Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Tatsuhito Uno"'
Autor:
Tetsuro Haruta, Junko Kawahara, Kazuyuki Hiratani, Tatsuhito Uno, Isao Usui, Yukiko Kanatani, Minoru Iwata, Atsuko Takano, Kazuyuki Tobe, Masashi Kobayashi
Publikováno v:
The Open Diabetes Journal. 3:14-21
IRS-1 is a major substrate for insulin receptor tyrosine kinase. It is reported that intracellular translocation of serine-phosphorylated IRS-1 from low density microsome (LDM) fraction to cytosol attenuates its ability to transmit insulin signaling
Autor:
Junko Kawahara, Tatsuhito Uno, Isao Usui, Minoru Iwata, Atsuko Takano, Tetsuro Haruta, Masashi Kobayashi
Publikováno v:
Molecular and Cellular Biology. 21:5050-5062
A pathway sensitive to rapamycin, a selective inhibitor of mammalian target of rapamycin (mTOR), down-regulates effects of insulin such as activation of Akt (protein kinase B) via proteasomal degradation of insulin receptor substrate 1 (IRS-1). We re
Autor:
Tetsuro Haruta, Junko Kawahara, Tatsuhito Uno, Eiichi Ueno, Isao Usui, Toshiyasu Sasaoka, Minoru Iwata, Masashi Kobayashi, Atsuko Takano
Publikováno v:
Diabetes. 50:1891-1900
Growth hormone (GH) is well known to induce in vivo insulin resistance. However, the molecular mechanism of GH-induced cellular insulin resistance is largely unknown. In this study, we demonstrated that chronic GH treatment of differentiated 3T3-L1 a
Autor:
Masashi Kobayashi, Tetsuro Haruta, Toshiyasu Sasaoka, Junko Kawahara, Tatsuhito Uno, Isao Usui, Eiichi Ueno, Minoru Iwata, Atsuko Takano
Publikováno v:
Biochemical and Biophysical Research Communications. 275:115-120
In the early phase of adipocyte differentiation, transient increase of DNA synthesis, called clonal expansion, and transient hyperphosphorylation of retinoblastoma protein (Rb) are observed. We investigated the role of these phenomena in insulin-indu
Autor:
Junko Kawahara, Tatsuhito Uno, Prem M. Sharma, Tetsuro Haruta, Katsuya Egawa, Atsuko Takano, Masashi Kobayashi, Jerrold M. Olefsky
Publikováno v:
Molecular Endocrinology. 14:783-794
Insulin receptor substrate-1 (IRS-1) is a major substrate of the insulin receptor and acts as a docking protein for Src homology 2 domain containing signaling molecules that mediate many of the pleiotropic actions of insulin. Insulin stimulation elic
Autor:
Tetsuro Haruta, Tsutomu Wada, Tatsuhito Uno, Isao Usui, Hajime Ishihara, Manabu Ishiki, Toshiyasu Sasaoka, Masashi Kobayashi, Minoru Iwata, Atsuko Takano, Eiichi Ueno
Publikováno v:
Biochemical and Biophysical Research Communications. 252:139-144
Shc is phosphorylated on Tyr-239/240 and/or Tyr-317, which serves as a docking site for Grb2. To clarify the relative involvement of Shc Tyr-239/240 and Tyr-317 in insulin-induced mitogenesis, we generated expression vectors for Y317F (1F)-Shc, Y239/