The relationship between myocardial cell damages and HSPs mRNA transcription in heat stressed broilers was studied using a spectrophotometer, the histopathological technique, and fluorescence quantitative reverse tran...The relationship between myocardial cell damages and HSPs mRNA transcription in heat stressed broilers was studied using a spectrophotometer, the histopathological technique, and fluorescence quantitative reverse transcription PCR （FQ RT-PCR）. The results showed that the activities of creatine kinase （CK） and glutamic-pyruvic transaminase （GPT） were induction during the persistent heat stress. The major lesions of the myocardial fibers were granular degeneration and necrosis. The transcription of constitutive or cognate heat shock protein 70 （HSC70） mRNA was changeable. The transcription of heat shock protein 70 （HSPT0） mRNA was increased obviously in the course of persistent heat stress. The results showed that the change of HSC70 mRNA transcription was contrary to the activity of CK, and the level of HSC70 mRNA transcription must be used as a symbol of the myocardial cell damages in the course of persistent heat stress.展开更多
Objective To investigate and compare the effect of radio-frequency(RF)field exposure on expression of heat shock proteins(Hsps)in three human glioma cell lines(MO54,A172,and T98).Methods Cells were exposed to sham or ...Objective To investigate and compare the effect of radio-frequency(RF)field exposure on expression of heat shock proteins(Hsps)in three human glioma cell lines(MO54,A172,and T98).Methods Cells were exposed to sham or 1950 MHz continuous-wave for 1 h.Specific absorption rates(SARs)were 1 and 10 W/kg.Localization and expression of Hsp27 and phosphorylated Hsp27((78)Ser)(p-Hsp27)were examined by immunocytochemistry.Expression levels of Hsp27,p-Hs27,and Hsp70 were determined by Western blotting.Results The Hsp27 was primarily located within the cytoplasm,p-Hsp27 in both cytoplasm and nuclei of MO54,A172,and T98 cells.RF field exposure did not affect the distribution or expression of Hsp27.In addition,Western blotting showed no significant differences in protein expression of Hsp27 or HspT0 between sham-and RF field-exposed cells at a SAR of 1 W/kg and 10 W/kg for 1 h in three cells lines.Exposure to RF field at a SAR of 10 W/kg for 1 h slightly decreased the protein level of phosphorylated Hsp27 in MO54 cells.Conclusion The 1950 MHz RF field has only little or no apparent effect on Hsp70 and Hsp27 expression in MO54,A172,and T98 cells.展开更多
Background Heat shock proteins(HSPs)are key molecular chaperones that help maintain protein homeostasis by stabilizing or removing damaged proteins during cellular stress.Aging weakens these stress–response systems,d...Background Heat shock proteins(HSPs)are key molecular chaperones that help maintain protein homeostasis by stabilizing or removing damaged proteins during cellular stress.Aging weakens these stress–response systems,disrupting proteostasis and increasing vulnerability to sarcopenia.High-intensity training(HIT)can counteract these declines by activating protective pathways such as the HSP response.HSPs are highly responsive to stress,examining their regulation during aging is important,as altered HSP activity is linked to the progressive loss of muscle mass.Methods This study investigated the abundance and phosphorylation of HSPs in skeletal muscle from healthy,active young and older adults(n=7 per group),assessed at baseline and again in the older group following 12 weeks of HIT.Using calibrated Western blotting on both whole-muscle homogenates and pooled single muscle fibres,we quantified HSP content and phosphorylation to determine how aging and exercise influence stress–responsive protein regulation at both the tissue and cellular levels.Results In whole muscle homogenates,HSPs(HSP72,HSP27,andαB-crystallin)did not differ between young and older adults,while higher phosphorylation of small HSPs(sHSPs):phospho-HSP27 at Serine15(pHSP27 Ser15)and phospho-αB-crystallin at Serine59(pαB-crystallin Ser59)(∼1.8-fold and∼2.9-fold,respectively)were found in muscle from older adults,indicating higher cellular stress associated with aging.A 12-week HIT intervention in older adults reduced homogenate pHSP27 Ser15 and pαB-crystallin Ser59 abundances to similar levels found in young adults.Total HSPs typically displayed a distinct fiber-type profile in both age groups,with more in type I compared to type II fibers,distinguished by the presence of myosin heavy chain I(MHCI)or MHCII.Phosphorylation at pHSP27 Ser15 and pαB-crystallin Ser59 was not different between type I and type II fibers.The HIT in older adults decreased total and phosphorylated sHSPs in both type I and type II fibers but increased HSP72 in type I fibers.Conclusion HIT has the potential to mitigate age-related cellular stress and modulate protein expression patterns in aging skeletal muscle and,perhaps,has the potential to delay age-related muscle decline,thereby improving muscle health in older adults.展开更多
基金This work was financially supported by the National Natural Science Foundation of China （30170682, 30571400） the Specialized Research Fund for the Doctoral Program of Higher Education, China （20050307008）.
