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Misfolded proteinase K–resistant hyperphosphorylated α-synuclein in aged transgenic mice with locomotor deterioration and in human α-synucleinopathies
Manuela Neumann, … , Hans A. Kretzschmar, Christian Haass
Manuela Neumann, … , Hans A. Kretzschmar, Christian Haass
Published November 15, 2002
Citation Information: J Clin Invest. 2002;110(10):1429-1439. https://doi.org/10.1172/JCI15777.
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Article Neuroscience

Misfolded proteinase K–resistant hyperphosphorylated α-synuclein in aged transgenic mice with locomotor deterioration and in human α-synucleinopathies

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Abstract

Research Article

Authors

Manuela Neumann, Philipp J. Kahle, Benoit I. Giasson, Laurence Ozmen, Edilio Borroni, Will Spooren, Veronika Müller, Sabine Odoy, Hideo Fujiwara, Masato Hasegawa, Takeshi Iwatsubo, John Q. Trojanowski, Hans A. Kretzschmar, Christian Haass

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Figure 5

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Pathological αS hyperphosphorylation in transgenic mice. (a) Human αS, m...
Pathological αS hyperphosphorylation in transgenic mice. (a) Human αS, mouse αS, and human βS were incubated without (–) or with (+) casein kinase 1 (CK1), and 20 ng synuclein aliquots were Western-probed with phosphospecific anti-αS (p-SYN, upper panel), MC42 anti-αS, and 6485 anti-βS, respectively (SYN, lower panels). (b–e) Immunohistochemistry with phosphospecific anti-αS of the pontine reticular field (b–d) and ventral horn of the SC (e) from heterozygous mice aged 11 months (b) and 24 months (c) as well as from a homozygous mouse aged 9 months (d and e). Inset in d highlights phospho-αS–containing neuronal cytosolic inclusions and neuritic swellings. Scale bar, 100 μm in b–e, 50 μm in inset.

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