scholarly journals Ovariectomy increases neuronal amyloid-β binding alcohol dehydrogenase level in the mouse hippocampus

2008 ◽  
Vol 52 (7) ◽  
pp. 1358-1364 ◽  
Author(s):  
Emiko Fukuzaki ◽  
Kazuhiro Takuma ◽  
Yoko Funatsu ◽  
Yukiko Himeno ◽  
Yuko Kitahara ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Amyloid Β ◽  
Mouse Hippocampus

Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/Amyloid-β binding alcohol dehydrogenase (ABAD)

2000 ◽  
Vol 303 (2) ◽  
pp. 311-327 ◽  
Author(s):  
A.J Powell ◽  
J.A Read ◽  
M.J Banfield ◽  
F Gunn-Moore ◽  
S.D Yan ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Amyloid Β ◽  
Type Ii ◽  
Hydroxyacyl Coa Dehydrogenase

Computational optimization of AG18051 inhibitor for amyloid-β binding alcohol dehydrogenase enzyme

2008 ◽  
Vol 108 (11) ◽  
pp. 1982-1991 ◽  
Author(s):  
Alexandra T. Marques ◽  
Agostinho Antunes ◽  
Pedro A. Fernandes ◽  
Maria J. Ramos
Keyword(s):  
Alcohol Dehydrogenase ◽  
Amyloid Β ◽  
Computational Optimization ◽  
Dehydrogenase Enzyme

Neuroprotective effects of N-adamantyl-4-methylthiazol-2-amine against amyloid β-induced oxidative stress in mouse hippocampus

2017 ◽  
Vol 128 ◽  
pp. 22-28 ◽  
Author(s):  
Jiae Kim ◽  
Chang Hun Cho ◽  
Hoh-Gyu Hahn ◽  
Soo-Young Choi ◽  
Sung-Woo Cho
Keyword(s):  
Oxidative Stress ◽  
Amyloid Β ◽  
Neuroprotective Effects ◽  
Mouse Hippocampus

scholarly journals Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase

1999 ◽  
Vol 345 (1) ◽  
pp. 139-143 ◽  
Author(s):  
Xue-Ying HE ◽  
Ying-Zi YANG ◽  
Horst SCHULZ ◽  
Song-Yu YANG
Keyword(s):  
Alcohol Dehydrogenase ◽  
Catalytic Properties ◽  
Amyloid Β ◽  
Hydroxysteroid Dehydrogenase ◽  
Amino Acid Sequences ◽  
Short Chain ◽  
Amyloid Β Peptide ◽  
Kinetic Measurements ◽  
Hydroxyacyl Coa Dehydrogenase ◽  
Adh Activity

The alcohol dehydrogenase (ADH) activity of human short-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) has been characterized kinetically. The kcat of the purified enzyme was estimated to be 2.2 min-1, with apparent Km values of 280 mM and 22μM for 2-propanol and NAD+, respectively. The kcat of the ADH activity was three orders of magnitude less than the L-3-hydroxyacyl-CoA dehydrogenase activity but was comparable with that of the enzyme's hydroxysteroid dehydrogenase (HSD) activity for oxidizing 17β-oestradiol [He, Merz, Mehta, Schulz and Yang (1999) J. Biol. Chem. 274, 15014-15019]. However, the kcat values of intrinsic ADH and HSD activities of human SCHAD were found to be two orders of magnitude less than those reported for endoplasmic-reticulum-associated amyloid β-peptide-binding protein (ERAB) [Yan, Shi, Zhu, Fu, Zhu, Zhu, Gibson, Stern, Collison, Al-Mohanna et al. (1999) J. Biol. Chem. 274, 2145-2156]. Since human SCHAD and ERAB apparently possess identical amino acid sequences, their catalytic properties should be identical. The recombinant SCHAD has been confirmed to be the right gene product and not a mutant variant. Steady-state kinetic measurements and quantitative analyses reveal that assay conditions such as pH and concentrations of coenzyme and substrate do not account for the kinetic differences reported for ERAB and SCHAD. Rather problematic experimental procedures appear to be responsible for the unrealistically high catalytic rate constants of ERAB. Eliminating the confusion surrounding the catalytic properties of this important multifunctional enzyme paves the way for exploring its role(s) in the pathogenesis of Alzheimer's disease.

Selective Impairment of Some Forms of Synaptic Plasticity by Oligomeric Amyloid-β Peptide in the Mouse Hippocampus: Implication of Extrasynaptic NMDA Receptors

2012 ◽  
Vol 32 (1) ◽  
pp. 183-196 ◽  
Author(s):  
Myriam Kervern ◽  
Arnaud Angeli ◽  
Olivier Nicole ◽  
Frédéric Léveillé ◽  
Bénédicte Parent ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Nmda Receptors ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Mouse Hippocampus ◽  
Selective Impairment

Cytoprotective role of mitochondrial amyloid β peptide-binding alcohol dehydrogenase against a cytotoxic aldehyde

2009 ◽  
Vol 30 (2) ◽  
pp. 325-329 ◽  
Author(s):  
Yayoi Murakami ◽  
Ikuroh Ohsawa ◽  
Tadashi Kasahara ◽  
Shigeo Ohta
Keyword(s):  
Alcohol Dehydrogenase ◽  
Peptide Binding ◽  
Amyloid Β ◽  
Amyloid Β Peptide

scholarly journals Amyloid β-Peptide-binding Alcohol Dehydrogenase Is a Component of the Cellular Response to Nutritional Stress

2000 ◽  
Vol 275 (35) ◽  
pp. 27100-27109
Author(s):  
Shi Du Yan ◽  
Yucui Zhu ◽  
Eric D. Stern ◽  
Yuying C. Hwang ◽  
Osamu Hori ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Cellular Response ◽  
Peptide Binding ◽  
Amyloid Β ◽  
Nutritional Stress ◽  
Amyloid Β Peptide
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