Myanmar migrant laborers in Ranong, Thailand

Thailand is the major destination for migrants in mainland Southeast Asia, and Myanmar (Burmese) migrants account for the dominant share. This paper sheds light on the actual working conditions and the life of Myanmar migrants in Thailand, based on our intensive survey in Ranong in southern Thailand in 2009. We found a wide range of serious problems that Myanmar migrants face in everyday life: very harsh working conditions, low income, heavy indebtedness, risk of being human-trafficking victims, harassment by the police and military (especially of sex workers), high risk of illness including malaria and HIV/AIDS and limited access to affordable medical facilities, and a poor educational environment for their children.Myanmar, Thailand, Migrant labor, Migration, Household

Myanmar migrant laborers in Ranong, Thailand

Thailand is the major destination for migrants in mainland Southeast Asia, and Myanmar (Burmese) migrants account for the dominant share. This paper sheds light on the actual working conditions and the life of Myanmar migrants in Thailand, based on our intensive survey in Ranong in southern Thailand in 2009. We found a wide range of serious problems that Myanmar migrants face in everyday life: very harsh working conditions, low income, heavy indebtedness, risk of being human-trafficking victims, harassment by the police and military (especially of sex workers), high risk of illness including malaria and HIV/AIDS and limited access to affordable medical facilities, and a poor educational environment for their children

Putrescine-dependent Tumor Invasion

Our previous study showed that treatment of highly invasive rat ascites hepatoma (LC-AH) cells with α-difluoromethylornithine (DFMO), an inhibitor of ornithine decarboxylase, decreased both their intracellular level of putrescine and their in vitro invasion of a monolayer of calf pulmonary arterial endothelial (CPAE) cells, and that both these decreases were completely reversed by exogenous putrescine, but not spermidine or spermine. Here we show that all adhering control (DFMO-untreated) cells migrated beneath CPAE monolayer with morphological change from round to cauliflower-shaped cells (migratory cells). DFMO treatment increased the number of cells that remained round without migration (nonmigratory cells). Exogenous putrescine, but not spermidine or spermine, induced transformation of all nonmigratory cells to migratory cells with a concomitant increase in their intracellular Ca2+ level, [Ca2+]i. The putrescine-induced increase in their [Ca2+]i preceded their transformation and these effects of putrescine were not affected by antagonists of the voltage-gated Ca2+ channel, but were completely suppressed by ryanodine, which also suppressed the invasiveness of the control cells. The DFMO-induced decreases in both [Ca2+]i and the invasiveness of the cells were restored by thapsigargin, which elevated [Ca2+]i by inhibiting endoplasmic Ca2+-ATPase, indicating that thapsigargin mimics the effects of putrescine. These results support the idea that putrescine is a cofactor for Ca2+ release through the Ca2+ channel in the endoplasmic reticulum that is inhibited by ryanodine, this release being initiated by cell adhesion and being a prerequisite for tumor cell invasion

近赤外イメージングを応用した神経機能マッピング新技術の開発

科学研究費助成事業 研究成果報告書：挑戦的萌芽研究2016-2017課題番号 : 16K1458

マウス高度非侵襲イメージングシステムの開発と応用

科学研究費助成事業 研究成果報告書：基盤研究(B)2015-2017課題番号 : 15H0428

Establishment of fluorescent in vivo Western method

科学研究費助成事業(科学研究費補助金)研究成果報告書：挑戦的萌芽研究2010-2011課題番号：2265009

<Abstract of Published Report>Identification of Amino Acid Residues Responsible for Difference in Substrate Specificity and Inhibitor Sensitivity Between Two Human Liver Dihydrodiol Dehydrogenase Isoenzymes by Site-directed Mutagenesis.

Human liver dihydrodiol dehydrogenase isoenzymes (DD1 and DD2), in which only seven amino acid residues are substituted, differ remarkably in specificity for steroidal substrates and inhibitor sensitivity: DD1 shows 20alpha-hydroxysteroid dehydrogenase activity and sensitivity to 1,10-phenanthroline, whereas DD2 oxidizes 3alpha-hydroxysteroids and is highly inhibited by bile acids. In the present study we performed site-directed mutagenesis of the seven residues (Thr-38, Arg-47, Leu-54, Cys-87, Val-151, Arg-170 and Gln-172) of DD1 to the corresponding residues (Val, His, Val, Ser, Met, His and Leu respectively) of DD2. Of the seven mutations, only the replacement of Leu-54 with Val produced an enzyme that had almost the same properties as DD2. No significant changes were observed in the other mutant enzymes. An additional site-directed mutagenesis of Tyr-55 of DD1 to Phe yielded an inactive protein, suggesting the catalytically important role of this residue. Thus a residue at a position before the catalytic Tyr residue might play a key role in determining the orientation of the substrates and inhibitors