TY - JOUR
T1 - Different complicated brain pathologies in monozygotic twins with Gerstmann-Sträussler-Scheinker disease
AU - Honda, Hiroyuki
AU - Sasaki, Kensuke
AU - Takashima, Hiroshi
AU - Mori, Daisuke
AU - Koyama, Sachiko
AU - Suzuki, Satoshi
AU - Iwaki, Toru
N1 - Funding Information:
Send correspondence to: Hiroyuki Honda, MD, PhD, Department of Neuropathology, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-Ku, Fukuoka 812-8582, Japan; E-mail: h-hiroyu@np.med.kyushu-u.ac.jp Financial support: Grant-in-Aid for Scientific Research (17K07097 and 2629007) from the Japan Society for the Promotion of Science (JSPS).
Publisher Copyright:
© 2017 American Association of Neuropathologists, Inc.
PY - 2017/10
Y1 - 2017/10
N2 - Gerstmann-Sträussler-Scheinker disease (GSS) is an autosomal, dominantly inherited prion disease. In this study, we present different complicated brain pathologies determined postmortem of monozygotic GSS twin sisters. Case 1 showed cerebellar ataxia at the age of 58 years, and died at 66 years. Case 2 became symptomatic at the age of 75 years, and died at 79 years. There was a 17-year difference in the age of onset between the twins. Postmortem examination revealed numerous prion protein (PrP) plaques in the brains of both cases. The spongiform change and brain atrophy in case 1 were more severe compared with those in case 2. Western-blot analysis identified proteinase-resistant PrP (PrPres) at the molecular weight of 21-30 kDa and 8 kDa in the twins. Gel filtration revealed that PrPres was mainly composed of PrP oligomer. PrPres signal patterns were similar between the twins. Additionally, case 1 showed α-synucleinopathy and case 2 showed Alzheimer disease pathology. These different proteinopathies were involved in the amyloid plaque formations of both cases. The degree of GSS pathology was mainly related to disease duration. The amyloid plaque formations could be decorated by concomitant neuropathological changes such as a-synucleinopathy and tauopathy.
AB - Gerstmann-Sträussler-Scheinker disease (GSS) is an autosomal, dominantly inherited prion disease. In this study, we present different complicated brain pathologies determined postmortem of monozygotic GSS twin sisters. Case 1 showed cerebellar ataxia at the age of 58 years, and died at 66 years. Case 2 became symptomatic at the age of 75 years, and died at 79 years. There was a 17-year difference in the age of onset between the twins. Postmortem examination revealed numerous prion protein (PrP) plaques in the brains of both cases. The spongiform change and brain atrophy in case 1 were more severe compared with those in case 2. Western-blot analysis identified proteinase-resistant PrP (PrPres) at the molecular weight of 21-30 kDa and 8 kDa in the twins. Gel filtration revealed that PrPres was mainly composed of PrP oligomer. PrPres signal patterns were similar between the twins. Additionally, case 1 showed α-synucleinopathy and case 2 showed Alzheimer disease pathology. These different proteinopathies were involved in the amyloid plaque formations of both cases. The degree of GSS pathology was mainly related to disease duration. The amyloid plaque formations could be decorated by concomitant neuropathological changes such as a-synucleinopathy and tauopathy.
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U2 - 10.1093/jnen/nlx068
DO - 10.1093/jnen/nlx068
M3 - Article
C2 - 28922846
AN - SCOPUS:85030615829
SN - 0022-3069
VL - 76
SP - 854
EP - 863
JO - Journal of Neuropathology and Experimental Neurology
JF - Journal of Neuropathology and Experimental Neurology
IS - 10
ER -