Introducing Professor Masataka Mori, Asia-Australian Regional Editor

Dear Colleagues

It is a pleasure to welcome Masataka Mori as our new Asia-Australian Regional Editor. Dr Mori succeeds Professor Takashi Yura, our founding Asia-Australian Regional Editor. Dr Yura will remain on the Editorial Board and continue to be active scientifically. Asia is a very important region to the future of Cell Stress & Chaperones. Currently 16% of our subscribers are in Asia, the third largest group behind the United States and Europe. Japan in particular has a very active presence in our field and interest is growing in Australia, China, India, and South Korea as well.

Masataka Mori is Professor and Chairman, Department of Molecular Genetics, Graduate School of Medical Sciences, Kumamoto University, Japan. He was born in Kyoto in 1940 and received his MD in 1965 and his PhD in Biochemistry in 1970 from Kyoto University. His PhD work was on heme biosynthesis in bacteria and mammals. He moved to Chiba University as a Lecturer and worked on pyrimidine biosynthesis in mammals with Dr Masamiti Tatibana. Dr Mori found the carbamylphosphate synthetase II complex consisting of the first 3 enzymes of the pathway, purified it, and showed that these 3 enzyme activities are located on a single polypeptide. In 1977–1978, Dr Mori worked as a Research Associate at the University of Wisconsin–Madison with Dr Philip Cohen on the urea cycle in frogs. He then returned to Chiba University as an Associate Professor and initiated his work on mitochondrial biogenesis and the urea cycle in mammals. He discovered larger precursors for mitochondrial proteins in mammals, developed an in vitro import system, and paved the way for molecular analysis of mitochondrial protein import. Dr Mori moved to Kumamoto University in 1985, where he was appointed Professor of Molecular Genetics. He has been working on molecular chaperones and the Tom complex in mitochondrial biogenesis in mammals. He found that DjA1 and DjA2, in combination with heat shock cognate (Hsc) 70, facilitate mitochondrial protein import. He also found that DjA1 and DjA2, rather than DjB1/Hsp40, work as partner chaperones with Hsc70 in refolding of denatured proteins. In addition, he cloned the genes for the urea cycle enzymes and revealed the mechanism of their liver-selective and coordinated expression. He extended his work on the urea cycle to nitric oxide (NO) synthesis and demonstrated a novel regulatory mechanism of NO production by the citrulline-NO cycle and arginase isoforms in various cell types. Recently, Dr Mori found a novel pathway of NO-induced apoptosis mediated by endoplasmic reticulum (ER) stress involving CHOP induction, and that ER stress–mediated apoptosis of β cells is involved in type 1 diabetes. He also found that diabetes of Akita mice with an insulin gene mutation and neuronal cell death by brain ischemia are caused by ER stress–mediated apoptosis, and they are markedly improved by disruption of the Chop gene. Dr Mori is now working on regulation of ER stress–mediated apoptosis by molecular chaperones. He has over 200 publications in international journals.

Two of the papers in the next issue are from the Asia-Australia region, including 1 from Dr Mori's group in collaboration with another lab at Kumamoto University (Lee et al 2004). Their report suggests that cytosolic Hsp70 and DnaJ family proteins or Hsp90 (or both) are induced in CCl₄-treated rat liver where they may be cytoprotective. A second paper represents a collaboration among investigators at Tongji Medical College and Yanan Hospital in China and at Laval University in Canada (Jin et al 2004). They showed that serum Hsp70 levels increased with age between 15 and 30 years but decreased in individuals between the age of 30 and 50. There was also an age-dependent decrease in lymphocyte Hsp70 levels in individuals older than 40 years. The authors concluded that age is a significant factor to consider when using serum and lymphocyte Hsp70 as biomarkers for disease states and exposure to environmental stresses.

If we look back over the past 2 years for contributions in Cell Stress & Chaperones from colleagues in this region, we find that Anil Grover (India) contributed a review of The Third International Workshop on the Molecular Biology of Stress Responses, organized by Daniel Ciocca in Mendoza (Grover 2002). Lakhotia et al (2002), also working in India, discovered a complex regulatory network for Hsp70 and Hsp64 in Drosophila larvae, involving transcriptional, translational, and posttranslational controls. Goo et al (2002) (South Korea) characterized a protein disulfide isomerase from the silkworm Bombyx mori, finding it concentrated in insect fat body and under hormonal control.

Another paper from the Mori lab in Japan described a new DnaJ/Hsp40 homolog, dj4, which increases in rat heart muscle cells during differentiation (Abdul et al 2002). When Hsp70 was overexpressed in these cells, their resistance to heat-induced cell killing increased, and coexpression of either dj4 or dj2 along with Hsp70 was even better. Also from Japan, Wadhwa et al (2002) described the differential subcellular localization of the mainly mitochondrial form of Hsp70 called mortalin in normal and immortal human and mouse cells. Aosai et al (2002) made the intriguing observation that Hsp70 from Toxoplasma gondii is a B cell mitogen, and they implicated the Toll-like receptor MyD88 protein in lipopolysaccharide-induced but not T gondii Hsp70–induced proliferative responses.

Additional contributions from the collaboration of Tangchun Wu (China) and Robert Tanguay (Canada) include a study of basal and inducible Hsp70 in military recruits during basic training. Individuals experiencing acute heat illness early in the training cycle had significantly higher basal levels of Hsp70 than the control group. Interestingly, the basal level of Hsp70 in lymphocytes from both groups was higher and essentially the same late in the training cycle, suggesting successful stress conditioning of both groups (Xiao et al 2003). In a study of factory workers exposed to coke-oven emissions, they found a negative correlation between Hsp levels and deoxyribonucleic acid damage in lymphocytes, suggesting a protective role against genotoxic damage from coke-oven emissions (Xiao et al 2002).

Manuscripts for the Asia-Australian Editor or any other section of Cell Stress & Chaperones can now be submitted electronically at our new website http://cellstress.allentrack.net.