Plasma Tau Variants Detected by a Novel Anti-Tau Monoclonal Antibody: A Potential Biomarker for Alzheimer’s Disease

2020 ◽  
Vol 77 (2) ◽  
pp. 877-883
Author(s):  
Andrea González ◽  
Leonardo Guzmán-Martínez ◽  
Ricardo B. Maccioni
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Western Blot ◽  
Low Molecular Weight ◽  
The Novel ◽  
Major Drawback ◽  
Blood Biomarker ◽  
Potential Biomarker

Background: A major drawback in Alzheimer’s disease (AD) is the lack of validated biomarkers for routine clinical diagnostic. We have reported earlier a novel blood biomarker, named Alz-tau®, based on variants of platelet tau. This marker evaluates the ratio of high molecular weight tau (HMWtau) and the low molecular weight (LMWtau) tau. Objective: To analyze a potential novel source of antigen for Alz-tau®, plasma tau, detected by immunoreactivity with the novel monoclonal antibody, tau51. Methods: We evaluated tau variants in plasma precipitated with ammonium sulfate from 36 AD patients and 15 control subjects by western blot with this novel monoclonal antibody. Results: The HMW/LMWtau ratio was statistically different between AD patients and controls. Conclusions: Plasma tau variants are suitable to be considered as a novel antigen source for the Alz-tau® biomarker for AD.

Isolation of Low-Molecular-Weight Proteins from Amyloid Plaque Fibers in Alzheimer's Disease

2006 ◽  
Vol 46 (6) ◽  
pp. 1820-1834 ◽  
Author(s):  
Dennis J. Selkoe ◽  
Carmela R. Abraham ◽  
Marcia B. Podlisny ◽  
Lawrence K. Duffy
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Amyloid Plaque ◽  
Low Molecular Weight ◽  
Low Molecular Weight Proteins

P3-282: Investigation of low molecular weight D-enantiomeric peptides for diagnosis and therapy of Alzheimer's disease

2009 ◽  
Vol 5 (4S_Part_14) ◽  
pp. P426-P426
Author(s):  
Dirk Bartnik ◽  
Susanne A. Funke ◽  
Yeliz Cinar ◽  
Oleksandr Brener ◽  
Luitgard Nagel-Steger ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Low Molecular Weight ◽  
Diagnosis And Therapy

Alterations of low molecular weight acid phosphatase protein level in Alzheimer's disease

1995 ◽  
Vol 699 (1) ◽  
pp. 125-129 ◽  
Author(s):  
Shun Shimohama ◽  
Sadaki Fujimoto ◽  
Motohiko Chachin ◽  
Takashi Taniguchi ◽  
George Perry ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Acid Phosphatase ◽  
Protein Level ◽  
Low Molecular Weight

Organotin compounds in trimethyltin-treated rats and in human brain in Alzheimer's Disease

1997 ◽  
Vol 16 (9) ◽  
pp. 512-515 ◽  
Author(s):  
F. Martin ◽  
FM Corrigan ◽  
Ofx Donard ◽  
J. Kelly ◽  
Jao Besson ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Human Brain ◽  
Brain Tissue ◽  
Hydride Generation ◽  
Organotin Compounds ◽  
Low Molecular Weight ◽  
Human Brain Tissue ◽  
Cryogenic Trapping

As blood tin concentrations are elevated in Alzheimer's disease and as some low molecular weight organotin compounds are neurotoxic, we have attempted to detect organotins in brain in Alzheimer's Disease. First we measured the concentration of trimethyltin (TMT) in the brains of rats which had been exposed to memory- impairing concentrations of TMT and, as the method of linking hydride generation, cryogenic trapping, gas chromatographic separation and atomic absorption spec trophotometric detection permitted the measurements of organotin compounds when the total tin was greater than 0.2 nanograms, we applied these techniques to human brain tissue, some of which showed neuropathological evidence of Alzheimer's Disease. No low molecular weight organotin compounds were detected in the human brain tissue, but it is possible that tin may be complexed with large organic molecules, the hydrides of which would not be volatile, but which could be identified by liquid chromatography.

scholarly journals Contributions of Mass Spectrometry to the Identification of Low Molecular Weight Molecules Able to Reduce the Toxicity of Amyloid-β Peptide to Cell Cultures and Transgenic Mouse Models of Alzheimer’s Disease

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1167 ◽  
Author(s):  
Raluca Ştefănescu ◽  
Gabriela Dumitriṭa Stanciu ◽  
Andrei Luca ◽  
Ioana Cezara Caba ◽  
Bogdan Ionel Tamba ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Mouse Models ◽  
Cell Cultures ◽  
Noncovalent Complex ◽  
Low Molecular Weight ◽  
Transgenic Mouse Models ◽  
Amyloid Peptides

Alzheimer’s Disease affects approximately 33 million people worldwide and is characterized by progressive loss of memory at the cognitive level. The formation of toxic amyloid oligomers, extracellular amyloid plaques and amyloid angiopathy in brain by amyloid beta peptides are considered a part of the identified mechanism involved in disease pathogenesis. The optimal treatment approach leads toward finding a chemical compound able to form a noncovalent complex with the amyloid peptide thus blocking the process of amyloid aggregation. This direction gained an increasing interest lately, many studies demonstrating that mass spectrometry is a valuable method useful for the identification and characterization of such molecules able to interact with amyloid peptides. In the present review we aim to identify in the scientific literature low molecular weight chemical compounds for which there is mass spectrometric evidence of noncovalent complex formation with amyloid peptides and also there are toxicity reduction results which verify the effects of these compounds on amyloid beta toxicity towards cell cultures and transgenic mouse models developing Alzheimer’s Disease.

Sign in / Sign up

Export Citation Format

Share Document