イネ ニオケル コメヌカ タンパクシツ ノ プロテオミクス

Rice bran has wide potential usage as a source of valuable nutrients, though little is known about its protein composition. Here, we identified rice bran proteins by using proteomic analysis. After extraction of crude protein from the bran of Koshihikari brown rice grains, we separated proteins by 2-D PAGE and analyzed 41 protein spots. N-terminal amino acid sequences were determined for 23 spots, 21 proteins of known function and 2 could not be identified by BLAST searching. For the other 18 spots, the N-terminal amino acids could not be determined. Of these, 4 were identified by using LC-MS/MS. After in-solution digestion of bran samples from Koshihikari and TN-1, we looked for differences in the bran proteins between these cultivars. A total of 83 proteins were detected and classified into 10 categories: storage proteins, carbohydrate metabolic enzymes, proteins related to synthesis and proteolysis, embryo proteins, stress-related proteins, regulatory proteins, antioxidant proteins, redox-related proteins, lipid biosynthesis proteins, and energy-related proteins. In the identified proteins, antioxidant proteins and redox-related proteins, such as peroxiredoxin and glyoxalase, respectively, considered to be unique to bran among seed proteins. Such proteins may play important roles as antioxidants for protecting cells in the embryo and aleurone layer from the stress of desiccation

Nationwide surveillance of bacterial respiratory pathogens conducted by the surveillance committee of Japanese Society of Chemotherapy, the Japanese Association for Infectious Diseases, and the Japanese Society for Clinical Microbiology in 2010: General view of the pathogens\u27 antibacterial susceptibility

The nationwide surveillance on antimicrobial susceptibility of bacterial respiratory pathogens from patients in Japan, was conducted by Japanese Society of Chemotherapy, Japanese Association for Infectious Diseases and Japanese Society for Clinical Microbiology in 2010.The isolates were collected from clinical specimens obtained from well-diagnosed adult patients with respiratory tract infections during the period from January and April 2010 by three societies. Antimicrobial susceptibility testing was conducted at the central reference laboratory according to the method recommended by Clinical and Laboratory Standard Institutes using maximum 45 antibacterial agents.Susceptibility testing was evaluable with 954 strains (206 Staphylococcus aureus, 189 Streptococcus pneumoniae, 4 Streptococcus pyogenes, 182 Haemophilus influenzae, 74 Moraxella catarrhalis, 139 Klebsiella pneumoniae and 160 Pseudomonas aeruginosa). Ratio of methicillin-resistant S.aureus was as high as 50.5%, and those of penicillin-intermediate and -resistant S.pneumoniae were 1.1% and 0.0%, respectively. Among H.influenzae, 17.6% of them were found to be β-lactamase-non-producing ampicillin (ABPC)-intermediately resistant, 33.5% to be β-lactamase-non-producing ABPC-resistant and 11.0% to be β-lactamase-producing ABPC-resistant strains. Extended spectrum β-lactamase-producing K.pneumoniae and multi-drug resistant P.aeruginosa with metallo β-lactamase were 2.9% and 0.6%, respectively.Continuous national surveillance of antimicrobial susceptibility of respiratory pathogens is crucial in order to monitor changing patterns of susceptibility and to be able to update treatment recommendations on a regular basis

Activation of AMP-activated protein kinase (AMPK) through inhibiting interaction with prohibitins

Summary: 5′-Adenosine monophosphate-activated protein kinase (AMPK) is a potential therapeutic target for various medical conditions. We here identify a small-molecule compound (RX-375) that activates AMPK and inhibits fatty acid synthesis in cultured human hepatocytes. RX-375 does not bind to AMPK but interacts with prohibitins (PHB1 and PHB2), which were found to form a complex with AMPK. RX-375 induced dissociation of this complex, and PHBs knockdown resulted in AMPK activation, in the cultured cells. Administration of RX-375 to obese mice activated AMPK and ameliorated steatosis in the liver. High-throughput screening based on disruption of the AMPK-PHB interaction identified a second small-molecule compound that activates AMPK, confirming the importance of this interaction in the regulation of AMPK. Our results thus indicate that PHBs are previously unrecognized negative regulators of AMPK, and that compounds that prevent the AMPK-PHB interaction constitute a class of AMPK activator