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RISS 인기검색어
- 검색키워드
- 저자 : ( Syed M. Hussaini Qadri ) (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
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( Dhanikachalam Velu ),( Kangayam. M. Ponnuvel ),( Syed. M. Hussaini Qadri ) 한국잠사학회 2008 International Journal of Industrial Entomology Vol.16 No.1
The expression of heat shock protein genes (Hsp 70, Hsp 40, Hsp 20.8 and Hsp 20.4) against thermal stress in silkworm Bombyx mori was performed through semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR). Upon exposure of silkworm to two temperature regimes (38℃ and 42℃), significant change in the expression of Hsp gene was observed as compared to the control. Hsp 70 and Hsp 40 showed increased expression than the small heat shock protein genes Hsp 20.8 and Hsp 20.4. The Hsp 70 showed increased expression during the recovery period as compared to 1 hr thermal treatments (38℃/1 hr and 42℃/1 hr). Whereas, Hsp 40, Hsp 20.8 and Hsp 20.4 genes showed higher expression level at initial stages that later gradually decrease during recovery period. Tissue specific expression of Hsp 70 showed variation in the level of expression amongst the tissues. The mid gut and fat body tissues showed higher expression than the cuticle and silk gland tissue. The Hsp 70, Hsp 40 gene expression was analyzed in thermotolerant (Nistari) and thermo susceptible silk worm strain (NB4D2) and results showed significant variation in their expression level. The Nistari showed higher expression of Hsp 70 and Hsp 40 genes than the NB4D2. These findings provide a better understanding of cellular protection mechanisms against environmental stress such as heat shock, as these Hsps are involved in an organism thermotolerance.
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Expression of the Heat Shock Protein Genes in Response to Thermal Stress in the Silkworm Bombyx mori
Velu, Dhanikachalam,Ponnuvel, Kangayam. M.,Qadri, Syed. M. Hussaini Korean Society of Sericultural Science 2008 International Journal of Industrial Entomology Vol.16 No.1
The expression of heat shock protein genes (Hsp 70, Hsp 40, Hsp 20.8 and Hsp 20.4) against thermal stress in silkworm Bombyx mori was performed through semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR). Upon exposure of silkworm to two temperature regimes ($38^{\circ}C$ and $42^{\circ}C$), significant change in the expression of Hsp gene was observed as compared to the control. Hsp 70 and Hsp 40 showed increased expression than the small heat shock protein genes Hsp 20.8 and Hsp 20.4. The Hsp 70 showed increased expression during the recovery period as compared to 1 hr thermal treatments ($38^{\circ}C$/1 hr and $42^{\circ}C$/1 hr). Whereas, Hsp 40, Hsp 20.8 and Hsp 20.4 genes showed higher expression level at initial stages that later gradually decrease during recovery period. Tissue specific expression of Hsp 70 showed variation in the level of expression amongst the tissues. The mid gut and fat body tissues showed higher expression than the cuticle and silk gland tissue. The Hsp 70, Hsp 40 gene expression was analyzed in thermotolerant (Nistari) and thermo susceptible silk worm strain (NB4D2) and results showed significant variation in their expression level. The Nistari showed higher expression of Hsp 70 and Hsp 40 genes than the NB4D2. These findings provide a better understanding of cellular protection mechanisms against environmental stress such as heat shock, as these Hsps are involved in an organism thermotolerance.
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Saravanakumar, Ragunathan,Ponnuvel, Kangayam M.,Velu, Dhanikachalam,Koundinya, Panguluri R.,Sinha, Randir K.,Qadri, Syed M. Hussaini Korean Society of Sericultural Science 2008 International Journal of Industrial Entomology Vol.16 No.2
The diapause and non diapause associated proteins of multivoltine silkworm eggs were analysed by two dimensional (2D) gel electrophoresis. The study was made at 0 hr, 24 hrs and 48 hrs after oviposition. A total of four protein spots in diapause eggs at 24 hrs of oviposition and two protein spots in non diapause eggs at 0 hrs of oviposition were observed. All the six protein spots were considered to have association with diapause and non diapause characters. The molecular weight (MW) and isoelectric point (PI) of these 6 protein spots were calculated. The protein spots 1 and 2 observed in 0 hr of non diapause eggs were found to have the MW of 67 and 75 KDa and PI of 8.6 and 8.4 respectively. Similarly the four protein spots observed in diapause egg at 24 hrs of oviposition exhibited MW viz., 15, 17,20 and 25 KDa and PI of 5.3, 5.8, 6.5 and 6.0 respectively. All these 6 identified protein spots were subjected to in-gel digestion and resulted tryptic peptides were analyzed by Matrix-assisted laser desorption/ionization time-of flight mass spectrometry (MALDI TOF-MS). Databases searched based on experimentally determined molecular weights of peptides for the determination of the identities of proteins. The identified proteins indicated homology of 34% to 95%. The results indicate that the proteins may playa role in development of diapause and non diapause eggs.
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( Ragunathan Saravanakumar ),( Kangayam M. Ponnuvel ),( Dhanikachalam Velu ),( Panguluri R. Koundinya ),( Randir K. Sinha ),( Syed M. Hussaini Qadri ) 한국잠사학회 2008 International Journal of Industrial Entomology Vol.16 No.2
The diapause and non diapause associated proteins of multivoltine silkworm eggs were analysed by two dimensional (2D) gel electrophoresis. The study was made at 0 hr, 24 hrs and 48 hrs after oviposition. A total of four protein spots in diapause eggs at 24 hrs of oviposition and two protein spots in non diapause eggs at 0 hrs of oviposition were observed. All the six protein spots were considered to have association with diapause and non diapause characters. The molecular weight (MW) and isoelectric point (PI) of these 6 protein spots were calculated. The protein spots 1 and 2 observed in 0 hr of non diapause eggs were found to have the MW of 67 and 75 KDa and PI of 8.6 and 8.4 respectively. Similarly the four protein spots observed in diapause egg at 24 hrs of oviposition exhibited MW viz., 15, 17, 20 and 25 KDa and PI of 5.3, 5.8, 6.5 and 6.0 respectively. All these 6 identified protein spots were subjected to in-gel digestion and resulted tryptic peptides were analyzed by Matrix-assisted laser desorption/ionization time-of flight mass spectrometry (MALDI TOF-MS). Databases searched based on experimentally determined molecular weights of peptides for the determination of the identities of proteins. The identified proteins indicated homology of 34% to 95%. The results indicate that the proteins may play a role in development of diapause and non diapause eggs.
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