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Nishi-Tokyo-shi, Japan

Okamoto H.,Sensory Medical | Okamoto H.,Ochanomizu University | Umeda S.,Ochanomizu University | Nozawa T.,AMR Inc. | And 4 more authors.
Experimental Animals | Year: 2010

The central region of the primate retina is called the macula. The fovea is located at the center of the macula, where the photoreceptors are concentrated to create a neural network adapted for high visual acuity. Damage to the fovea, e.g., by macular dystrophies and age-related macular degeneration, can reduce central visual acuity. The molecular mechanisms leading to these diseases are most likely dependent on the proteins in the macula which differ from those in the peripheral retina in expression level. To investigate whether the distribution of proteins in the macula is different from the peripheral retina, proteomic analyses of tissues from these two regions of cynomolgus monkeys were compared. Two-dimensional gel electrophoresis and mass spectrometry identified 26 proteins that were present only in the macular gel spots. The expression levels of five proteins, cone photoreceptor specific arrestin-C, γ-synuclein, epidermal fatty acid binding protein, tropomyosin 1α chain, and heterogeneous nuclear ribonucleoproteins A2/B1, were significantly higher in the macula than in the peripheral retina. Immunostaining of macula sections by antibodies to each identified protein revealed unique localization in the retina, retinal pigment epithelial cells and the choroidal layer. Some of these proteins were located in cells with higher densities in the macula. We suggest that it will be important to study these proteins to determine their contribution to the pathogenesis and progression of macula diseases. Source


Sagawa T.,Kraft Foods Inc. | Kudou Y.,Bio Chromato Incorporated | Nishiguchi T.,Bio Chromato Incorporated | Kawamukai T.,AMR Inc. | And 5 more authors.
Nippon Shokuhin Kagaku Kogaku Kaishi | Year: 2015

Recently, studies on odor-active compounds and flavor release phenomena from foods have been carried out. During flavor release, rheological and thermodynamic phenomena occur within seconds. However, continuous analysis of volatile compounds from foods during flavor release is challenging because of the lack of facile procedures and adequate instrumentation for such measurements. Therefore, a system was developed using direct analysis in real time mass spectrometry to facilitate the continuous analysis of volatile compounds during flavor release. We also prepared model foods such as chocolate from sugar and oil and added two volatile compounds (l-carvone and dlimonene). Using the developedsystem, we successfully and continuously analyzedthe release of volatile compounds from the model foods within seconds. Copyright © 2015, Japanese Society for Food Science and Technology. Source


Niimori-Kita K.,Kumamoto University | Ogino K.,Kumamoto University | Mikami S.,AMR Inc. | Kudoh S.,Kumamoto University | And 9 more authors.
FEBS Open Bio | Year: 2014

Smoking is a risk factor for lung diseases, including chronic obstructive pulmonary disease and lung cancer. However, the molecular mechanisms mediating the progression of these diseases remain unclear. Therefore, we sought to identify signaling pathways activated by tobacco-smoke exposure, by analyzing nuclear phosphoprotein expression using phosphoproteomic analysis of lung tissue from mice exposed to tobacco smoke. Sixteen mice were exposed to tobacco smoke for 1 or 7. days, and the expression of phosphorylated peptides was analyzed by mass spectrometry. A total of 253 phosphoproteins were identified, including FACT complex subunit SPT16 in the 1-day exposure group, keratin type 1 cytoskeletal 18 (K18), and adipocyte fatty acid-binding protein, in the 7-day exposure group, and peroxiredoxin-1 (OSF3) and spectrin β chain brain 1 (SPTBN1), in both groups. Semi-quantitative analysis of the identified phosphoproteins revealed that 33 proteins were significantly differentially expressed between the control and exposed groups. The identified phosphoproteins were classified according to their biological functions. We found that the identified proteins were related to inflammation, regeneration, repair, proliferation, differentiation, morphogenesis, and response to stress and nicotine. In conclusion, we identified proteins, including OSF3 and SPTBN1, as candidate tobacco smoke-exposure markers; our results provide insights into the mechanisms of tobacco smoke-induced diseases. © 2014 The Authors. Source


Sekimoto K.,Yokohama City University | Sakakura M.,AMR Inc. | Kawamukai T.,AMR Inc. | Hike H.,AMR Inc. | And 4 more authors.
Analyst | Year: 2014

The positive and negative ionization characteristics of 20 different α-amino acids were investigated using Direct Analysis in Real Time (DART) mass spectrometry. Almost all of the amino acids M were ionized to generate the (de)protonated analytes [M ± H]±via proton transfer reactions with the typical background ions H3O+(H 2O)n and O2 ̇- and resonant electron capture by M. The application of DART to amino acids also resulted in molecular ion formation, fragmentation, oxidations involving oxygen attachment and hydrogen loss, and formation of adducts [M + R]- with negative background ions R- (O2 ̇-, HCO 2 -, NO2 - and COO-(COOH)), depending on the physicochemical and/or structural properties of individual amino acids. The relationship between each amino acid and the ionization reactions observed suggested that fragmentation can be attributed to pyrolysis during analyte desorption as well as excess energy obtained via (de)protonation. Oxidation and [M + R]- adduct formation, in contrast, most likely originate from reactions with active oxygen such as hydroxyl radicals HO ̇, indicating that the typical background neutral species involved in analyte ionization in DART mass spectrometry contain HO ̇. © the Partner Organisations 2014. Source

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