Preparation and characterization of neurotoxic tau oligomers. 2010

Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
The George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, Department of Neurology, University of Texas Medical Branch, Galveston, Texas 77555-1045, United States.

Tau aggregation is a pathological hallmark of Alzheimer's disease, Parkinson's disease, and many other neurodegenerative disorders known as tauopathies. Tau aggregates take on many forms, and their formation is a multistage process with intermediate stages. Recently, tau oligomers have emerged as the pathogenic species in tauopathies and a possible mediator of amyloid-β toxicity in Alzheimer's disease. Here, we use a novel, physiologically relevant method (oligomer cross-seeding) to prepare homogeneous populations of tau oligomers and characterize these oligomers in vitro. We show that both Aβ and α-synuclein oligomers induce tau aggregation and the formation of β-sheet-rich neurotoxic tau oligomers.

UI MeSH Term Description Entries
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D016229 Amyloid beta-Peptides Peptides generated from AMYLOID BETA-PEPTIDES PRECURSOR. An amyloid fibrillar form of these peptides is the major component of amyloid plaques found in individuals with Alzheimer's disease and in aged individuals with trisomy 21 (DOWN SYNDROME). The peptide is found predominantly in the nervous system, but there have been reports of its presence in non-neural tissue. Alzheimer beta-Protein,Amyloid Protein A4,Amyloid beta-Peptide,Amyloid beta-Protein,beta Amyloid,beta-Amyloid Protein,Alzheimer's ABP,Alzheimer's Amyloid Fibril Protein,Amyloid AD-AP,Amyloid Fibril Protein, Alzheimer's,Amyloid beta-Proteins,ABP, Alzheimer's,AD-AP, Amyloid,Alzheimer ABP,Alzheimer beta Protein,Alzheimers ABP,Amyloid AD AP,Amyloid beta Peptide,Amyloid beta Peptides,Amyloid beta Protein,Amyloid beta Proteins,Amyloid, beta,Protein A4, Amyloid,Protein, beta-Amyloid,beta Amyloid Protein,beta-Peptide, Amyloid,beta-Peptides, Amyloid,beta-Protein, Alzheimer,beta-Protein, Amyloid,beta-Proteins, Amyloid
D016875 tau Proteins Microtubule-associated proteins that are mainly expressed in neurons. Tau proteins constitute several isoforms and play an important role in the assembly of tubulin monomers into microtubules and in maintaining the cytoskeleton and axonal transport. Aggregation of specific sets of tau proteins in filamentous inclusions is the common feature of intraneuronal and glial fibrillar lesions (NEUROFIBRILLARY TANGLES; NEUROPIL THREADS) in numerous neurodegenerative disorders (ALZHEIMER DISEASE; TAUOPATHIES). tau Protein,Protein, tau,Proteins, tau
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D045744 Cell Line, Tumor A cell line derived from cultured tumor cells. Tumor Cell Line,Cell Lines, Tumor,Line, Tumor Cell,Lines, Tumor Cell,Tumor Cell Lines
D051844 alpha-Synuclein A synuclein that is a major component of LEWY BODIES and plays a role in SYNUCLEINOPATHIES, neurodegeneration and neuroprotection. Non-AB Component of AD Amyloid Protein,Non AB Component of AD Amyloid Protein,alpha Synuclein
D055503 Protein Multimerization The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS. Protein Dimerization,Protein Heteromultimerizaton,Protein Multimer Assembly,Protein Trimerization,Assembly, Protein Multimer,Dimerization, Protein,Heteromultimerizaton, Protein,Heteromultimerizatons, Protein,Multimer Assembly, Protein,Multimerization, Protein,Trimerization, Protein
D019636 Neurodegenerative Diseases Hereditary and sporadic conditions which are characterized by progressive nervous system dysfunction. These disorders are often associated with atrophy of the affected central or peripheral nervous system structures. Degenerative Diseases, Nervous System,Degenerative Diseases, Central Nervous System,Degenerative Diseases, Neurologic,Degenerative Diseases, Spinal Cord,Degenerative Neurologic Diseases,Degenerative Neurologic Disorders,Nervous System Degenerative Diseases,Neurodegenerative Disorders,Neurologic Degenerative Conditions,Neurologic Degenerative Diseases,Neurologic Diseases, Degenerative,Degenerative Condition, Neurologic,Degenerative Conditions, Neurologic,Degenerative Neurologic Disease,Degenerative Neurologic Disorder,Neurodegenerative Disease,Neurodegenerative Disorder,Neurologic Degenerative Condition,Neurologic Degenerative Disease,Neurologic Disease, Degenerative,Neurologic Disorder, Degenerative,Neurologic Disorders, Degenerative

Related Publications

Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2019, Brain communications,
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2024, Methods in molecular biology (Clifton, N.J.),
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2018, Methods in molecular biology (Clifton, N.J.),
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
February 2019, Analytical biochemistry,
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
October 1989, International journal of biological macromolecules,
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2019, Advances in experimental medicine and biology,
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2013, Journal of Alzheimer's disease : JAD,
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2018, Methods in molecular biology (Clifton, N.J.),
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
January 2021, Life (Basel, Switzerland),
Cristian A Lasagna-Reeves, and Diana L Castillo-Carranza, and Marcos J Guerrero-Muoz, and George R Jackson, and Rakez Kayed
July 2011, The Journal of biological chemistry,
Copied contents to your clipboard!