
DOI . ORG {
}
Title[redir]:
A cardiac mitochondrial cAMP signaling pathway regulates calcium accumulation, permeability transition and cell death | Cell Death & Disease
Description:
Although cardiac cytosolic cyclic 3′,5′-adenosine monophosphate (cAMP) regulates multiple processes, such as beating, contractility, metabolism and apoptosis, little is known yet on the role of this second messenger within cardiac mitochondria. Using cellular and subcellular approaches, we demonstrate here the local expression of several actors of cAMP signaling within cardiac mitochondria, namely a truncated form of soluble AC (sACt) and the exchange protein directly activated by cAMP 1 (Epac1), and show a protective role for sACt against cell death, apoptosis as well as necrosis in primary cardiomyocytes. Upon stimulation with bicarbonate (HCO3−) and Ca2+, sACt produces cAMP, which in turn stimulates oxygen consumption, increases the mitochondrial membrane potential (ΔΨm) and ATP production. cAMP is rate limiting for matrix Ca2+ entry via Epac1 and the mitochondrial calcium uniporter and, as a consequence, prevents mitochondrial permeability transition (MPT). The mitochondrial cAMP effects involve neither protein kinase A, Epac2 nor the mitochondrial Na+/Ca2+ exchanger. In addition, in mitochondria isolated from failing rat hearts, stimulation of the mitochondrial cAMP pathway by HCO3− rescued the sensitization of mitochondria to Ca2+-induced MPT. Thus, our study identifies a link between mitochondrial cAMP, mitochondrial metabolism and cell death in the heart, which is independent of cytosolic cAMP signaling. Our results might have implications for therapeutic prevention of cell death in cardiac pathologies.
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Keywords {🔍}
mitochondrial, camp, mitochondria, pubmed, article, cell, epac, google, scholar, cas, hco, death, sac, figure, cardiomyocytes, δψm, mpt, isolated, cardiac, heart, figures, shown, rat, neonatal, induced, central, sact, protein, control, signaling, pathway, production, nature, cells, presence, experiments, usa, mcu, versus, effect, supplementary, sensor, measured, swelling, cef, membrane, effects, cyclase, inhibitor, calcium,
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open-access journal published nature publishing group nature portfolio animal research privacy policy dimensional-guided m-mode echocardiography china scholarship council pcdna-4mt-d3-cpv vector advertising nature 1998 nature thermo scientific pcdna-4mt-epac-sh187 vector social media east biosciences author information authors voltage-dependent anion channel mitochondrial camp/sact/epac1/mcu pathway 0/ reprints enzyme-linked immunosorbent assay open 4mt-epac-sh187 camp sensor peroxidase-conjugated secondary antibody dna double-strand sequencing laminin-coated culture dishes oxygen-sensitive phosphorescent dye camp-binding protein epac bicarbonate-sensitive adenylyl cyclase author correspondence tumor necrosis factor-α previously published sensors mitochondrial na+/ca2+ exchanger camp-dependent protein kinase 4mt-epac-sh187 exposed apoptosis/necrosis detection kit bravo-san pedro jm 49 acin-perez l-type ca2+ channels adenoviruses encoding β-galactosidase mitochondrial-targeting sequence 4mt 4mt-epac-sh187 adenoviruses mitochondrial calcium uniporter soluble adenylyl cyclase 'soluble' adenylyl cyclase complex i-driven respiration permissions adenoviruses encoding epac-sh187 membrane-permeant camp analog central control point mitochondria appeared round-shaped
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headline:A cardiac mitochondrial cAMP signaling pathway regulates calcium accumulation, permeability transition and cell death
