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Digitale Medien

Regulation of liver and brain hexose monophosphate dehydrogenases by insulin and dietary intake in the female rat (1986)

Martins, Ralph N. ; Stokes, Gilbert B. ; Masters, Colin L.

Springer

Molecular and cellular biochemistry 70 (1986), S. 169-175

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ISSN: 1573-4919

Schlagwort(e): diabetic female rat ; glucose 6-phosphate dehydrogenase ; insulin ; liver ; brain ; adrenaline

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Chemie und Pharmazie , Medizin

Notizen: Summary Liver glucose 6-phosphate dehydrogenase and phosphogluconate dehydrogenase activities were significantly decreased in both diabetic and fasted rats. Treatment of diabetic rats with insulin resulted in liver glucose 6-phosphate dehydrogenase and phosphogluconate dehydrogenase activities that were significantly greater than controls. Insulin promoted an increase in food consumption that was blocked by adrenaline. Insulin, when administered together with adrenaline, restored hepatic glucose 6-phosphate dehydrogenase and phosphogluconate dehydrogenas activities of diabetic animals to control values, without altering food consumption. Brain glucose 6-phosphate dehydrogenase and phosphogluconate dehydrogenase activities were not significantly altered by either dietary restriction, diabetes or insulin treatment. These results demonstrate a dissociation between the action of insulin on hepatic glucose 6-phosphate dehydrogenase activity and its action to increase food intake.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00229431

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Digitale Medien

Characterization of the high affinity heparin binding site of the Alzheimer's disease βA4 amyloid precursor protein (APP) and its enhancement by zinc(II) (1995)

Maulthaup, Gerd ; Mechler, Hans ; Masters, Colin L.

Chicester [u.a.] : Wiley-Blackwell

Journal of Molecular Recognition 8 (1995), S. 247-257

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ISSN: 0952-3499

Schlagwort(e): APP ; heparin binding site ; zinc binding site ; processing of APP ; βA4 amyloid formation ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: The Alzheimer's disease βA4 amyloid precursor protein (APP) has been shown to be involved in a diverse set of biological protein precursor-like proteins (APLP1 and APLP2) belong to a superfamily of proteins that are probably functionally related. In order to characterize the cell adhesion properties of APP the brain specific isoform APP695 was purified and used to assess the binding to herparin, a structural and functional analogue of the glycosaminoglycan heparan sulfate. We show that APP binds in a time dependent and saturable manner to heparin. The salt concentration of 620 mM at which APP elutes from heparin Sepharose is greater than physiological. Tha apparent equilibrium constant for dissociation was determined to be 300 pM for APP binding to heparin Sepharose. A high affinity heparin binding site was identified within a region conversed in rodent and human APP, APLP1 and APLP2. This binding site was located between residues 316-337 of APP695 which is within the carbohydrate domain of APP. We also demonstrate an interaction between this heparin binding site and the zinc(II) binding site which is conserved in all members of the APP superfamily. We show by using an automated surface plasmon resonance biosensor (BIAcore, Pharmacia) that the affinity for heparin is increased two- to four-fold in the presence of micromolar zinc(II). The identification of zinc-enhanced binding of APP to heparin sulfate side chains of proteoglycans offers a molecular link between zinc(II), as a putative environmental toxin for Alzheimer's disease, and aggregation of amyloid βA4 protein.

Zusätzliches Material: 6 Ill.