Search

Your search keyword '"Kayed R"' showing total 5 results
Start Over Author "Kayed R" Database OpenAIRE
5 results on '"Kayed R"'

1. Aβ Amyloid Pathology Affects the Hearts of Patients With Alzheimer's Disease: Mind the Heart

Author

Troncone L., Luciani M., Coggins M., Wilker E. H., Ho C. -Y., Codispoti K. E., Frosch M. P., Kayed R., del Monte F., Troncone L., Luciani M., Coggins M., Wilker E.H., Ho C.-Y., Codispoti K.E., Frosch M.P., Kayed R., and del Monte F.

Subjects
Aged, 80 and over, Cross-Sectional Studie, Male, amyloidosi, Aging, Amyloid beta-Peptide, Myocardium, Immunoblotting, heart failure, Brain, Enzyme-Linked Immunosorbent Assay, Immunohistochemistry, protein aggregate, Microscopy, Electron, Transmission, Alzheimer Disease, Female, cardiomyopathy, dementia, Aged, Cardiomyopathie, Human, Retrospective Studies
Abstract

Background Individually, heart failure (HF) and Alzheimer's disease (AD) are severe threats to population health, and their potential coexistence is an alarming prospect. In addition to sharing analogous epidemiological and genetic profiles, biochemical characteristics, and common triggers, the authors recently recognized common molecular and pathological features between the 2 conditions. Whereas cognitive impairment has been linked to HF through perfusion defects, angiopathy, and inflammation, whether patients with AD present with myocardial dysfunction, and if the 2conditions bear a common pathogenesis as neglected siblings are unknown. Objectives Here, the authors investigated whether amyloid beta (Aβ) protein aggregates are present in the hearts of patients with a primary diagnosis of AD, affecting myocardial function. Methods The authors examined myocardial function in a retrospective cross-sectional study from a cohort of AD patients and age-matched controls. Imaging and proteomics approaches were used to identify and quantify Aβ deposits in AD heart and brain specimens compared with controls. Cell shortening and calcium transients were measured on isolated adult cardiomyocytes. Results Echocardiographic measurements of myocardial function suggest that patients with AD present with an anticipated diastolic dysfunction. As in the brain, Aβ40 and Aβ42 are present in the heart, and their expression is increased in AD. Conclusions Here, the authors provide the first report of the presence of compromised myocardial function and intramyocardial deposits of Aβ in AD patients. The findings depict a novel biological framework in which AD may beviewed either as a systemic disease or as a metastatic disorder leading to heart, and possibly multiorgan failure. ADandHF are both debilitating and life-threatening conditions, affecting enormous patient populations. Our findingsunderline a previously dismissed problem of a magnitude that will require new diagnostic approaches andtreatmentsforbrain and heart disease, and their combination.

Published
2016

3. Immunotherapy for the treatment of Alzheimer's disease: amyloid-β or tau, which is the right target?

Author

Castillo-Carranza DL, Guerrero-Muñoz MJ, and Kayed R

Subjects
lcsh:Immunologic diseases. Allergy, β-amyloid, Immunotherapy, tau, lcsh:RC581-607, Alzheimer’s disease
Abstract

Diana L Castillo-Carranza,1,2 Marcos J Guerrero-Muñoz,1,2 Rakez Kayed1–31Mitchell Center for Neurodegenerative Diseases, 2Departments of Neurology, Neuroscience, and Cell Biology, 3Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston, TX, USAAbstract: Alzheimer's disease (AD) is characterized by the presence of amyloid plaques composed mainly of amyloid-β (Aβ) protein. Overproduction or slow clearance of Aβ initiates a cascade of pathologic events that may lead to formation of neurofibrillary tangles, neuronal cell death, and dementia. Although immunotherapy in animal models has been demonstrated to be successful at removing plaques or prefibrillar forms of Aβ, clinical trials have yielded disappointing results. The lack of substantial cognitive improvement obtained by targeting Aβ raises the question of whether or not this is the correct target. Another important pathologic process in the AD brain is tau aggregation, which seems to become independent once initiated. Recent studies targeting tau in AD mouse models have displayed evidence of cognitive improvement, providing a novel therapeutic approach for the treatment of AD. In this review, we describe new advances in immunotherapy targeting Aβ peptide and tau protein, as well as future directions.Keywords: immunotherapy, Alzheimer's disease, β-amyloid, tau

