Disease relevance of Ide

• This study was to detect the dynamical effects and mechanisms of CS on the activity of hepatic insulinase in CCl4 induced liver cirrhosis in rats [1].
• It belongs to the pitrilysin family and shows 24 and 34% identity with E. coli protease III (EC 3.4.24.54) and insulysin (EC 3.4.24.55) respectively [2].

Psychiatry related information on Ide

• Insulysin: an allosteric enzyme as a target for Alzheimer's disease [3].

High impact information on Ide

• A biotin-containing aldehyde-reactive probe (ARP) [Kubo, K., Ide, H., Wallace, S. S. & Kow, Y. W. (1992) Biochemistry 31, 3703-3708] is used to measure AP sites in living cells [4].
• Taken together, these data suggest that insulysin specificity is directed toward the amino side of hydrophobic and basic residues and that the enzyme has an extended substrate binding site [5].
• Insulin-degrading enzyme (IDE), which proteolytically degraded insulin with a high degree of specificity, was purified from pig skeletal muscle by ammonium sulfate precipitation, chromatography on Bio-Gel P-200 and DEAE-cellulose, and finally rechromatography on Sephadex G-200 (rechromatography fraction) [6].
• The activity of the insulin-degrading enzyme neutral cysteine proteinase (EC 3.4.22.11, insulinase) was studied in adipose tissue and in liver of nondiabetic, streptozotocin-diabetic, and insulin-treated diabetic rats [7].
• Insulin protease was purified 700-fold from rat liver homogenate by combined ultracentrifugation, ammonium sulfate fractionation, and glucagon-Sepharose-4B affinity chromatography [8].

Biological context of Ide

• Small peptide substrates increase the activity of insulysin toward the hydrolysis of A(beta)1-40 without affecting the activity of the enzyme toward insulin [3].
• The kinetics of the reaction of insulysin with the synthetic peptide substrate Abz-G-G-F-L-R-K-H-G-Q-EDDnp displays allosteric properties indicative of a regulated enzyme [3].

Anatomical context of Ide

• Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins [9].
• Insulin degrading enzyme activity was assessed in synaptosomes and high speed cytosol using [125I]insulin [10].
• Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques [11].

Associations of Ide with chemical compounds

• The insulysin-dependent cleavage of A(beta) prevents both the neurotoxic effects of the peptide as well as the ability of A(beta) to deposit onto synthetic amyloid plaques [3].
• Purification of nonantibiotic insulinase inhibitors from bacitracin [12].
• And radioimmunological assays were used to determine the changes of hyaluronic acid (HA), insulin levels in serum and the activity of hepatic insulinase [1].
• Biochemical studies on precatorine. (II) Insulinase inhibitory action of L-tryptophan and its N-methyl derivatives [13].

Analytical, diagnostic and therapeutic context of Ide

• Moreover, the elution profile of the endosomal acidic insulinase activity on a gel-filtration TSK-GEL G3000 SW(XL) high performance liquid chromatography column corresponded exactly with the elution profile of the immunoreactive 45-kDa mature form of endosomal CD [14].
• Dynamical influence of Cordyceps sinensis on the activity of hepatic insulinase of experimental liver cirrhosis [1].

References