Characteristic Experssion of 105-kDa Heat Shock Protein (HSP105) in Various Tissues of Nonstressed and Heat-Stressed Rats
スポンサーリンク
概要
- 論文の詳細を見る
Although the induction of heat shock proteins (HSP) has been studied extensively in cultured cells, compariatively few studies have examined their expression in vivo. In this report, we investigated the expression and the state of 105-kDa heat shock protein (HSP105) in various tissues of rats, and found that two isoforms of HSP105 (HSP105-a and HSP105-b) were both moderately expressed in adrenal, spleen, liver and heart, and both increased markedly after heat shock. However, in brain HSP105-a was characteristically highly expressed over HSP105-b, but neither increased after heat shock. In addition, a 100-kDa protein (p100), a possible testis-specific HSP105 homologue was found in testis. When the effects of adrenaline and its antagonists on the heat-inducibility of HSP105 were examined, the induction of HSP105 in adrenal gland seemed to be negatively regulated through the α-adrenergic receptor. Furthermore, HSP105 was found to be associated with HSC70/HSP70,and to exist as high molecular mass complexes of 300-800-kDa and of 300-500-kDa in various tissues of nonstressed and heat-stressed rats, respectively. The molecular interaction between HSP105 and HSC70 suggests the possibility that HSP105 functions with HSC70 cooperatively in various tissues of rats.
- 公益社団法人日本薬学会の論文
- 1998-09-15
著者
-
HATAYAMA Takumi
Department of Biochemistry, Kyoto Pharmaceutical University
-
Hatayama Takumi
Department Of Biochemistry And Molecular Biology Kyoto Pharmaceutical University
-
WAKATSUKI Tohru
Department of Biochemistry, Kyoto Pharmaceutical University
-
Wakatsuki Tohru
Department Of Biochemistry Kyoto Pharmaceutical University
-
Hatayama Takumi
Department of Biochemistry & Molecular Biology, Division of Biological Sciences, Kyoto Pharmaceutical University
関連論文
- Hsp105α Enhances Stress-Induced Apoptosis but Not Necrosis in Mouse Embryonal F9 cells
- Characteristic Expression of High Molecular Mass Heat Shock Protein HSP105 during Mouse Embryo Development
- Synthetic small interfering RNA targeting heat shock protein 105 induces apoptosis of various cancer cells both in vitro and in vivo
- DNA vaccination of HSP105 leads to tumor rejection of colorectal cancer and melanoma in mice through activation of both CD4^+ T cells and CD8^+ T cells
- A Comparison of Heat Shock Protein Induction in HeLa Cells by Heat and Chemical Treatments
- Reduced Induction of HSP70 in PC12 Cells during Neuronal Differentiation
- Nuclear Localization Mechanism of Hsp105β and its Possible Function in Mammalian Cells
- Effects of Hyperosmotic NaCl and Glycerol Stress on Stress Response of Human HeLa Cells
- Characteristic Experssion of 105-kDa Heat Shock Protein (HSP105) in Various Tissues of Nonstressed and Heat-Stressed Rats
- Production of Phytochelatins in Polygonum cuspidatum on Exposure to Copper but not to Zinc
- Purification and Some Properties of Copper Reductase from Cell Surface of Debaryomyces hansenii
- Solubilization and Properties of Copper Reducing Enzyme Systems from the Yeast Cell Surface in Debaryomyces hansenii
- Respiratory Inhibition by Copper in Tetrahymena pyriformis GL
- Growth Inhibition by Copper and Copper Intake in Tetrahymena pyriformis GL
- Copper Reduction by Yeast Cell Wall Materials and Its Role on Copper Uptake in Debaryomyces hansenii
- Naringenin Inhibits the Aggregation of Expanded Polyglutamine Tract-Containing Protein through the Induction of Endoplasmic Reticulum Chaperone GRP78
- Reduced Induction of HSP70 in PC12 Cells during Neuronal Differentiation.