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פותח על ידי קלירמאש פתרונות בע"מ -
Low-energy laser irradiation enhances de novo protein synthesis via its effects on translation-regulatory proteins in skeletal muscle myoblasts
Year:
2003
Authors :
ברש, איתמר
;
.
Volume :
1593
Co-Authors:
Shefer, G., Department of Animal Sciences, Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel
Barash, I., Institute of Animal Science, ARO The Volcani Center, Bet Dagan 50250, Israel
Oron, U., Department of Zoology, George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Halevy, O., Department of Animal Sciences, Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel
Facilitators :
From page:
131
To page:
139
(
Total pages:
9
)
Abstract:
Low-energy laser irradiation (LELI) drives quiescent skeletal muscle satellite cells into the cell cycle and enhances their proliferation, thereby promoting skeletal muscle regeneration. Ongoing protein synthesis is a prerequisite for these processes. Here, we studied the signaling pathways involved in the LELI regulation of protein synthesis. High levels of labeled [35S]methionine incorporation were detected in LELI cells as early as 20 min after irradiation, suggesting translation of pre-existing mRNAs. Induced levels of protein synthesis were detected up until 8 h after LELI implying a role for LELI in de novo protein synthesis. Elevated levels of cyclin D1, associated with augmented phosphorylation of the eukaryotic initiation factor 4E (eIF4E) and its inhibitory binding protein PHAS-I, suggested the involvement of LELI in the initiation steps of protein translation. In the presence of the MEK inhibitor, PD98059, eIF4E phosphorylation was abolished and levels of cyclin D1 were dramatically reduced. The LELI-induced PHAS-I phosphorylation was abolished after preincubation with the PI3K inhibitor, Wortmannin. Concomitantly, LELI enhanced Akt phosphorylation, which was attenuated in the presence of Wortmannin. Taken together, these results suggest that LELI induces protein translation via the PI3K/Akt and Ras/Raf/ERK pathways. © 2002 Elsevier Science B.V. All rights reserved.
Note:
Related Files :
Animals
Cell Proliferation
drug effect
low energy radiation
mice
Phosphoproteins
sulfur 35
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/S0167-4889(02)00350-6
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
22553
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:52
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Scientific Publication
Low-energy laser irradiation enhances de novo protein synthesis via its effects on translation-regulatory proteins in skeletal muscle myoblasts
1593
Shefer, G., Department of Animal Sciences, Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel
Barash, I., Institute of Animal Science, ARO The Volcani Center, Bet Dagan 50250, Israel
Oron, U., Department of Zoology, George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Halevy, O., Department of Animal Sciences, Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel
Low-energy laser irradiation enhances de novo protein synthesis via its effects on translation-regulatory proteins in skeletal muscle myoblasts
Low-energy laser irradiation (LELI) drives quiescent skeletal muscle satellite cells into the cell cycle and enhances their proliferation, thereby promoting skeletal muscle regeneration. Ongoing protein synthesis is a prerequisite for these processes. Here, we studied the signaling pathways involved in the LELI regulation of protein synthesis. High levels of labeled [35S]methionine incorporation were detected in LELI cells as early as 20 min after irradiation, suggesting translation of pre-existing mRNAs. Induced levels of protein synthesis were detected up until 8 h after LELI implying a role for LELI in de novo protein synthesis. Elevated levels of cyclin D1, associated with augmented phosphorylation of the eukaryotic initiation factor 4E (eIF4E) and its inhibitory binding protein PHAS-I, suggested the involvement of LELI in the initiation steps of protein translation. In the presence of the MEK inhibitor, PD98059, eIF4E phosphorylation was abolished and levels of cyclin D1 were dramatically reduced. The LELI-induced PHAS-I phosphorylation was abolished after preincubation with the PI3K inhibitor, Wortmannin. Concomitantly, LELI enhanced Akt phosphorylation, which was attenuated in the presence of Wortmannin. Taken together, these results suggest that LELI induces protein translation via the PI3K/Akt and Ras/Raf/ERK pathways. © 2002 Elsevier Science B.V. All rights reserved.
Scientific Publication
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