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Des-acyl ghrelin ha...
Des-acyl ghrelin has specific binding sites and different metabolic effects from ghrelin in cardiomyocytes
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Lear, PV (author)
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- Iglesias, MJ (author)
- Karolinska Institutet
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Feijoo-Bandin, S (author)
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Rodriguez-Penas, D (author)
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Mosquera-Leal, A (author)
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Garcia-Rua, V (author)
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Gualillo, O (author)
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Ghe, C (author)
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Arnoletti, E (author)
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Muccioli, G (author)
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Dieguez, C (author)
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Gonzalez-Juanatey, JR (author)
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Lago, F (author)
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(creator_code:org_t)
- 2010-04-21
- 2010
- English.
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In: Endocrinology. - : The Endocrine Society. - 1945-7170 .- 0013-7227. ; 151:7, s. 3286-3298
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Abstract
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- The current study aimed to compare the effects of the peptide hormone ghrelin and des-G, its unacylated isoform, on glucose and fatty acid uptake and to identify des-G-specific binding sites in cardiomyocytes. In the murine HL-1 adult cardiomyocyte line, ghrelin and des-G had opposing metabolic effects: des-G increased medium-chain fatty acid uptake (BODIPY fluorescence intensity), whereas neither ghrelin alone nor in combination with des-G did so. Ghrelin inhibited the increase in glucose uptake normally induced by insulin (rate of 2-[3H]deoxy-d-glucose incorporation), but des-G did not; des-G was also able to partially reverse the inhibitory effect of ghrelin. In HL-1 cells and primary cultures of neonatal rat cardiomyocytes, des-G but not ghrelin increased insulin-induced translocation of glucose transporter-4 from nuclear to cytoplasmic compartments (immunohistochemistry and quantitative confocal analysis). AKT was phosphorylated by insulin but not affected by ghrelin or des-G, whereas neither AMP-activated protein kinase nor phosphatase and tensin homolog deleted from chromosome 10 was phosphorylated by any treatments. HL-1 and primary-cultured mouse and rat cardiomyocytes each possessed two independent specific binding sites for des-G not recognized by ghrelin (radioreceptor assays). Neither ghrelin nor des-G affected viability (dimethylthiazol diphenyltetrazolium bromide assays), whereas both isoforms were equally protective against apoptosis. Therefore, in cardiomyocytes, des-G binds to specific receptors and has effects on glucose and medium-chain fatty acid uptake that are distinct from those of ghrelin. Real-time PCR indicated that expression levels of ghrelin O-acyltransferase RNA were comparable between HL-1 cells, human myocardial tissue, and human and murine stomach tissue, indicating the possibility of des-G conversion to ghrelin within our model.
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- By the author/editor
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Lear, PV
-
Iglesias, MJ
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Feijoo-Bandin, S
-
Rodriguez-Penas, ...
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Mosquera-Leal, A
-
Garcia-Rua, V
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show more...
-
Gualillo, O
-
Ghe, C
-
Arnoletti, E
-
Muccioli, G
-
Dieguez, C
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Gonzalez-Juanate ...
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Lago, F
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show less...
- Articles in the publication
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Endocrinology
- By the university
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Karolinska Institutet