Effect of 43°C treatment on expression of heat shock proteins 105, 70 and 60 in cultured monkey Sertoli cells

Min Chen, Jin Xiang Yuan, Yu Qiang Shi, Xue Sen Zhang, Zhao Yuan Hu, Fei Gao, Yi Xun Liu

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Aim: To examine the possible effect of heat treatment on expression of heat shock proteins (Hsps) 105, 70, and 60 in primary monkey Sertoli cells and to evaluate the possible signal pathways. Methods: Western blot analysis, realtime polymerase chain reaction (PCR), and confocal immunohistochemistry were used to analyze mRNA and protein levels of the Hsps in response to 43°C treatment of Sertoli cells isolated from pubertal monkey testes. Results: Staining with Hoechst 33342 indicated Sertoli cells did not undergo apoptosis after heat treatment. Hsp105 was expressed in cytoplasm of untreated Sertoli cells. Both Hsp105 mRNA and protein levels were increased approximately 20-fold compared to those of the untreated controls at 12 h after heat treatment. Untreated Sertoli cells did not express Hsp70, but heat stress induced its expression in the cell cytoplasm. The time-course of changes in Hsp70 was similar to that of Hsp105. In contrast to Hsp105 and Hsp70, the change in Hsp60 expression was much less obvious. The protein level between 12 h and 48 h after heat treatment was only approximately 1.5-fold that of the untreated control. Extracellular regulated kinase (ERK) 1/2 inhibitor (U0126) or phosphoinositide kinase-3 (PI3K) inhibitor (LY294002) could partially block the response of Hsp105 and Hsp70 induced by heat treatment. Conclusion: These results indicate that the heat-induced expression of the three types of Hsp in monkey Sertoli cells might be regulated by ERK and/or PI3K signal pathways, but the profile of their expression is different, suggesting that they might have different regulatory functions in Sertoli cells.

Original languageEnglish (US)
Pages (from-to)474-485
Number of pages12
JournalAsian Journal of Andrology
Volume10
Issue number3
DOIs
StatePublished - May 2008
Externally publishedYes

Fingerprint

Chaperonin 60
HSP70 Heat-Shock Proteins
Sertoli Cells
Haplorhini
Hot Temperature
Phosphatidylinositol 3-Kinases
Therapeutics
Signal Transduction
Cytoplasm
Phosphotransferases
Messenger RNA
Proteins
2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one
1-Phosphatidylinositol 4-Kinase
Heat-Shock Proteins
Testis
Western Blotting
Immunohistochemistry
Apoptosis
Staining and Labeling

Keywords

  • Heat treatment
  • Hsp105
  • Hsp60
  • Hsp70
  • Monkey
  • Sertoli cells

ASJC Scopus subject areas

  • Nephrology
  • Endocrinology

Cite this

Effect of 43°C treatment on expression of heat shock proteins 105, 70 and 60 in cultured monkey Sertoli cells. / Chen, Min; Yuan, Jin Xiang; Shi, Yu Qiang; Zhang, Xue Sen; Hu, Zhao Yuan; Gao, Fei; Liu, Yi Xun.

In: Asian Journal of Andrology, Vol. 10, No. 3, 05.2008, p. 474-485.

Research output: Contribution to journalArticle

Chen, Min ; Yuan, Jin Xiang ; Shi, Yu Qiang ; Zhang, Xue Sen ; Hu, Zhao Yuan ; Gao, Fei ; Liu, Yi Xun. / Effect of 43°C treatment on expression of heat shock proteins 105, 70 and 60 in cultured monkey Sertoli cells. In: Asian Journal of Andrology. 2008 ; Vol. 10, No. 3. pp. 474-485.
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abstract = "Aim: To examine the possible effect of heat treatment on expression of heat shock proteins (Hsps) 105, 70, and 60 in primary monkey Sertoli cells and to evaluate the possible signal pathways. Methods: Western blot analysis, realtime polymerase chain reaction (PCR), and confocal immunohistochemistry were used to analyze mRNA and protein levels of the Hsps in response to 43°C treatment of Sertoli cells isolated from pubertal monkey testes. Results: Staining with Hoechst 33342 indicated Sertoli cells did not undergo apoptosis after heat treatment. Hsp105 was expressed in cytoplasm of untreated Sertoli cells. Both Hsp105 mRNA and protein levels were increased approximately 20-fold compared to those of the untreated controls at 12 h after heat treatment. Untreated Sertoli cells did not express Hsp70, but heat stress induced its expression in the cell cytoplasm. The time-course of changes in Hsp70 was similar to that of Hsp105. In contrast to Hsp105 and Hsp70, the change in Hsp60 expression was much less obvious. The protein level between 12 h and 48 h after heat treatment was only approximately 1.5-fold that of the untreated control. Extracellular regulated kinase (ERK) 1/2 inhibitor (U0126) or phosphoinositide kinase-3 (PI3K) inhibitor (LY294002) could partially block the response of Hsp105 and Hsp70 induced by heat treatment. Conclusion: These results indicate that the heat-induced expression of the three types of Hsp in monkey Sertoli cells might be regulated by ERK and/or PI3K signal pathways, but the profile of their expression is different, suggesting that they might have different regulatory functions in Sertoli cells.",
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T1 - Effect of 43°C treatment on expression of heat shock proteins 105, 70 and 60 in cultured monkey Sertoli cells

