Anomalously phosphorylated tau and Abeta fragments in the CSF correlates with cognitive impairment in MCI subjects.

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the presence of extracellular amyloid deposits, consisting largely of Abeta peptide and the presence of intraneuronal aggregates of neurofibillary tangles formed by tau. Development of cerebrospinal fluid (CSF) biomarkers has become a rapidly growing research field, considering the need for diagnostic tools for AD, thus allowing therapeutic compounds to have the greatest potential for being effective. We have focused on the relationships between critical biomarkers such as tau and Abeta in the CSF and the cognitive impairment of patients, as assessed by a battery of neuropsychological tests derived from CDR and CERAD, of value in the evaluation of AD patients.

ApoE alleles and tau markers in patients with different levels of cognitive impairment.

Background: The presence of brain hyperphosphorylated tau constitutes a hallmark of neurodegenerative disorders of the Alzheimer's type. This report describes the relationships between tau markers in the cerebrospinal fluid (CSF), the degree of cognitive impairment and the predictive value of genetic markers such the alleles of apolipoprotein E, namely, the presence of Apo-epsilon4, as part of a longitudinal study.

Methods: Three major groups of patients with ages ranging from 65-73 years were evaluated in this study (n=72): Alzheimer's disease patients (AD), a group with mild cognitive impairment (MCI) and normal senile patients (NS).

Determination of cobalt in urine by FI-ICP-AES with online preconcentration.

A method for the preconcentration and determination of cobalt in human urine samples was developed. The online preconcentration and determination were attained using inductively coupled plasma atomic emission spectromety (ICP-AES) coupled to a flow injection (FI) method. Cobalt was retained on an Amberlite XAD-7 resin as cobalt-2-(5-bromo-2-pyridylazo)-5-diethylaminophenol complex at pH 9.

Tubulin, actin, and tau protein interactions and the study of their macromolecular assemblies.

The intracellular polymerization of cytoskeletal proteins into their supramolecular assemblies raises many questions regarding the regulatory patterns that control this process. Binding experiments using the ELISA solid phase system, together with protein assembly assays and electron microscopical studies provided clues on the protein-protein associations in the polymerization of tubulin and actin networks. In vitro reconstitution experiments of these cytoskeletal filaments using purified tau, tubulin, and actin proteins were carried out.