Published
2013

4. Curcumin as Scaffold for Drug Discovery against Neurodegenerative Diseases

Author

Paola Marzullo, Rakez Kayed, Filippa Lo Cascio, Antonio Palumbo Piccionello, Lo Cascio F., Marzullo P., Kayed R., and Palumbo Piccionello A.

Subjects
Scaffold, Drug discovery, business.industry, Medicine (miscellaneous), amyloid, Settore CHIM/06 - Chimica Organica, Review, Disease, Metabolic stability, Bioinformatics, General Biochemistry, Genetics and Molecular Biology, chemistry.chemical_compound, chemistry, lcsh:Biology (General), Curcumin, Medicine, curcumin, tau, business, Alzheimer’s disease, lcsh:QH301-705.5
Abstract

Neurodegenerative diseases (NDs) are one of major public health problems and their impact is continuously growing. Curcumin has been proposed for the treatment of several of these pathologies, such as Alzheimer’s disease (AD) and Parkinson’s disease (PD) due to the ability of this molecule to reduce inflammation and aggregation of involved proteins. Nevertheless, the poor metabolic stability and bioavailability of curcumin reduce the possibilities of its practical use. For these reasons, many curcumin derivatives were synthetized in order to overcome some limitations. In this review will be highlighted recent results on modification of curcumin scaffold in the search of new effective therapeutic agents against NDs, with particular emphasis on AD.

