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Green Tea Amyloidosis

Manuel Hora, Martin Carballo-Pacheco, Benedikt Weber, Vanessa K Morris, Antje Wittkopf, Johannes Buchner, Birgit Strodel, Bernd Reif
Antibody light chain amyloidosis is a rare disease caused by fibril formation of secreted immunoglobulin light chains (LCs). The huge variety of antibody sequences puts a serious challenge to drug discovery. The green tea polyphenol epigallocatechin-3-gallate (EGCG) is known to interfere with fibril formation in general. Here we present solution- and solid-state NMR studies as well as MD simulations to characterise the interaction of EGCG with LC variable domains. We identified two distinct EGCG binding sites, both of which include a proline as an important recognition element...
January 27, 2017: Scientific Reports
Sohsuke Meshitsuka, Sumito Shingaki, Masatoshi Hotta, Miku Goto, Makoto Kobayashi, Yuuichi Ukawa, Yuko M Sagesaka, Yasuyo Wada, Masanori Nojima, Kenshi Suzuki
Previous studies have suggested that an increase in mitochondrial reactive oxygen species may cause organ damage in patients with light-chain (AL) amyloidosis; however, this damage can be decreased by antioxidant-agent treatment. Epigallocatechin gallate (EGCG), the major natural catechin in green tea, has potent antioxidant activity. Because EGCG has recently been reported to have a favorable toxicity profile for treating amyloidosis, we sought to examine the clinical efficacy and toxicity of EGCG in patients with AL amyloidosis...
March 2017: International Journal of Hematology
Hans L A Nienhuis, Johan Bijzet, Bouke P C Hazenberg
BACKGROUND: Amyloidosis has been a mystery for centuries, but research of the last decennia has clarified many of the secrets of this group of diseases. A protein-based classification of amyloidosis helps to understand problems that were part of the obsolete clinical classification in primary, secondary, and familial amyloidosis. All types of amyloid are secondary to some underlying precursor-producing process: each type is caused by a misfolded soluble precursor protein that becomes deposited as insoluble amyloid fibrils...
April 2016: Kidney Diseases
Xiang-Hua Huang, Zhi-Hong Liu
BACKGROUND: Amyloidosis includes a group of diseases characterized by the extracellular deposition of various fibrillary proteins that can autoaggregate in a highly abnormal fibrillary conformation. The amyloid precursor protein of systemic light-chain (AL) amyloidosis is comprised of monoclonal light chains that are due to plasma cell dyscrasia. The clinical presentation of patients with AL amyloidosis varies from patient to patient. Current treatment strategies target the clone in order to decrease the production of the pathologic light chains...
April 2016: Kidney Diseases
Fabian aus dem Siepen, Ralf Bauer, Matthias Aurich, Sebastian J Buss, Henning Steen, Klaus Altland, Hugo A Katus, Arnt V Kristen
BACKGROUND: Causative treatment of patients with wild-type transthyretin amyloid cardiomyopathy (wtATTR-CM) is lacking. Recent reports indicate the potential use of epigallocatechin-3-gallate (EGCG), the most abundant catechin in green tea, to inhibit amyloid fibril formation. We sought to investigate changes of cardiac function and morphology in patients with wtATTR-CM after consumption of green tea extract (GTE). METHODS: Twenty-five male patients (71 [64; 80] years) with wtATTR-CM were submitted to clinical examination, echocardiography, cardiac magnetic resonance imaging (cMRI) (n=14), and laboratory testing before and after daily consumption of GTE capsules containing 600 mg epigallocatechin-3-gallate for at least 12 months...
2015: Drug Design, Development and Therapy
Fabian aus dem Siepen, Sebastian J Buss, Florian Andre, Sebastian Seitz, Evangelos Giannitsis, Henning Steen, Hugo A Katus, Arnt V Kristen
OBJECTIVES: T1 mapping by cardiac magnetic resonance imaging (CMR) is able to determine the extracellular volume fraction. Wild-type transthyretin amyloidosis (WT-ATTR) is characterized by extracellular amyloid deposition in the heart. Recent reports indicated a reduction of left ventricular (LV) myocardial mass in WT-ATTR after consumption of epigallocatechin-3-gallate, the main catechin in green tea. It remained unclear, whether reduction of LV myocardial mass reflects decrease of amyloid load or progressive atrophy of cardiomyocytes...
August 2015: Clinical Research in Cardiology: Official Journal of the German Cardiac Society
Arnt V Kristen, Stephanie Lehrke, Sebastian Buss, Derliz Mereles, Henning Steen, Philipp Ehlermann, Stefan Hardt, Evangelos Giannitsis, Rupert Schreiner, Uwe Haberkorn, Philipp A Schnabel, Reinhold P Linke, Christoph Röcken, Erich E Wanker, Thomas J Dengler, Klaus Altland, Hugo A Katus
BACKGROUND: Treatment options in patients with amyloidotic transthyretin (ATTR) cardiomyopathy are limited. Epigallocatechin-3-gallate (EGCG), the most abundant catechin in green tea (GT), inhibits fibril formation from several amyloidogenic proteins in vitro. Thus, it might also halt progression of TTR amyloidosis. This is a single-center observational report on the effects of GT consumption in patients with ATTR cardiomopathy. METHODS: 19 patients with ATTR cardiomyopathy were evaluated by standard blood tests, echocardiography, and cardiac MRI (n = 9) before and after consumption of GT and/or green tea extracts (GTE) for 12 months...
