Transthyretin-Related Hereditary Amyloidosis in a Chinese Family with TTR Y114C Mutation

被引：12
|
作者：
Zhang, Yu [1 ,2 ]
Deng, Yu-Lei [1 ,2 ]
Ma, Jian-Fang [1 ,2 ]
Zheng, Lan [1 ,2 ]
Hong, Zhen [1 ,2 ]
Wang, Zhi-Quan [3 ,4 ]
Sheng, Cheng-Yu [3 ,4 ]
Xiao, Qin [1 ,2 ]
Cao, Li [1 ,2 ]
Chen, Sheng-Di [1 ,3 ,4 ]
机构：
[1] Shanghai Jiao Tong Univ, Sch Med, Ruijin Hosp Affiliated, Dept Neurol, Shanghai 200025, Peoples R China
[2] Shanghai Jiao Tong Univ, Sch Med, Ruijin Hosp Affiliated, Inst Neurol, Shanghai 200025, Peoples R China
[3] Chinese Acad Sci, Shanghai Inst Biol Sci, Lab Neurodegenerat Dis, Shanghai, Peoples R China
[4] Chinese Acad Sci, Key Lab Stem Cell Biol, Inst Hlth Sci, Shanghai Inst Biol Sci, Shanghai, Peoples R China
来源：
NEURODEGENERATIVE DISEASES | 2011年 / 8卷 / 04期
关键词：
Transthyretin-related hereditary amyloidosis; Extracellular-signal-regulated kinase 1/2; Tyr114Cys; Chinese; ELECTRON MICROSCOPE; PERIPHERAL NERVE; POLYNEUROPATHY; ACTIVATION; DISEASE;
D O I：
10.1159/000321679
中图分类号：
R74 [神经病学与精神病学];
学科分类号：
摘要：
Background: Transthyretin-related hereditary amyloidosis is an autosomal dominant inherited disease caused by mutations in the transthyretin (TTR) gene. Corresponding to the various transthyretin gene mutations and a wide range of geographical distribution, transthyretin-related hereditary amyloidosis presents diverse characteristics in genotype-phenotype correlation. Objective/Method: Here, we identify the clinical characteristics of a Chinese family affected by transthyretin-related hereditary amyloidosis with TTR Tyr114Cys mutation. Results/Conclusion: The pathogenic mechanism studies showed that the protein encoded by TTR Tyr114Cys is more easily depolymerized to form amyloid fibrils. Moreover, the cytotoxicity of the TTR Tyr114Cys may be attributed to its ability to persistently activate the extracellular-signal-regulated kinase 1/2 pathway. Copyright (C) 2010 S. Karger AG, Basel
引用
收藏
页码：187 / 193
页数：7
相关论文
共 50 条
  • [31] Ocular amyloid angiopathy associated with familial amyloidotic polyneuropathy caused by amyloidogenic transthyretin Y114C
    Kawaji, T
    Ando, Y
    Nakamura, M
    Yamashita, T
    Wakita, M
    Ando, E
    Hirata, A
    Tanihara, H
    OPHTHALMOLOGY, 2005, 112 (12) : 2212 - 2218
  • [32] Unusual self-association properties of transthyretin Y114C related to familial amyloidotic polyneuropathy: Effects on detection and quantification
    Ando, Y
    Almeida, MD
    Ohlsson, PI
    Ando, E
    Negi, A
    Suhr, O
    Terazaki, H
    Obayashi, K
    Ando, M
    Saraiva, MJM
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 261 (02) : 264 - 269
  • [33] Cardiac function in patients with transthyretin-related hereditary amyloidosis and its relation to other clinical parameters
    Gospodinova, M.
    Sarafov, S.
    Guergelcheva, V.
    Ivanova, R.
    Kirov, A.
    Todorov, T.
    Todorova, A.
    Tournev, I.
    Denchev, S.
    EUROPEAN JOURNAL OF HEART FAILURE, 2014, 16 : 118 - 118
  • [34] Hereditary Transthyretin-Related Amyloidosis Ongoing Observational Study: A Baseline Report of the First 3167 Participants
    Roesner, Sabine
    Pardo, Luba M.
