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Metabolic Disorders : Adiposcience-based approach toward novel therapies for the metabolic syndrome
( Hiroaki Masuzaki ),( Tomohiro Tanaka ),( Shintaro Yasue ),( Takako Ishii ),( Sadanori Okada ),( Ken Ebihara ),( Kiminori Hosoda ),( Kazuwa Nakao ) 한국생화학분자생물학회 (구 한국생화학회) 2008 생화학분자생물학회 춘계학술발표논문집 Vol.2008 No.-
Ham, Mira,Lee, Joo-Won,Choi, A Hyun,Jang, Hagoon,Choi, Goun,Park, Jiyoung,Kozuka, Chisayo,Sears, Dorothy D.,Masuzaki, Hiroaki,Kim, Jae Bum American Society for Microbiology 2013 Molecular and cellular biology Vol.33 No.12
<P>Glucose-6-phosphate dehydrogenase (G6PD) is a key enzyme that regulates cellular redox potential. In this study, we demonstrate that macrophage G6PD plays an important role in the modulation of proinflammatory responses and oxidative stress. The G6PD levels in macrophages in the adipose tissue of obese animals were elevated, and G6PD mRNA levels positively correlated with those of proinflammatory genes. Lipopolysaccharide (LPS) and free fatty acids, which initiate proinflammatory signals, stimulated macrophage G6PD. Overexpression of macrophage G6PD potentiated the expression of proinflammatory and pro-oxidative genes responsible for the aggravation of insulin sensitivity in adipocytes. In contrast, when macrophage G6PD was inhibited or suppressed via chemical inhibitors or small interfering RNA (siRNA), respectively, basal and LPS-induced proinflammatory gene expression was attenuated. Furthermore, macrophage G6PD increased activation of the p38 mitogen-activated protein kinase (MAPK) and NF-κB pathways, which may lead to a vicious cycle of oxidative stress and proinflammatory cascade. Together, these data suggest that an abnormal increase of G6PD in macrophages promotes oxidative stress and inflammatory responses in the adipose tissue of obese animals.</P>
Role of Rho-kinase in regulation of insulin action and glucose homeostasis
Furukawa, Noboru,Ongusaha, Pat,Jahng, Wan Jin,Araki, Kazushi,Choi, Cheol Soo,Kim, Hyo-Jeong,Lee, Yong Hee,Kaibuchi, Kozo,Kahn, Barbara B.,Masuzaki, Hiroaki,Kim, Jason K.,Lee, Sam W.,Kim, Young-Bum Elsevier 2005 Cell metabolism Vol.2 No.2
<P><B>Summary</B></P><P>Accumulating evidence indicates an important role for serine phosphorylation of IRS-1 in the regulation of insulin action. Recent studies suggest that Rho-kinase (ROK) is a mediator of insulin signaling, via interaction with IRS-1. Here we show that insulin stimulation of glucose transport is impaired when ROK is chemically or biologically inhibited in cultured adipocytes and myotubes and in isolated soleus muscle ex vivo. Inactivation of ROK also reduces insulin-stimulated IRS-1 tyrosine phosphorylation and PI3K activity. Moreover, inhibition of ROK activity in mice causes insulin resistance by reducing insulin-stimulated glucose uptake in skeletal muscle in vivo. Mass spectrometry analysis identifies IRS-1 Ser632/635 as substrates of ROK in vitro, and mutation of these sites inhibits insulin signaling. These results strongly suggest that ROK regulates insulin-stimulated glucose transport in vitro and in vivo. Thus, ROK is an important regulator of insulin signaling and glucose metabolism.</P>