Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: the deterioration of antioxidant system.

Oxidative stress plays a pivotal role in normal brain aging and various neurodegenerative diseases, including Alzheimer's disease (AD). Irreversible protein carbonylation, a widely used marker for oxidative stress, rises during aging. The temporal cortex is essential for learning and memory and particularly susceptible to oxidative stress during aging and in AD patients.

Proteomic analysis of a membrane skeleton fraction from human liver.

The cytoskeleton networks around liver cell cortex can resist Triton extraction and co-pellet with their tightly associated integral membrane proteins, forming assemblies called "membrane skeletons". Despite their important roles in determining cell shape and in signal transduction pathways, the membrane skeletons of human liver cells are uncharacterized to a great extent. In the present work, we prepared a membrane skeleton fraction by Triton extraction of human liver plasma membranes and then separated its protein components by 2-D gels.

Comparison of two-dimensional gel electrophoresis based and shotgun strategies in the study of plasma membrane proteome.

Membrane proteins play important roles in various plasma membrane (PM) activities such as signal transduction and cell recognition. However, a comprehensive proteomic study of membrane proteins remains difficult. Different strategies have been employed to study PM proteome, but little effort has been made to systematically evaluate them.

Proteomic analysis and comparison of the biopsy and autopsy specimen of human brain temporal lobe.

The proteomic study on human temporal lobe can help us to understand the physiological function of CNS in normal as well as in pathological state. Proteomic tools are potent for the assessment of protein stability post mortem. In this pilot study, the human temporal lobe biopsy specimen with chronic pharmacoresistant temporal lobe epilepsy (TLE) and autopsy specimen in control were separated by 2-DE.

[Identification of biomarkers in serum of early rheumatoid arthritis by proteomic methods].

Objective: To discover the biomarkers of early rheumatoid arthritis (RA) patients and healthy person were analyzed by proteomic methods to discover serum biomarkers.

Methods: Samples of peripheral blood were collected form 10 newly diagnosed active RA patients, 5 males and 5 females, aged 54.3 +/- 12.

[A preliminary proteomic analysis of tauopathies].

Objective: To investigate the molecular mechanisms of tauopathies. Comparative proteomic analysis of brain proteins was employed to study 4 patients with tauopathies as compared with 4 controls.

Methods: The brains of subjects who died without clinical or pathological involvement of nervous system and brains of patients with tauopathies were obtained at autopsy.

[Proteomic comparison between human cerebellums and frontal lobes].

Objective: To compare the results of proteomics between the cerebellum and frontal lobe of the aged.

Method: Proteins were isolated from human cerebellums and frontal lobes and separated by two-dimensional (2D) gel electrophoresis. The proteins were then stained with silver or colloidal coomassie blue to produce a high-resolution map of the proteome.

Proteomic comparison between human young and old brains by two-dimensional gel electrophoresis and identification of proteins.

To investigate molecular mechanisms of human brain aging, brain proteins were isolated from postmortem human young and old brains and profiled by two-dimensional gel electrophoresis (2-DE). With the help of special software, five down-regulated protein spots in two-dimensional gel electrophoresis gels of old brains were found compared with young brains, four of which was identified as a protein similar to peroxiredoxin 2 (accession-numbered as gi | 13631440), two of stathmin (phosphoprotein p19) and apolipoprotein A-I precursor (apo-AI) by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). Eight common proteins, whose expressions were not altered between young and old brains, were also identified.