    Bertoli-Avella, Aida M.
    Skrahina, Volha
    Engel, Pierre
    Schroeder, Sabine
    Zielske, Susan
    Bonke, Valerie
    Kreth, Janett
    Westphal, Gina
    Reder, Felix
    Skobalj, Snezana
    Zielke, Susanne
    Bogdanovic, Xenia
    Grieger, Paula
    Rennecke, Joerg
    Skripuletz, Thomas
    Patten, Monica
    Assmus, Birgit
    Hahn, Katrin
    Rolfs, Arndt
    Bauer, Peter
    JOURNAL OF CLINICAL MEDICINE, 2024, 13 (20)
  • [35] Effects of liver transplantation on hereditary cerebral amyloid angiopathy associated with ATTR Y114C
    Yamashita, T.
    Ando, Y.
    Ueda, M.
    Nakamura, M.
    Okamoto, S.
    Hirahara, T.
    Ueda, A.
    Misumi, Y.
    Obayashi, K.
    Uchino, M.
    XIth International Symposium on Amyloidosis, 2008, : 211 - 213
  • [36] TRANSTHYRETIN-RELATED AMYLOIDOSIS IN THE MEDITERRANEAN AND BALKAN AREA: FOCUS ON THE GLU89GLN MUTATION
    Milandri, A.
    Gospodinova, M.
    Mazzeo, A.
    Alfonzo, A.
    Stancanelli, C.
    Vita, G.
    Rapezzi, C.
    Tournev, I
    JOURNAL OF THE PERIPHERAL NERVOUS SYSTEM, 2016, 21 (03) : 281 - 281
  • [37] Disease profile and differential diagnosis of hereditary transthyretin-related amyloidosis with exclusively cardiac phenotype: an Italian perspective
    Rapezzi, Claudio
    Quarta, Candida Cristina
    Obici, Laura
    Perfetto, Federico
    Longhi, Simone
    Salvi, Fabrizio
    Biagini, Elena
    Lorenzini, Massimiliano
    Grigioni, Francesco
    Leone, Ornella
    Cappelli, Francesco
    Palladini, Giovanni
    Rimessi, Paola
    Ferlini, Alessandra
    Arpesella, Giorgio
    Pinna, Antonio Daniele
    Merlini, Giampaolo
    Perlini, Stefano
    EUROPEAN HEART JOURNAL, 2013, 34 (07) : 520 - 528
  • [38] Base to apex left ventricular longitudinal strain gradient in patients with hereditary transthyretin-related cardiac amyloidosis
    Gospodinova, M.
    Sarafov, S.
    Guergelcheva, V.
    Kuneva, Z.
    Vladimirova, L.
    Tournev, I.
    Denchev, S.
    EUROPEAN JOURNAL OF HEART FAILURE, 2014, 16 : 249 - 250
  • [39] Progressive Hereditary Transthyretin-Related Amyloidosis (ATTRv) Aggravated by ATTR Wild-Type and Complement Activation
    Mattig, Isabel
    Heidecker, Bettina
    Tschoepe, Carsten
    Messroghli, Daniel
    Eurich, Dennis
    Kleefeld, Felix
    Gaedeke, Jens
    Stenzel, Werner
    Schmidt, Hartmut H. -J
    Roecken, Christoph
    Knebel, Fabian
    Hahn, Katrin
    JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY, 2022, 81 (04): : 299 - 303
  • [40] Role of 99mTc-DPD Scintigraphy in Diagnosis and Prognosis of Hereditary Transthyretin-Related Cardiac Amyloidosis
    Rapezzi, Claudio
    Quarta, Candida C.
    Guidalotti, Pier Luigi
    Pettinato, Cinzia
    Fanti, Stefano
    Leone, Ornella
    Ferlini, Alessandra
    Longhi, Simone
    Lorenzini, Massimiliano
    Reggiani, Letizia Bacchi
    Gagliardi, Christian
    Gallo, Pamela
    Villani, Caterina
    Salvi, Fabrizio
    JACC-CARDIOVASCULAR IMAGING, 2011, 4 (06) : 659 - 670
12345