Effects of an inhibitor of α-secretase, which metabolizes the amyloid peptide precursor, on memory formation in rats

被引：6

作者：

Dubrovskaya N.M. ^{[1
]}

Nalivaeva N.N. ^{[1
,2
]}

Turner A.J. ^{[2
]}

Zhuravin I.A. ^{[1
]}

机构：

[1] I. M. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg

[2] Department of Biochemistry and Microbiology, Leeds

来源：

Neuroscience and Behavioral Physiology | 2006年 / 36卷 / 9期

基金：

俄罗斯基础研究基金会;

关键词：

Alpha-secretase; Alzheimer's disease; Amyloid precursor protein; Batimastat; Behavior; Cortex; Memory;

D O I：

10.1007/s11055-006-0106-9

中图分类号：

学科分类号：

摘要：

Intracortical administration of 10-4 M batimastat, a specific inhibitor of α-secretase (a metalloproteinase which cleaves the amyloid peptide precursor), decreased the number of correct runs in a single-level eight-arm maze to 92.78 ± 1.03% compared with baseline (p < 0.01) within 60 min. However, injection of batimastat into the cerebral cortex of animals during the early postnatal period (days 5 and 7 of life) led to impaired orientation in the simple single-level maze when these adults reached adulthood (90.92 7plusmn; 2.21% correct runs, p < 0.001) as compared with controls. The data obtained here provide evidence for the important role of α-secretase in memory processes. The possible role of α-secretase in memory processes and the pathogenesis of Alzheimer's disease is discussed. © Springer Science+Business Media, Inc. 2006.

引用

页码：911 / 913

页数：2

共 14 条

[1]

Buresh Ya., Bureshova O., Houston P.J., Methods and Basic Experiments for Studies of the Brain and Behavior, (1991)

[2]

Zhuravin I.A., Dubrovsksya N.M., Kochkina E.G., Nalivaeva N.N., Plesneva S.A., The role of the conditions of embryonic development in the formation of learning mechanisms during mammalian ontogenesis, Ros. Fiziol. Zh., 90, 8, pp. 173-174, (2004)

[3]

Zhuravin I.A., Tumanova N.L., Dubrovskaya N.M., Fedoseeva K.N., Impairments to the formation of the paleo-and neocortex in altered conditions of embryonic development, Zh. Évolyuts. Biokhim. Fiziol., 39, 6, pp. 609-618, (2003)

[4]

Bour A., Little S., Dodart J.C., Kelche C., Mathis C., A secreted form of the beta-amyloid precursor protein (sAPP695) improves spatial recognition memory in OF1 mice, Neurobiol. Learn. Mem., 81, pp. 27-38, (2004)

[5]

Caille I., Allinquant B., Dupont E., Bouillot C., Langer A., Muller U., Prochiantz A., Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone, Development, 131, pp. 2173-2181, (2004)

[6]

Fifkova E., Marsala J., Stereotaxic atlases for the cat, rabbit and rat, Electrophysiological Methods in Biological Research, pp. 653-695, (1967)

[7]

Kaether C., Haass C., A lipid boundary separates APP and secretases and limits amyloid β-peptide generation, J. Cell. Biol., 167, pp. 809-812, (2004)

[8]

Lichtenthaler S.F., Haass C., Amyloid at the cutting edge: Activation of α-secretase prevents amyloidogenesis in an Alzheimer disease mouse model, J. Clin. Invest., 113, pp. 1384-1387, (2004)

[9]

Mattson M.P., Cellular action of β-amyloid precursor protein and its soluble and fibrillogenic derivatives, Physiol. Rev., 77, pp. 1081-1132, (1999)

[10]

Nalivaeva N.N., Fisk L., Canet Aviles R.M., Plesneva S.A., Zhuravin I.A., Turner A.J., Effect of prenatal hypoxia on expression of amyloid precursor protein and metallopeptidases in the rat brain, Lett. Peptide Sci., 10, pp. 455-462, (2004)

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