scholarly journals Characterization of Heat Shock Protein 60 as an Interacting Partner of Superoxide Dismutase 2 in the Silkworm, Bombyx mori, and Its Response to the Molting Hormone, 20-Hydroxyecdysone

Antioxidants ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 1385
Author(s):  
Yosui Nojima
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Bombyx Mori ◽  
Molecular Mechanisms ◽  
Heat Shock Protein 60 ◽  
Molting Hormone ◽  
Superoxide Dismutase 2 ◽  
Silkworm Bombyx Mori

Oxidative stress promotes pupation in some holometabolous insects. The levels of superoxide, a reactive oxygen species (ROS), are increased and superoxide dismutase 1 (BmSod1) and superoxide dismutase 2 (BmSod2) are decreased during metamorphic events in silkworm (Bombyx mori). These observations strongly suggest that pupation is initiated by oxidative stress via the down-regulation of BmSod1 and BmSod2. However, the molecular mechanisms underlying ROS production during metamorphic events in silkworm remain unknown. To investigate these molecular mechanisms, the peripheral proteins of BmSod1 and BmSod2 were identified and characterized using dry and wet approaches in this study. Based on the results, silkworm heat shock protein 60 (BmHsp60) was identified as an interacting partner of BmSod2, which belongs to the Fe/MnSOD family. Furthermore, the present study results showed that BmHsp60 mRNA expression levels were increased in response to oxidative stress caused by ultraviolet radiation and that BmHsp60 protein levels (but not mRNA levels) were decreased during metamorphic events, which are regulated by the molting hormone 20-hydroxyecdysone. These findings improve our understanding of the mechanisms by which holometabolous insects control ROS during metamorphosis.

Expression of metabolic enzyme genes and heat-shock protein genes during embryonic development in diapause and non-diapause egg of multivoltine silkworm Bombyx mori

Biologia ◽  
2008 ◽  
Vol 63 (5) ◽  
Author(s):  
Ragunathan Saravanakumar ◽  
Kangayam Ponnuvel ◽  
Syed Qadri
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Bombyx Mori ◽  
Early Stage ◽  
Metabolic Enzyme ◽  
Dehydrogenase Gene ◽  
Heat Shock Protein Genes ◽  
High Level ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Silkworm Bombyx Mori

AbstractThe expression of metabolic enzyme genes and heat-shock protein genes (Hsp) during early embryogenesis in diapause and non-diapause eggs of the silkworm Bombyx mori was quantified by semi-quantitative RT-PCR. The trehalase gene (Tre) was expressed in non-diapause eggs up-to nine days, while in diapause eggs was not up regulated. The glycogen phosphorylase gene (GPase) was expressed in non-diapause eggs, whereas in diapause eggs a high level was observed in early stage, but down regulated in later stage. The phosphofructokinase gene (PFK) and sorbitol dehyrogenase-2 gene (SDH-2) expression was fluctuated in non-diapause eggs, whereas in diapause eggs these were expressed only at early stage and not observed in later stage. The glucose-6-phosphate dehydrogenase gene (G6P-DH) in non-diapause eggs was highly expressed during the differentiation phase and decreased in the organogenesis phase. In contrast to this, expression in diapause eggs was of low level during differentiation phase and of high level observed in the organogenesis phase. In the tissues, PFK and SDH-2 were selectively expressed in cuticle and midgut, whereas Tre expression was high in midgut and ovary of larvae incubated at 15°C. The Hsp (20.4, 20.8, 40, 70, and 90) were expressed in both diapause and non-diapause eggs. Their expression was, however, selective in tissues with Hsp20.4 in midgut and ovary, Hsp40 in head, Hsp70 in cuticle and Hsp90 in ovary and head in high amounts at 15°C. These results suggest that the metabolic enzyme genes studied except Hsp play a major role during embryogenesis of diapause and non-diapause silkworm.

scholarly journals Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function

2016 ◽  
Vol 292 (6) ◽  
pp. 2369-2378 ◽  
Author(s):  
Adeleye J. Afolayan ◽  
Maxwell Alexander ◽  
Rebecca L. Holme ◽  
Teresa Michalkiewicz ◽  
Ujala Rana ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Glutamic Acid ◽  
Heat Shock Protein 70 ◽  
Domain Mapping ◽  
Superoxide Dismutase 2