文摘The relationship between myocardial cell damages and HSPs mRNA transcription in heat stressed broilers was studied using a spectrophotometer, the histopathological technique, and fluorescence quantitative reverse transcription PCR （FQ RT-PCR）. The results showed that the activities of creatine kinase （CK） and glutamic-pyruvic transaminase （GPT） were induction during the persistent heat stress. The major lesions of the myocardial fibers were granular degeneration and necrosis. The transcription of constitutive or cognate heat shock protein 70 （HSC70） mRNA was changeable. The transcription of heat shock protein 70 （HSPT0） mRNA was increased obviously in the course of persistent heat stress. The results showed that the change of HSC70 mRNA transcription was contrary to the activity of CK, and the level of HSC70 mRNA transcription must be used as a symbol of the myocardial cell damages in the course of persistent heat stress.
文摘Objective To investigate and compare the effect of radio-frequency(RF)field exposure on expression of heat shock proteins(Hsps)in three human glioma cell lines(MO54,A172,and T98).Methods Cells were exposed to sham or 1950 MHz continuous-wave for 1 h.Specific absorption rates(SARs)were 1 and 10 W/kg.Localization and expression of Hsp27 and phosphorylated Hsp27((78)Ser)(p-Hsp27)were examined by immunocytochemistry.Expression levels of Hsp27,p-Hs27,and Hsp70 were determined by Western blotting.Results The Hsp27 was primarily located within the cytoplasm,p-Hsp27 in both cytoplasm and nuclei of MO54,A172,and T98 cells.RF field exposure did not affect the distribution or expression of Hsp27.In addition,Western blotting showed no significant differences in protein expression of Hsp27 or HspT0 between sham-and RF field-exposed cells at a SAR of 1 W/kg and 10 W/kg for 1 h in three cells lines.Exposure to RF field at a SAR of 10 W/kg for 1 h slightly decreased the protein level of phosphorylated Hsp27 in MO54 cells.Conclusion The 1950 MHz RF field has only little or no apparent effect on Hsp70 and Hsp27 expression in MO54,A172,and T98 cells.
文摘Background Heat shock proteins(HSPs)are key molecular chaperones that help maintain protein homeostasis by stabilizing or removing damaged proteins during cellular stress.Aging weakens these stress–response systems,disrupting proteostasis and increasing vulnerability to sarcopenia.High-intensity training(HIT)can counteract these declines by activating protective pathways such as the HSP response.HSPs are highly responsive to stress,examining their regulation during aging is important,as altered HSP activity is linked to the progressive loss of muscle mass.Methods This study investigated the abundance and phosphorylation of HSPs in skeletal muscle from healthy,active young and older adults(n=7 per group),assessed at baseline and again in the older group following 12 weeks of HIT.Using calibrated Western blotting on both whole-muscle homogenates and pooled single muscle fibres,we quantified HSP content and phosphorylation to determine how aging and exercise influence stress–responsive protein regulation at both the tissue and cellular levels.Results In whole muscle homogenates,HSPs(HSP72,HSP27,andαB-crystallin)did not differ between young and older adults,while higher phosphorylation of small HSPs(sHSPs):phospho-HSP27 at Serine15(pHSP27 Ser15)and phospho-αB-crystallin at Serine59(pαB-crystallin Ser59)(∼1.8-fold and∼2.9-fold,respectively)were found in muscle from older adults,indicating higher cellular stress associated with aging.A 12-week HIT intervention in older adults reduced homogenate pHSP27 Ser15 and pαB-crystallin Ser59 abundances to similar levels found in young adults.Total HSPs typically displayed a distinct fiber-type profile in both age groups,with more in type I compared to type II fibers,distinguished by the presence of myosin heavy chain I(MHCI)or MHCII.Phosphorylation at pHSP27 Ser15 and pαB-crystallin Ser59 was not different between type I and type II fibers.The HIT in older adults decreased total and phosphorylated sHSPs in both type I and type II fibers but increased HSP72 in type I fibers.Conclusion HIT has the potential to mitigate age-related cellular stress and modulate protein expression patterns in aging skeletal muscle and,perhaps,has the potential to delay age-related muscle decline,thereby improving muscle health in older adults.
