cholesterol/phosphatidylcholine liposomes for 60 min at 37 degrees C. Cholesterol loading or depletion of the membranes was accompanied by a decrease or increase, respectively, in their lipid fluidity, as assessed by steady-state fluorescence polarization techniques using the lipid-soluble fluorophore 1,6-diphenyl-1,3,5-hexatriene. Increasing the cholesterol/phospholipid molar ratio also decreased alkaline phosphatase specific activity by approximately 20-30%, whereas decreasing this ratio increased this enzymatic activity by 20-30%. Sucrase, maltase, and lactase specific activities were not affected in these same preparations. Since the changes in alkaline phosphatase activity could be secondary to alterations in fluidity, cholesterol, or both, additional experiments were performed using benzyl alcohol, a known fluidizer. Benzyl alcohol (25 mM) restored the fluidity of cholesterol-enriched preparations to control levels, did not change the cholesterol/phospholipid molar ratio, and failed to alter alkaline phosphatase activity. These findings, therefore, indicate that alterations in the cholesterol content and cholesterol/phospholipid molar ratio of microvillus membranes can modulate alkaline phosphatase but not sucrase, maltase, or lactase activities. Moreover, membrane fluidity does not appear to be an important physiological regulator of these enzymatic activities.
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PMID:Cholesterol modulates alkaline phosphatase activity of rat intestinal microvillus membranes. 337 34