Acute and severe hypobaric hypoxia increases oxidative stress and impairs mitochondrial function in mouse skeletal muscle

2005 ◽  
Vol 99 (4) ◽  
pp. 1247-1253 ◽  
Author(s):  
José Magalhães ◽  
António Ascensão ◽  
José M. C. Soares ◽  
Rita Ferreira ◽  
Maria J. Neuparth ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Vitamin E ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Hypobaric Hypoxia ◽  
Sulfhydryl Group ◽  
Protein Carbonyls ◽  
Heat Shock Protein 60

Severe high-altitude hypoxia exposure is considered a triggering stimulus for redox disturbances at distinct levels of cellular organization. The effect of an in vivo acute and severe hypobaric hypoxic insult (48 h at a pressure equivalent to 8,500 m) on oxidative damage and respiratory function was analyzed in skeletal muscle mitochondria isolated from vitamin E-supplemented (60 mg/kg ip, 3 times/wk for 3 wk) and nonsupplemented mice. Forty male mice were randomly divided into four groups: control + placebo, hypoxia + placebo (H + P), control + vitamin E, and hypoxia + vitamin E. Significant increases in mitochondrial heat shock protein 60 expression and protein carbonyls group levels and decreases in aconitase activity and sulfhydryl group content were found in the H + P group when compared with the control + placebo group. Mitochondrial respiration was significantly impaired in animals from the H + P group, as demonstrated by decreased state 3 respiratory control ratio and ADP-to-oxygen ratio and by increased state 4 with both complex I- and II-linked substrates. Using malate + pyruvate as substrates, hypoxia decreased the respiratory rate in the presence of carbonyl cyanide m-chlorophenylhydrazone and also stimulated oligomycin-inhibited respiration. However, vitamin E treatment attenuated the effect of hypoxia on the mitochondrial levels of heat shock protein 60 and markers of oxidative stress. Vitamin E was also able to prevent most mitochondrial alterations induced by hypobaric hypoxia. In conclusion, hypobaric hypoxia increases mitochondrial oxidative stress while decreasing mitochondrial capacity for oxidative phosphorylation. Vitamin E was an effective preventive agent, which further supports the oxidative character of mitochondrial dysfunction induced by hypoxia.

scholarly journals Systemic Response of Antioxidants, Heat Shock Proteins, and Inflammatory Biomarkers to Short-Lasting Exercise Training in Healthy Male Subjects

2021 ◽  
Vol 2021 ◽  
pp. 1-15
Author(s):  
Ivan Dimauro ◽  
Elisa Grazioli ◽  
Veronica Lisi ◽  
Flavia Guidotti ◽  
Cristina Fantini ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Lipid Oxidation ◽  
Immune Cells ◽  
Aerobic Training ◽  
Fold Change ◽  
Carbonyl Content ◽  
Short Term

Regular physical activity can enhance immune function and effectively prevents the spread of the cytokine response, thus reducing systemic low-grade inflammation and improving various immune markers. Moreover, regular exercise maintains redox homeostasis in skeletal muscle and other tissues, including immune cells, but the interconnection between the anti-inflammatory effects of exercise with the redox status of immune cells is still poorly understood. With the aim to verify the overall beneficial effect of regular training on the immune system, we have examined the acute and short-term effect of a 5-day exercise program on the modulation of protein and lipid oxidation, antioxidants (i.e., superoxide dismutase-1 (SOD1) and superoxide dismutase-2 (SOD2), glutathione peroxide 1 (GPx1), thioredoxin reductase-1 (TrxR1), and catalase (CAT)), and heat shock protein expression (i.e., heat shock protein-70 (HSP70) and heat shock protein-27 (HSP27)), at both mRNA and protein levels, as well as the activation of the nuclear factor kappa light chain enhancer of activated B cells (NFκB) in peripheral blood mononuclear cells (PBMCs). Moreover, plasmatic markers of oxidative stress, inflammation, and stress response (i.e., protein carbonyl content, interleukin-6 (IL6), interleukin-8 (IL8), interleukin-10 (IL10), interleukin-17E (IL17E), interleukin-17F (IL17F), interleukin-21 (IL21), interleukin-22 (IL22), and interleukin-23 (IL23)) were analyzed in active untrained young adult subjects. Even in the absence of an increased amount of protein or lipid oxidation, we confirmed a PBMC upregulation of SOD1 ( 1.26 ± 0.07 fold change, p < 0.05 ), HSP70 ( 1.59 ± 0.28 fold change, p < 0.05 ), and HSP27 gene expression ( 1.49 ± 0.09 fold change, p < 0.05 ) after 3 hours from the first bout of exercise, followed by an increase in proteins’ amount at 24 hours (SOD1, 1.80 ± 0.34 fold change; HSP70, 3.40 ± 0.58 fold change; and HSP27, 1.81 ± 0.20 fold change, p < 0.05 ) and return to basal levels after the 5 days of aerobic training. Indeed, the posttraining basal levels of oxidized molecules in plasma and PBMCs were statistically lower than the pretraining levels (carbonyl content, 0.50 ± 0.05 fold change, p < 0.01 ), paralleled by a lower expression of SOD2, Gpx1, and TrxR1, at mRNA (SOD2, 0.63 ± 0.06 ; GPx1, 0.69 ± 0.07 ; and TrxR1, 0.69 ± 0.12 fold change, p < 0.05 ) and protein (TrxR1, 0.49 ± 0.11 fold change, p < 0.05 ) levels. These results verified the existence of an early phase of redox adaptation to physical exercise already achievable after 5 days of moderate, regular aerobic training. More interestingly, this phenomenon was paralleled by the degree of NFκB activation in PBMCs and the decrease of plasmatic proinflammatory cytokines IL8, IL21, and IL22 in the posttraining period, suggesting an interconnected, short-term efficacy of aerobic exercise towards systemic oxidative stress and inflammation.

scholarly journals The small heat shock protein (sHSP) genes in the silkworm, Bombyx mori, and comparative analysis with other insect sHSP genes

2009 ◽  
Vol 9 (1) ◽  
pp. 215 ◽  
Author(s):  
Zi-Wen Li ◽  
Xue Li ◽  
Quan-You Yu ◽  
Zhong-Huai Xiang ◽  
Hirohisa Kishino ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Bombyx Mori ◽  
Small Heat Shock Protein ◽  
Silkworm Bombyx Mori

scholarly journals Analysis of transcripts of heat shock protein genes in silkworm, Bombyx mori (Lepidoptera: Bombycidae)

2015 ◽  
Vol 112 (4) ◽  
pp. 676-687 ◽  
Author(s):  
Nalavadi CHANDRAKANTH ◽  
Kangayam M. PONNUVEL ◽  
Shunmugam M. MOORTHY ◽  
Sirigineedi SASIBHUSHAN ◽  
Vankadara SIVAPRASAD
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Bombyx Mori ◽  
Heat Shock Protein Genes ◽  
Silkworm Bombyx Mori

scholarly journals Superoxide dismutase down-regulation and the oxidative stress is required to initiate pupation in Bombyx mori

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Yosui Nojima ◽  
Hidemasa Bono ◽  
Takeshi Yokoyama ◽  
Kikuo Iwabuchi ◽  
Ryoichi Sato ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Bombyx Mori ◽  
Microarray Data ◽  
Molting Hormone ◽  
Down Regulation ◽  
Regulation Of Expression ◽  
Defense Systems ◽  
Lepidopteran Insects ◽  
The Common

Abstract Perhaps, oxidative stress progresses pupation in some Lepidopteran insects; however, the reasons for this remain obscure. In our previous study, we clarified Bombyx mori SOD1 (BmSOD1) and B. mori SOD2 (BmSOD2) proteins respond in common to ultraviolet irradiation (UV) oxidative stress and metamorphosis. This result strongly suggested pupation initiates by oxidative stress and might mediate by down-regulation of expression of BmSOD1 and BmSOD2 proteins. Thus, we examined about these relationships in B. mori in this study. In the microarray data reanalysis, we found the Notch signaling pathways as the common pathways in pupation and UV oxidative stress in B. mori. Also, we showed a molting hormone, 20-hydroxyecdysone, leads not only generation of superoxide but also downregulation of the expression of BmSOD proteins during pupation in B. mori. Our findings can contribute to a deeper understanding of how biological defense systems work against environmental oxidative stress.

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