Published
2021

5. Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

Author

Ruth Nussinov, Pritam Ganguly, Son Tung Ngo, Carol K. Hall, John E. Straub, Laura Dominguez, Alfonso De Simone, Guanghong Wei, Bikash R. Sahoo, Brianna Hnath, Ayyalusamy Ramamoorthy, Sylvain Lesné, Fabio Sterpone, Simone Melchionna, Nikolay V. Dokholyan, Yiming Wang, Jie Zheng, Rakez Kayed, Jiaxing Chen, Birgit Habenstein, Peter Faller, Philippe Derreumaux, Antoine Loquet, Mara Chiricotto, Birgit Strodel, Buyong Ma, Stepan Timr, James McCarty, Phuong H. Nguyen, Mai Suan Li, Andrew J. Doig, Joan-Emma Shea, Saeed Najafi, Yifat Miller, Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J. -E., Dokholyan, N. V., De Simone, A., Ma, B., Nussinov, R., Najafi, S., Ngo, S. T., Loquet, A., Chiricotto, M., Ganguly, P., Mccarty, J., Li, M. S., Hall, C., Wang, Y., Miller, Y., Melchionna, S., Habenstein, B., Timr, S., Chen, J., Hnath, B., Strodel, B., Kayed, R., Lesne, S., Wei, G., Sterpone, F., Doig, A. J., Derreumaux, P., Laboratoire de biochimie théorique [Paris] (LBT (UPR_9080)), Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Laura Dominguez gratefully acknowledges the support of PAIP 5000-9155, LANCAD-UNAM-DGTIC-306, and CONACyT Ciencia Básica A1-S-8866. John E. Straub gratefully acknowledges the generous support of the National Science Foundation (Grant No. CHE-1900416) and the National Institutes of Health (Grant No. R01 GM107703). Alfonso De Simone acknowledges funding from the European Research Council (ERC), Consolidator Grant (CoG) 'BioDisOrder' (819644). Yiming Wang and Carol K. Hall acknowledge the support of a Cheney Visiting Scholar Fellowship from the University of Leeds. The work was also supported by NSF Division of Chemical, Bioengineering, Environmental, and Transport Systems Grants 1743432 and 1512059. Antoine Loquet thanks the ERC starting Grant no. 639020. For Buyong Ma and Ruth Nussinov, this project has been funded in whole or in part with federal funds from the National Cancer Institute, National Institutes of Health, under contract HHSN26120080001E. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the U.S. Government. This Research was supported [in part] by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research. Birgit Strodel acknowledges funding by a Helmholtz ERC Recognition Award. Jie Zheng acknowledges funding from NSF (1806138 and 1825122). Stepan Timr acknowledges funding from the European Union’s Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant agreement No 840395. Fabio Sterpone acknowledges funding from the ERC (FP7/2007-2013) Grant Agreement no. 258748. Nikolay Dokholyan acknowledges support from the National Institutes for Health grants 1R35 GM134864 and UL1 TR002014 and the Passan Foundation. Joan-Emma Shea acknowledges computational support from the Extreme Science and Engineering Discovery Environment (XSEDE) through the National Science Foundation (NSF) grant number TG-MCA05S027. J.-E. Shea acknowledges the support from the National Science Foundation (NSF Grant MCB-1716956). The funding from the National Institutes of Health (NIH grant R01-GM118560-01A) and partial support from the National Science Foundation MRSEC grant No. DMR 1720256 is also acknowledged. She thanks the Center for Scientific Computing at the California Nanosystems Institute (NSF Grant CNS-1725797). The work of Sylvain Lesné was supported by grants from the National Institutes of Health (NIH) to (RF1-AG044342, R21-AG065693, R01-NS092918, R01-AG062135, and R56-NS113549). Additional support included start-up funds from the University of Minnesota Foundation and bridge funds from the Institute of Translational Neuroscience to S.L. Rakez Kayed was supported by National Institute of Health grants R01AG054025 and R01NS094557. Mai Suan Li was supported by Narodowe Centrum Nauki in Poland (grant 2019/35/B/ST4/02086) and the Department of Science and Technology, Ho Chi Minh City, Vietnam (grant 07/2019/HĐ-KHCNTT). Yifat Miller thanks the Israel Science Foundation, grant no. 532/15 and FP7-PEOPLE-2011-CIG, research grant no. 303741. Son Tung Ngo was supported by Vietnam National Foundation for Science & Technology Development (NAFOSTED) grant #104.99-2019.57. Research in the Ramamoorthy lab is supported by NIH (AG048934). Guanghong Wei acknowledges the financial support from the National Science Foundation of China (Grant Nos. 11674065 and 11274075) and National Key Research and Development Program of China (2016YFA0501702). Philippe Derreumaux acknowledges the support of the Université de Paris, ANR SIMI7 GRAL 12-BS07-0017, 'Initiative d’Excellence' program from the French State (Grant 'DYNAMO', ANR- 11-LABX-0011-01) and the CNRS Institute of Chemistry (INC) for two years of délégation in 2017 and 2018., and Nguyen, Phuong

Subjects
Models, Molecular, Amyloid, Parkinson's disease, [SDV]Life Sciences [q-bio], Central nervous system, tau Proteins, Disease, Protein aggregation, 010402 general chemistry, Protein Aggregation, Pathological, 01 natural sciences, Article, Superoxide dismutase, Superoxide Dismutase-1, Alzheimer Disease, Diabetes mellitus, medicine, Animals, Humans, [CHIM]Chemical Sciences, Proteostasis Deficiencies, Amyotrophic lateral sclerosis, Glycoproteins, Amyloid beta-Peptides, biology, 010405 organic chemistry, Chemistry, Amyotrophic Lateral Sclerosis, Neurodegenerative Diseases, Parkinson Disease, General Chemistry, Aluminum compounds, medicine.disease, Islet Amyloid Polypeptide, 3. Good health, 0104 chemical sciences, Enzymes, [SDV] Life Sciences [q-bio], medicine.anatomical_structure, Diabetes Mellitus, Type 2, Oligomers, ddc:540, alpha-Synuclein, biology.protein, Neuroscience
Abstract

International audience; Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. Here we review what computer, in vitro, in vivo and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease (AD), Parkinson's disease (PD), type II diabetes (T2D) and amyotrophic lateral sclerosis (ALS) research, respectively for over many years.

Published
2021

Catalog

Books, media, physical & digital resources
See catalog results