scholarly journals Soluble adenylyl cyclase‐mediated cAMP signaling and the putative role of PKA and EPAC in cerebral mitochondrial function

2019 ◽  
Vol 97 (8) ◽  
pp. 1018-1038 ◽  
Author(s):  
Emil Jakobsen ◽  
Sofie C. Lange ◽  
Lasse K. Bak
Keyword(s):  
Adenylyl Cyclase ◽  
Mitochondrial Function ◽  
Camp Signaling ◽  
Soluble Adenylyl Cyclase ◽  
Putative Role

scholarly journals cAMP and Mitochondria

Physiology ◽  
2013 ◽  
Vol 28 (3) ◽  
pp. 199-209 ◽  
Author(s):  
Federica Valsecchi ◽  
Lavoisier S. Ramos-Espiritu ◽  
Jochen Buck ◽  
Lonny R. Levin ◽  
Giovanni Manfredi
Keyword(s):  
Protein Phosphorylation ◽  
Adenylyl Cyclase ◽  
Regulatory Mechanism ◽  
Mitochondrial Proteins ◽  
Camp Signaling ◽  
Metabolic Adaptation ◽  
Mitochondrial Bioenergetics ◽  
Soluble Adenylyl Cyclase

Phosphorylation of mitochondrial proteins has emerged as a major regulatory mechanism for metabolic adaptation. cAMP signaling and PKA phosphorylation of mitochondrial proteins have just started to be investigated, and the presence of cAMP-generating enzymes and PKA inside mitochondria is still controversial. Here, we discuss the role of cAMP in regulating mitochondrial bioenergetics through protein phosphorylation and the evidence for soluble adenylyl cyclase as the source of cAMP inside mitochondria.

Increased levels of calcium-sensitive adenylyl cyclase subtypes in the limbic system of alcoholics: evidence for a specific role of cAMP signaling in the human addictive brain

2001 ◽  
Vol 895 (1-2) ◽  
pp. 233-237 ◽  
Author(s):  
Megumi Yamamoto ◽  
Sabine Pohli ◽  
Nuria Durany ◽  
Hiroki Ozawa ◽  
Toshikazu Saito ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Limbic System ◽  
Specific Role ◽  
Camp Signaling

scholarly journals Intracellular cAMP signaling by soluble adenylyl cyclase

2011 ◽  
Vol 79 (12) ◽  
pp. 1277-1288 ◽  
Author(s):  
Martin Tresguerres ◽  
Lonny R. Levin ◽  
Jochen Buck
Keyword(s):  
Adenylyl Cyclase ◽  
Camp Signaling ