Synthesis of 60- and 72 kDa heat shock proteins in early porcine embryogenesis

King, Y.T; Lee, W.C; Gao, Mengxiang; Wang, J.L; Tu, Ching-Fu; Wu, Shinn-Chih; Kuo, Y. H.

doi:10.1016/s0378-4320(00)00174-3

Cited by 5 publications

(2 citation statements)

References 17 publications

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“…Two-dimensional (2D)-PAGE was performed as described previously (King et al, 2000). Approximately 300 µg of protein was loaded onto the isoelectrofocusing (IEF) gel and electrophoresized at 400 V for 16 h and then at 800 V for 1 h. Subsequently, the IEF gels were laid onto 9 % SDSpolyacrylamide slab gels with a 4.75 % stacking gel in the second dimension.…”

Section: Gel Electrophoresis and Immunoblot Analysismentioning

confidence: 99%

Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice

King

Lin

et al. 2002

Journal of Experimental Biology

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SUMMARY Molecular mechanisms of whole-body thermotolerance (WBT) in mammals have not been investigated thoroughly. The purpose of this study was to assess the induction of the 70 kDa heat shock protein (HSP70) and antioxidant enzyme activity in animal WBT, which was induced by whole-body hyperthermia (WBH) in mice. As a preconditioning treatment, WBH was applied to mice to induce WBT. Synthesis of inducible HSP70 (HSP70i) and quantification of its increased level in liver were investigated by one- and two-dimensional polyacrylamide gel electrophoresis and immunoblotting. HSP70i synthesis in mice liver was induced by non-lethal WBH (41°C, 30 min). When compared to control animals, the level of liver HSP70i increased substantially (by 3.6-fold; P<0.0001). When exposed to 30 min of hyperthermia preconditioning, and after recovery for 48 h, the survival rate was 88.2 %, which was significantly higher than that of the control group (37.5 %; P<0.01). Moreover, the survival rate of animals subjected to preconditioning for 15 min was 72.2 %, which was also significantly higher than that of the control group (P<0.05). In contrast, the survival rate of animals subjected to preconditioning for 45 min was 63.5 %, which was not different from the control group. Nonetheless, the protection index of the group subjected to 15 min and 30 min of preconditioning was 1.93 and 2.37, respectively. Furthermore, to assess their contributions to WBT, the activities of antioxidant enzymes were also measured. After 48 h of recovery in preconditioned animals, hepatic antioxidant enzyme activities, including superoxide dismutase, catalase and glutathione peroxidase, had not changed significantly. To study the molecular mechanism of WBT, we successfully developed a mouse model and suggest that, rather than the activities of antioxidant enzymes, it is HSP70i that has a role to help animals survive during severe heat stress.

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Section: Gel Electrophoresis and Immunoblot Analysismentioning

confidence: 99%

Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice

King

Lin

et al. 2002

Journal of Experimental Biology

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“…The failure of heat shock protein induction after receiving heat shock also could be observed in bovine oocytes, and immature bovine oocytes could exhibit the reaction of heat shock cognate (HSC70) and HSP70 induction associated protein, nonetheless, the reaction rate of between these two proteins are not changed by heat shock (Edwards and Hansen, 1996). King et al (2000) have reported that after the blocking stage, the necessity of HSP60 and HSP72 protein were increased for the development of porcine fertilized oocytes. This phenomenon proved that the HSP gene group is essential for the development of early porcine embryos.…”

Section: Introductionmentioning

confidence: 99%

Association between HSP70 Genotypes and Oocytes Development on In vitro Maturation/Fertilization in Pig

Wee¹,

Park²,

Cho³

et al. 2008

Asian Australas. J. Anim. Sci

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This study was performed to clarify whether the variation of stress related heat shock protein 70 (HSP70) (GenBank X68213) gene was associated with the nuclear morphological change of in vitro maturation and in vitro capacitation in oocytes of pig ovaries obtained at the slaughterhouse. The nucleic acid substitution of C to G at the 483rd position was found out in HSP70 K1 (290-512) from X68213. The ovaries were categorized into CC, CG, and GG genotypes using polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) (BsiHKA I). After the second in vitro maturation of immature fresh oocytes, the relation of nuclear morphological change in oocytes with the genotype of HSP70 K1 gene was such that the MII ratios of the genotype GG and CG (46.93% and 42.20%, respectively) were significantly higher than that of the CC genotype (10.71%) (p<0.05). With respect to in vitro maturation of frozen-thawed oocytes by an open pulled straw (OPS) method, the percentage of oocytes matured to MII stage of the CG genotype showed a higher trend than CC and GG genotypes. After the in vitro maturation of immature fresh oocytes and frozen-thawed oocytes by the OPS method, the relation of the pronuclei change in oocytes matured in vitro with HSP70 genotype was assessed, and the result showed that the enlarged sperm heads (ESH) of matured fresh oocytes and frozen-thawed oocytes were 80.0% and 60.0% in the CC genotype, respectively. The CC genotype group had a significantly higher rate of ESH than the CG and the GG genotype group (p<0.05). The ratios of polyspermic invasion were not different among HSP70 of the three genotypes. It was considered that the rate of in vitro maturation of fertilized oocytes was expected to differ according to genotype of the stress related gene.

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Expression of HSP70/HSC70 in swine blastocysts: Effects of oxidative and thermal stress

Bernardini

Fantinati

Zannoni

et al. 2004

Molecular Reproduction Devel

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Stress proteins are induced in response to a wide range of biological and physicochemical stresses; HSC70 (constitutive) and HSP70 (inducible) belong to the HSP70 stress protein family. The present study aimed at investigating whether environmental stress, particularly thermal and oxidative stress, is involved in modulating HSP70/HSC70 expression in in vitro porcine embryos from two/four cell stage to blastocyst. For oxidative stress, embryos were cultured at 38.5 degrees C under a 5% O2-5% CO2 atmosphere or 5% CO2 in air (approximately 20% O2); for thermal stress, embryos were cultured at 38.5 degrees C under 5% O2, 5% CO2, and exposed to heat shock (1 hr at 42 degrees C). At the end of culture, embryos were analysed by Western blotting, using specific antibodies discriminating HSP70 from HSC70. Embryos cultured under 20% O2 showed HSC70 levels significantly higher (P < 0.005) than embryos cultured under 5% O2, while heat shocked embryos presented HSP70 levels higher (P < 0.01) than control group. In addition, the developmental rate of embryos was negatively affected by the higher oxygen tension (P < 0.05). Our data indicate that porcine embryos express both HSP70 and HSC70 and could differentially respond to both oxidative and heat stress by up-regulating HSC70 and HSP70, respectively.

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Synthesis of 60- and 72 kDa heat shock proteins in early porcine embryogenesis

Cited by 5 publications

References 17 publications

Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice

Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice

Association between HSP70 Genotypes and Oocytes Development on In vitro Maturation/Fertilization in Pig

Expression of HSP70/HSC70 in swine blastocysts: Effects of oxidative and thermal stress

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