Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes

Rocío Foncea; Anita Gálvez; Viviana Pérez; María Paz Morales; Andrea Calixto; Jaime Meléndez; Fabián González-Jara; Guillermo Díaz-Araya; Mario Sapag-Hagar; Peter H. Sugden; Derek Leroith; Sergio Lavandero

doi:10.1006/bbrc.2000.3008

Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes

Rocío Foncea, Anita Gálvez, Viviana Pérez, María Paz Morales, Andrea Calixto, Jaime Meléndez, Fabián González-Jara, Guillermo Díaz-Araya, Mario Sapag-Hagar, Peter H. Sugden, Derek Leroith, Sergio Lavandero

Universidad de Chile

Résultat de recherche › examen par les pairs

37 Citations (Scopus)

Résumé

This study aims to elucidate the signaling pathway for insulin-like growth factor-1 (IGF-1) in cultured neonatal rat cardiomyocytes and particularly the role of IGF-1 in cardiac apoptosis. IGF-1 stimulated polyphosphoinositide turnover, translocation of protein kinase C (PKC) isoforms (α, ε, and δ) from the soluble to the particulate fraction, activation of phospholipid-dependent and Ca²⁺-, phospholipid-dependent PKC, and activation of the extracellular-regulated kinase (ERK). IGF-1 attenuated sorbitol-induced cardiomyocyte viability and nuclear DNA fragmentation. These antiapoptotic effects of IGF-1 were blocked by PD-098059 (an MEK inhibitor) but not by bisindolylmaleimide I (BIM, a specific PKC inhibitor). The ERK pathway may therefore be an important component in the mechanism whereby IGF-1 exerts its antiapoptotic effect on the cardiomyocyte. (C) 2000 Academic Press.

Langue d'origine	English
Pages (de-à)	736-744
Nombre de pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	273
Numéro de publication	2
DOI	https://doi.org/10.1006/bbrc.2000.3008
Statut de publication	Published - juill. 5 2000

Financement

Bailleurs de fonds	Numéro du bailleur de fonds
National Institutes of Health
Comisión Nacional de Investigación Científica y Tecnológica	19980-2063
Fondo Nacional de Ciencia y Tecnología	1980908, 1950452, 296001

ASJC Scopus Subject Areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.2000.3008

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Foncea, R., Gálvez, A., Pérez, V., Morales, M. P., Calixto, A., Meléndez, J., González-Jara, F., Díaz-Araya, G., Sapag-Hagar, M., Sugden, P. H., Leroith, D., & Lavandero, S. (2000). Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes. Biochemical and Biophysical Research Communications, 273(2), 736-744. https://doi.org/10.1006/bbrc.2000.3008

Foncea, R, Gálvez, A, Pérez, V, Morales, MP, Calixto, A, Meléndez, J, González-Jara, F, Díaz-Araya, G, Sapag-Hagar, M, Sugden, PH, Leroith, D & Lavandero, S 2000, 'Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes', Biochemical and Biophysical Research Communications, vol. 273, n° 2, pp. 736-744. https://doi.org/10.1006/bbrc.2000.3008

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title = "Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes",

abstract = "This study aims to elucidate the signaling pathway for insulin-like growth factor-1 (IGF-1) in cultured neonatal rat cardiomyocytes and particularly the role of IGF-1 in cardiac apoptosis. IGF-1 stimulated polyphosphoinositide turnover, translocation of protein kinase C (PKC) isoforms (α, ε, and δ) from the soluble to the particulate fraction, activation of phospholipid-dependent and Ca2+-, phospholipid-dependent PKC, and activation of the extracellular-regulated kinase (ERK). IGF-1 attenuated sorbitol-induced cardiomyocyte viability and nuclear DNA fragmentation. These antiapoptotic effects of IGF-1 were blocked by PD-098059 (an MEK inhibitor) but not by bisindolylmaleimide I (BIM, a specific PKC inhibitor). The ERK pathway may therefore be an important component in the mechanism whereby IGF-1 exerts its antiapoptotic effect on the cardiomyocyte. (C) 2000 Academic Press.",

