dc.contributor.author |
Katona D |
|
dc.contributor.author |
Rajki, Anikó |
|
dc.contributor.author |
Di Benedetto G |
|
dc.contributor.author |
Pozzan T |
|
dc.contributor.author |
Spät, András |
|
dc.date.accessioned |
2017-06-08T07:27:46Z |
|
dc.date.available |
2017-06-08T07:27:46Z |
|
dc.date.issued |
2015 |
|
dc.identifier |
84929643251 |
|
dc.identifier.citation |
pagination=196-204;
journalVolume=412;
journalTitle=MOLECULAR AND CELLULAR ENDOCRINOLOGY; |
|
dc.identifier.uri |
http://repo.lib.semmelweis.hu//handle/123456789/2793 |
|
dc.identifier.uri |
doi:10.1016/j.mce.2015.05.002 |
|
dc.description.abstract |
Glomerulosa cells secrete aldosterone in response to agonists coupled to Ca2+ increases such as angiotensin II and corticotrophin, coupled to a cAMP dependent pathway. A recently recognized interaction between Ca2+ and cAMP is the Ca2+-induced cAMP formation in the mitochondrial matrix. Here we describe that soluble adenylyl cyclase (sAC) is expressed in H295R adrenocortical cells. Mitochondrial cAMP formation, monitored with a mitochondria-targeted fluorescent sensor (4mtH30), is enhanced by HCO<inf>3</inf> - and the Ca2+ mobilizing agonist angiotensin II. The effect of angiotensin II is inhibited by 2-OHE, an inhibitor of sAC, and by RNA interference of sAC, but enhanced by an inhibitor of phosphodiesterase PDE2A. Heterologous expression of the Ca2+ binding protein S100G within the mitochondrial matrix attenuates angiotensin II-induced mitochondrial cAMP formation. Inhibition and knockdown of sAC significantly reduce angiotensin II-induced aldosterone production. These data provide the first evidence for a cell-specific functional role of mitochondrial cAMP. © 2015 Elsevier Ireland Ltd. |
|
dc.relation.ispartof |
urn:issn:0303-7207 |
|
dc.title |
Calcium-dependent mitochondrial cAMP production enhances aldosterone secretion |
|
dc.type |
Journal Article |
|
dc.date.updated |
2015-11-26T10:09:40Z |
|
dc.language.rfc3066 |
en |
|
dc.identifier.mtmt |
2919568 |
|
dc.contributor.department |
SE/AOK/I/Élettani Intézet |
|
dc.contributor.institution |
Semmelweis Egyetem |
|