AU - Chen, Min

AU - Yuan, Jin Xiang

AU - Shi, Yu Qiang

AU - Zhang, Xue Sen

AU - Hu, Zhao Yuan

AU - Gao, Fei

AU - Liu, Yi Xun

PY - 2008/5

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N2 - Aim: To examine the possible effect of heat treatment on expression of heat shock proteins (Hsps) 105, 70, and 60 in primary monkey Sertoli cells and to evaluate the possible signal pathways. Methods: Western blot analysis, realtime polymerase chain reaction (PCR), and confocal immunohistochemistry were used to analyze mRNA and protein levels of the Hsps in response to 43°C treatment of Sertoli cells isolated from pubertal monkey testes. Results: Staining with Hoechst 33342 indicated Sertoli cells did not undergo apoptosis after heat treatment. Hsp105 was expressed in cytoplasm of untreated Sertoli cells. Both Hsp105 mRNA and protein levels were increased approximately 20-fold compared to those of the untreated controls at 12 h after heat treatment. Untreated Sertoli cells did not express Hsp70, but heat stress induced its expression in the cell cytoplasm. The time-course of changes in Hsp70 was similar to that of Hsp105. In contrast to Hsp105 and Hsp70, the change in Hsp60 expression was much less obvious. The protein level between 12 h and 48 h after heat treatment was only approximately 1.5-fold that of the untreated control. Extracellular regulated kinase (ERK) 1/2 inhibitor (U0126) or phosphoinositide kinase-3 (PI3K) inhibitor (LY294002) could partially block the response of Hsp105 and Hsp70 induced by heat treatment. Conclusion: These results indicate that the heat-induced expression of the three types of Hsp in monkey Sertoli cells might be regulated by ERK and/or PI3K signal pathways, but the profile of their expression is different, suggesting that they might have different regulatory functions in Sertoli cells.

AB - Aim: To examine the possible effect of heat treatment on expression of heat shock proteins (Hsps) 105, 70, and 60 in primary monkey Sertoli cells and to evaluate the possible signal pathways. Methods: Western blot analysis, realtime polymerase chain reaction (PCR), and confocal immunohistochemistry were used to analyze mRNA and protein levels of the Hsps in response to 43°C treatment of Sertoli cells isolated from pubertal monkey testes. Results: Staining with Hoechst 33342 indicated Sertoli cells did not undergo apoptosis after heat treatment. Hsp105 was expressed in cytoplasm of untreated Sertoli cells. Both Hsp105 mRNA and protein levels were increased approximately 20-fold compared to those of the untreated controls at 12 h after heat treatment. Untreated Sertoli cells did not express Hsp70, but heat stress induced its expression in the cell cytoplasm. The time-course of changes in Hsp70 was similar to that of Hsp105. In contrast to Hsp105 and Hsp70, the change in Hsp60 expression was much less obvious. The protein level between 12 h and 48 h after heat treatment was only approximately 1.5-fold that of the untreated control. Extracellular regulated kinase (ERK) 1/2 inhibitor (U0126) or phosphoinositide kinase-3 (PI3K) inhibitor (LY294002) could partially block the response of Hsp105 and Hsp70 induced by heat treatment. Conclusion: These results indicate that the heat-induced expression of the three types of Hsp in monkey Sertoli cells might be regulated by ERK and/or PI3K signal pathways, but the profile of their expression is different, suggesting that they might have different regulatory functions in Sertoli cells.

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