author = "Roc{\'i}o Foncea and Anita G{\'a}lvez and Viviana P{\'e}rez and Morales, {Mar{\'i}a Paz} and Andrea Calixto and Jaime Mel{\'e}ndez and Fabi{\'a}n Gonz{\'a}lez-Jara and Guillermo D{\'i}az-Araya and Mario Sapag-Hagar and Sugden, {Peter H.} and Derek Leroith and Sergio Lavandero",

note = "Funding Information: We thank Professor C. I. Pogson for help in the preparation of the manuscript. This work was supported in part by Fondo Nacional de Ciencia y Tecnolog{\'i}a (FONDECYT) Grants 1980908 (S.L), 296001 (R.F.), and 1950452 (S.L.) and Cooperaci{\'o}n Internacional NIH– CONICYT Grant 19980-2063 (S.L.). R. Foncea, A. G{\'a}lvez, and F. Gonz{\'a}lez-Jara are recipients of CONICYT fellowships.",

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T1 - Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes

AU - Foncea, Rocío

AU - Gálvez, Anita

AU - Pérez, Viviana

AU - Morales, María Paz

AU - Calixto, Andrea

AU - Meléndez, Jaime

AU - González-Jara, Fabián

AU - Díaz-Araya, Guillermo

AU - Sapag-Hagar, Mario

AU - Sugden, Peter H.

AU - Leroith, Derek

AU - Lavandero, Sergio

N1 - Funding Information: We thank Professor C. I. Pogson for help in the preparation of the manuscript. This work was supported in part by Fondo Nacional de Ciencia y Tecnología (FONDECYT) Grants 1980908 (S.L), 296001 (R.F.), and 1950452 (S.L.) and Cooperación Internacional NIH– CONICYT Grant 19980-2063 (S.L.). R. Foncea, A. Gálvez, and F. González-Jara are recipients of CONICYT fellowships.

PY - 2000/7/5

Y1 - 2000/7/5

N2 - This study aims to elucidate the signaling pathway for insulin-like growth factor-1 (IGF-1) in cultured neonatal rat cardiomyocytes and particularly the role of IGF-1 in cardiac apoptosis. IGF-1 stimulated polyphosphoinositide turnover, translocation of protein kinase C (PKC) isoforms (α, ε, and δ) from the soluble to the particulate fraction, activation of phospholipid-dependent and Ca2+-, phospholipid-dependent PKC, and activation of the extracellular-regulated kinase (ERK). IGF-1 attenuated sorbitol-induced cardiomyocyte viability and nuclear DNA fragmentation. These antiapoptotic effects of IGF-1 were blocked by PD-098059 (an MEK inhibitor) but not by bisindolylmaleimide I (BIM, a specific PKC inhibitor). The ERK pathway may therefore be an important component in the mechanism whereby IGF-1 exerts its antiapoptotic effect on the cardiomyocyte. (C) 2000 Academic Press.

AB - This study aims to elucidate the signaling pathway for insulin-like growth factor-1 (IGF-1) in cultured neonatal rat cardiomyocytes and particularly the role of IGF-1 in cardiac apoptosis. IGF-1 stimulated polyphosphoinositide turnover, translocation of protein kinase C (PKC) isoforms (α, ε, and δ) from the soluble to the particulate fraction, activation of phospholipid-dependent and Ca2+-, phospholipid-dependent PKC, and activation of the extracellular-regulated kinase (ERK). IGF-1 attenuated sorbitol-induced cardiomyocyte viability and nuclear DNA fragmentation. These antiapoptotic effects of IGF-1 were blocked by PD-098059 (an MEK inhibitor) but not by bisindolylmaleimide I (BIM, a specific PKC inhibitor). The ERK pathway may therefore be an important component in the mechanism whereby IGF-1 exerts its antiapoptotic effect on the cardiomyocyte. (C) 2000 Academic Press.

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Extracellular regulated kinase, but not protein kinase C, is an antiapoptotic signal of insulin-like growth factor-1 on cultured cardiac myocytes

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ASJC Scopus Subject Areas

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