proteinchip systems  (Bio-Rad)

Journal: BMC Pharmacology

Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

doi: 10.1186/1471-2210-4-18

Figure Lengend Snippet: Analysis of proteomic profiles in mouse serum using SELDI-TOF-MS. Serum samples from fasting wild-type (+m/+m) mice were loaded onto the spots of CM10 (a cationic exchanger, pH4) ProteinChip arrays. The spots were analyzed using the SELDI ProteinChip system on three different ranges: m/z 3000 – 10000, m/z 10000 – 20000 and m/z 20000 – 100000. The y-axis of the spectra indicates the mass-to-charge ratio (m/z) of protonated proteins, and the x-axis indicates the relative intensities of mass spectral signals. Note: The intensity of each peak is directly proportional to the amount of protein, but the peak intensities could not be comparable among the different proteins because of the difference in ionization.

Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

Techniques:

Journal: BMC Pharmacology

Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

doi: 10.1186/1471-2210-4-18

Figure Lengend Snippet: Proteomic analyses demonstrating the differences in protein profiles of sera from diabetic and wild-type mice. Serum samples from fasting diabetic (db+/db+) mice and fasting wild-type (+m/+m) mice were loaded onto ProteinChip arrays. (A) List of peaks of proteins and/or peptides with indicated m/z values, the peak intensities of which were significantly changed in the diabetic state. Relative peak intensities were averaged (n = 8). The fold changes are presented as ratios of the peak intensities at indicated m/z values in db+/db+ to those in the +m/+m mice. Peaks at m/z 4203, 4576, 8515, 9291, 17406 and 18678 were obtained using CM10 ProteinChip (pH4). Peaks at 8733 and 9311 m/z were obtained using CM10 ProteinChip (pH7). Peaks at m/z 3933, 4119, 4206, 4369, 4566, 4579, 4637, 8523, 8827, 8915, 9283, 13075, 17407, 17418, 17622, 18431, 18691, 22334 and 26100 were obtained using Q10 ProteinChip. Peak at m/z 4211 was obtained using IMAC30. The chips were analyzed by SELDI-TOF-MS. (B) and (C) Typical data of relative peak intensities in +m/+m and db+/db+ mouse sera (upper, representative of 4–8 independent observations) and the peak intensity averages at m/z 4206 and 26100 (lower, n = 4 for +m/+m, n = 8 for db+/db+). The analyzed peak is indicated by arrows in the data of mass spectral signals. **P < 0.01; significantly different from the peak in wild-type mice, by unpaired t -test.

Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

Techniques:

Journal: BMC Pharmacology

Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

doi: 10.1186/1471-2210-4-18

Figure Lengend Snippet: Changes in serum protein profiles in db+/db+ mice by administration of green tea. Serum samples from fasting diabetic (db+/db+) mice 2 h after administration of green tea suspension were loaded onto ProteinChip Arrays. The chips were analyzed using SELDI-TOF-MS. (A) List of peaks of proteins and/or peptides with indicated m/z values, the peak intensities of which were significantly changed by the green tea administration. Relative peak intensities were averaged (n = 4). The fold changes are presented as ratios of the peak intensities at indicated m/z values 2 h after to before green tea administration. Peaks at m/z 7495, 7595, 7808, 7920, 14983, 15612 and 15614 were obtained using CM10 ProteinChip (pH4), whereas those at m/z 7503, 7611, 7823, 7926, 11651, 11664, 11863, 15004 and 15638 were obtained using CM10 ProteinChip (pH7). Peaks at m/z 4212, 4226, 7499, 11637, 11846, 13711, 13831, 14974, 15180, 31204 and 65906 were obtained using IMAC30 ProteinChip. (B) Typical data of relative peak intensities (upper, representative of 4 independent observations) and the peak intensity average at m/z 11863 (lower, n = 4) after green tea administration and saline control. The analyzed peak is indicated by arrows in the data of mass spectral signals. **P < 0.01; significantly different from the peak obtained before the administration, by unpaired t -test.

Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

Techniques:

Journal: BMC Pharmacology

Article Title: Effect of green tea on blood glucose levels and serum proteomic patterns in diabetic (db/db) mice and on glucose metabolism in healthy humans

doi: 10.1186/1471-2210-4-18

Figure Lengend Snippet: Hemoglobin-related multiple SELDI-TOF-MS signals in db+/db+ mice. Samples of sera from nontreated db+/db+ mice in the fasting state were loaded onto ProteinChip arrays. Left panel: hemoglobin-related multi-MS signals. From the average of 8 data, the signals were detected from m/z 14974 to 15638 (+H) using CM10 ProteinChip (pH7). The double-charged m/z values appear to be observed from m/z 7495 to 7823 (+2H). These values may correspond to hemoglobin α- and β-chains, and other hemoglobin-related proteins. Right panel: multi-MS signals observed at approximately double the single-charged m/z values for the hemoglobin-related signals, using IMAC ProteinChip. These signals may correspond to the dimers of hemoglobin α- and β-chains.

Article Snippet: The spots were analyzed using the SELDI ProteinChip system (PBS-IIc, Ciphergen Biosystems).

Techniques:

Journal: Proteome Science

Article Title: Transchromosomic cell model of Down syndrome shows aberrant migration, adhesion and proteome response to extracellular matrix

doi: 10.1186/1477-5956-7-31

Figure Lengend Snippet: Representative SELDI-TOF MS spectra from A9 samples . (A) A9 and WA17 cells were lysed and proteins resolved by SDS-PAGE. Equal amounts of total protein lysate were used for electrophoresis (20 μg). (B) An example of SELDI protein-profiling spectra of 2 μg of whole cell protein extract of A9 cell line on four different chromatographic arrays (H50, IMAC, Q10 and CM10) is shown. (C) A dilution series of A9 cell protein extract sample was prepared and 2 μl of each was analyzed on a Q10 and CM10 ProteinChip array. The total amount of protein analyzed was 2, 1, 0.5 and 0.1 μg, respectively.

Article Snippet: We then analysed protein extracts from each cell line (A9 and WA17) on the ProteinChip system (Ciphergen Biosystems, Fremont, CA), which is based on the integration of chemically modified array surfaces with surface-enhanced laser desorption/ionization (SELDI) time-of-flight (TOF) mass-spectrometry (MS) detection [ ].

Techniques: SDS Page, Electrophoresis

Journal: BMC Neurology

Article Title: Identification of novel biomarker candidates by proteomic analysis of cerebrospinal fluid from patients with moyamoya disease using SELDI-TOF-MS

doi: 10.1186/1471-2377-10-112

Figure Lengend Snippet: CART analysis using peaks obtained by SELDI-TOF-MS to discriminate between patients with MMD and control patients. The decision tree was constructed using CSF samples from 32 patients with MMD and control patients. The classification is determined starting at the roof node, following by appropriate splitting decisions based on the peak intensity at each node. If the peak intensity is lower than the cutoff intensity value, the left node is selected. This splitting process is continued until no further classification is achieved and terminal nodes are produced. Using m/z 4473, 2406 and 6338 peaks (pH 5), m/z 4588 and 7250 peaks (pH 7), and m/z 4746 and 1044 peaks (pH 9), CART for Q10 ProteinChip was applied to identify patients with MMD and control patients. The analysis correctly classified all 20 patients with MMD under pH 5 condition and 19 of 20 under the pH 7 and 9 conditions; all 12 control patients were classified under all pH conditions.

Article Snippet: The protein mass spectral data was generated with ProteinChip System 4000 SELDI-TOF mass spectrometer (Enterprise version; Bio-Rad Laboratories) using automated data collection protocol with Ciphergen Express version 3.0.6 software interface (Bio-Rad Laboratories).

Techniques: Construct, Produced