description:Although cardiac cytosolic cyclic 3â²,5â²-adenosine monophosphate (cAMP) regulates multiple processes, such as beating, contractility, metabolism and apoptosis, little is known yet on the role of this second messenger within cardiac mitochondria. Using cellular and subcellular approaches, we demonstrate here the local expression of several actors of cAMP signaling within cardiac mitochondria, namely a truncated form of soluble AC (sACt) and the exchange protein directly activated by cAMP 1 (Epac1), and show a protective role for sACt against cell death, apoptosis as well as necrosis in primary cardiomyocytes. Upon stimulation with bicarbonate (HCO3â) and Ca2+, sACt produces cAMP, which in turn stimulates oxygen consumption, increases the mitochondrial membrane potential (ÎΨm) and ATP production. cAMP is rate limiting for matrix Ca2+ entry via Epac1 and the mitochondrial calcium uniporter and, as a consequence, prevents mitochondrial permeability transition (MPT). The mitochondrial cAMP effects involve neither protein kinase A, Epac2 nor the mitochondrial Na+/Ca2+ exchanger. In addition, in mitochondria isolated from failing rat hearts, stimulation of the mitochondrial cAMP pathway by HCO3â rescued the sensitization of mitochondria to Ca2+-induced MPT. Thus, our study identifies a link between mitochondrial cAMP, mitochondrial metabolism and cell death in the heart, which is independent of cytosolic cAMP signaling. Our results might have implications for therapeutic prevention of cell death in cardiac pathologies.
datePublished:2016-04-21T00:00:00Z
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Cardiovascular diseases
Cell death
Cell signalling
Life Sciences
general
Biochemistry
Cell Biology
Immunology
Cell Culture
Antibodies
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headline:A cardiac mitochondrial cAMP signaling pathway regulates calcium accumulation, permeability transition and cell death
description:Although cardiac cytosolic cyclic 3â²,5â²-adenosine monophosphate (cAMP) regulates multiple processes, such as beating, contractility, metabolism and apoptosis, little is known yet on the role of this second messenger within cardiac mitochondria. Using cellular and subcellular approaches, we demonstrate here the local expression of several actors of cAMP signaling within cardiac mitochondria, namely a truncated form of soluble AC (sACt) and the exchange protein directly activated by cAMP 1 (Epac1), and show a protective role for sACt against cell death, apoptosis as well as necrosis in primary cardiomyocytes. Upon stimulation with bicarbonate (HCO3â) and Ca2+, sACt produces cAMP, which in turn stimulates oxygen consumption, increases the mitochondrial membrane potential (ÎΨm) and ATP production. cAMP is rate limiting for matrix Ca2+ entry via Epac1 and the mitochondrial calcium uniporter and, as a consequence, prevents mitochondrial permeability transition (MPT). The mitochondrial cAMP effects involve neither protein kinase A, Epac2 nor the mitochondrial Na+/Ca2+ exchanger. In addition, in mitochondria isolated from failing rat hearts, stimulation of the mitochondrial cAMP pathway by HCO3â rescued the sensitization of mitochondria to Ca2+-induced MPT. Thus, our study identifies a link between mitochondrial cAMP, mitochondrial metabolism and cell death in the heart, which is independent of cytosolic cAMP signaling. Our results might have implications for therapeutic prevention of cell death in cardiac pathologies.
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type:Organization
name:G Vandecasteele
affiliation:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay
address:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
type:PostalAddress
type:Organization
name:R Fischmeister
affiliation:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay
address:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
type:PostalAddress
type:Organization
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay
address:
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
type:PostalAddress
type:Organization
name:C Brenner
affiliation:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay
address:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
type:PostalAddress
type:Organization
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay
address:
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
type:PostalAddress
type:Organization
email:[email protected]
PostalAddress:
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM I2MC, UMR 1048, Université Paul Sabatier, Toulouse, France
name:INSERM I2MC, UMR 1048, Université Paul Sabatier, Toulouse, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:INSERM UMR-S 1180, Faculté de Pharmacie, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
name:UMSâIPSIT, Université Paris-Sud, Université Paris-Saclay, Châtenay-Malabry, France
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