Insulin Degrading Enzyme
Mostrando 1-12 de 15 artigos, teses e dissertações.
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1. Efeito inibitÃrio do extrato aquoso do guaranÃ, do chà verde e da epigalocatecina-3 galato sobre a atividade da enzima que degrada a insulina em prÃstata de rato
Insulin degrading enzyme (IDE) is an intracellular protein that degrades insulin and others peptides and hormones. Insulin degradation is important both in the control of cellular responses to the hormone and in the interaction of the hormone with their target tissues. Multiple cellular functions are related to the IDE in addition to degradation, including b
Publicado em: 2006
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2. ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity
The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of
Brazilian Journal of Medical and Biological Research. Publicado em: 2001-11
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3. Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease.
Four monoclonal antibodies were identified by their ability to bind to 125I-labeled insulin covalently linked to a cytosolic insulin-degrading enzyme from human erythrocytes. All four antibodies were also found to remove more than 90% of the insulin-degrading activity from erythrocyte extracts. These antibodies were shown to be directed to different sites on
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4. Direct measurement of proinsulin in human plasma by the use of an insulin-degrading enzyme
A method has been described for the direct measurement of proinsulin in human plasma. The method makes use of an insulin-degrading enzyme designated “insulin-specific protease (ISP)”, which is obtained from rat skeletal muscle. Under the conditions used, this enzyme rapidly degrades insulin and insulin-like polypeptides to nonimmunoassayable components,
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5. Cellular distribution of insulin-degrading enzyme gene expression. Comparison with insulin and insulin-like growth factor receptors.
Insulin-degrading enzyme (IDE) hydrolyzes both insulin and IGFs and has been proposed to play a role in signal termination after binding of these peptides to their receptors. In situ hybridization was used to investigate the cellular distribution of IDE mRNA and to compare it with insulin receptor (IR) and IGF-I receptor (IGFR) gene expression in serial thin
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6. Purification of Insulin-Specific Protease by Affinity Chromatography
A single enzyme that proteolytically degrades insulin was isolated from rat skeletal muscle. This enzyme was purified 1000-fold by a series of steps, including affinity chromatography on insulin bound to agarose at the NH2-terminal phenylalanine of the B chain. Insulin linked to agarose at the B-29 lysine residue did not bind the enzyme and, therefore, was n
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7. Developmental regulation of an insulin-degrading enzyme from Drosophila melanogaster.
The precise mechanism by which insulin is degraded in mammalian cells is not presently known. Several lines of evidence suggest that degradation is initiated by a specific nonlysosomal insulin-degrading enzyme (IDE). The potential importance of this insulin protease is illustrated by the fact that there is an IDE in Drosophila melanogaster Kc cells that shar
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8. Insulin‐degrading enzyme is genetically associated with Alzheimer's disease in the Finnish population
The gene for insulin‐degrading enzyme (IDE), which is located at chromosome 10q24, has been previously proposed as a candidate gene for late‐onset Alzheimer's disease (AD) based on its ability to degrade amyloid β‐protein. Genotyping of single nucleotide polymorphisms (SNPs) in the IDE gene in Finnish patients with AD and controls revealed SNPs rs4646
BMJ Group.
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9. Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme
The intermediate filament (IF) protein nestin coassembles with vimentin and promotes the disassembly of these copolymers when vimentin is hyperphosphorylated during mitosis. The aim of this study is to determine the function of these nonfilamentous particles by identifying their interacting partners. In this study, we report that these disassembled vimentin/
The Federation of American Societies for Experimental Biology.
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10. Molecular Basis of Catalytic Chamber-assisted Unfolding and Cleavage of Human Insulin by Human Insulin-degrading Enzyme*S⃞
Insulin is a hormone vital for glucose homeostasis, and insulin-degrading enzyme (IDE) plays a key role in its clearance. IDE exhibits a remarkable specificity to degrade insulin without breaking the disulfide bonds that hold the insulin A and B chains together. Using Fourier transform ion cyclotron resonance (FTICR) mass spectrometry to obtain high mass
American Society for Biochemistry and Molecular Biology.
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11. Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo
Two substrates of insulin-degrading enzyme (IDE), amyloid β-protein (Aβ) and insulin, are critically important in the pathogenesis of Alzheimer's disease (AD) and type 2 diabetes mellitus (DM2), respectively. We previously identified IDE as a principal regulator of Aβ levels in neuronal and microglial cells. A small chromosomal region containing a mutant
The National Academy of Sciences.
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12. Degradation of the cleaved leader peptide of thiolase by a peroxisomal proteinase.
A peroxisomal location for insulin-degrading enzyme (IDE) has been defined by confocal immunofluorescence microscopy of stably transfected CHO cells overexpressing IDE and digitonin-permeabilization studies in normal nontransfected fibroblasts. The functional significance of IDE in degrading cleaved leader peptides of peroxisomal proteins targeted by the typ