October 2012: Clinical Research in Cardiology: Official Journal of the German Cardiac Society
Nelson Ferreira, Maria João Saraiva, Maria Rosário Almeida
BACKGROUND: Familial amyloidotic polyneuropathy (FAP) is a neurodegenerative disease caused by the extracellular deposition of mutant transthyretin (TTR), with special involvement of the peripheral nervous system (PNS). Currently, hepatic transplantation is considered the most efficient therapy to halt the progression of clinical symptoms in FAP since more than 95% of TTR is produced by the liver. However, less invasive and more reliable therapeutic approaches have been proposed for FAP therapy, namely based on drugs acting as inhibitors of amyloid formation or as amyloid disruptors...
2012: PloS One
Masanori Miyata, Takashi Sato, Miyuki Kugimiya, Misato Sho, Teruya Nakamura, Shinji Ikemizu, Mami Chirifu, Mineyuki Mizuguchi, Yuko Nabeshima, Yoshiaki Suwa, Hiroshi Morioka, Takao Arimori, Mary Ann Suico, Tsuyoshi Shuto, Yasuhiro Sako, Mamiko Momohara, Tomoaki Koga, Saori Morino-Koga, Yuriko Yamagata, Hirofumi Kai
Amyloid fibril formation is associated with protein misfolding disorders, including neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's diseases. Familial amyloid polyneuropathy (FAP) is a hereditary disease caused by a point mutation of the human plasma protein, transthyretin (TTR), which binds and transports thyroxine (T(4)). TTR variants contribute to the pathogenesis of amyloidosis by forming amyloid fibrils in the extracellular environment. A recent report showed that epigallocatechin 3-gallate (EGCG), the major polyphenol component of green tea, binds to TTR and suppresses TTR amyloid fibril formation...
July 27, 2010: Biochemistry
Derliz Mereles, Sebastian J Buss, Stefan E Hardt, Werner Hunstein, Hugo A Katus
BACKGROUND: Amyloid light chain (AL) amyloidosis is a rare disease with poor prognosis and limited therapeutic alternatives. Recently, one clinical case with cardiac involvement, as well as a compelling evidence of green tea polyphenol, epigallocatechin-3-gallate (EGCG), inducing the formation of benign aggregation products that do not polymerize into fibrils were published. This is a report of the cardiac effects of green tea consumption in these patients. METHODS: Patients with known cardiac involvement in AL amyloidosis were examined by routine cardiovascular examinations that took place every 3-6 months...
August 2010: Clinical Research in Cardiology: Official Journal of the German Cardiac Society
Nelson Ferreira, Isabel Cardoso, Maria Rosário Domingues, Rui Vitorino, Margarida Bastos, Guangyue Bai, Maria João Saraiva, Maria Rosário Almeida
More than 100 transthyretin (TTR) variants are associated with hereditary amyloidosis. Approaches for TTR amyloidosis that interfere with any step of the cascade of events leading to fibril formation have therapeutic potential. In this study we tested (-)-epigallocatechin-3-gallate (EGCG), the most abundant catechin of green tea, as an inhibitor of TTR amyloid formation. We demonstrate that EGCG binds to TTR "in vitro" and "ex vivo" and that EGCG inhibits TTR aggregation "in vitro" and in a cell culture system...
November 19, 2009: FEBS Letters
Derliz Mereles, Erich E Wanker, Hugo A Katus
No abstract text is available yet for this article.
May 2008: Clinical Research in Cardiology: Official Journal of the German Cardiac Society
Demian F Obregon, Kavon Rezai-Zadeh, Yun Bai, Nan Sun, Huayan Hou, Jared Ehrhart, Jin Zeng, Takashi Mori, Gary W Arendash, Doug Shytle, Terrence Town, Jun Tan
Recently, we have shown that green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG) exerts a beneficial role on reducing brain Abeta levels, resulting in mitigation of cerebral amyloidosis in a mouse model of Alzheimer disease. EGCG seems to accomplish this by modulating amyloid precursor protein (APP) processing, resulting in enhanced cleavage of the alpha-COOH-terminal fragment (alpha-CTF) of APP and corresponding elevation of the NH(2)-terminal APP product, soluble APP-alpha (sAPP-alpha). These beneficial effects were associated with increased alpha-secretase cleavage activity, but no significant alteration in beta-or gamma-secretase activities...
June 16, 2006: Journal of Biological Chemistry
Kavon Rezai-Zadeh, Doug Shytle, Nan Sun, Takashi Mori, Huayan Hou, Deborah Jeanniton, Jared Ehrhart, Kirk Townsend, Jin Zeng, David Morgan, John Hardy, Terrence Town, Jun Tan
Alzheimer's disease (AD) is a progressive neurodegenerative disorder pathologically characterized by deposition of beta-amyloid (Abeta) peptides as senile plaques in the brain. Recent studies suggest that green tea flavonoids may be used for the prevention and treatment of a variety of neurodegenerative diseases. Here, we report that (-)-epigallocatechin-3-gallate (EGCG), the main polyphenolic constituent of green tea, reduces Abeta generation in both murine neuron-like cells (N2a) transfected with the human "Swedish" mutant amyloid precursor protein (APP) and in primary neurons derived from Swedish mutant APP-overexpressing mice (Tg APPsw line 2576)...
September 21, 2005: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
Edward J Okello, Sergey U Savelev, Elaine K Perry
The primary target of licensed drugs for the treatment of Alzheimer's disease is the inhibition of the enzyme acetylcholinesterase, although preventing beta-amyloidosis is a prime target for drugs in development. The in vitro dual anti-cholinesterase and beta-secretase activities of Camellia sinensis L. extract (tea) is reported. Green and black tea inhibited human acetylcholinesterase (AChE) with IC(50) values of 0.03 mg/mL and 0.06 mg/mL respectively, and human butyrylcholinesterase (BuChE) with IC(50) values 0...
August 2004: Phytotherapy Research: PTR
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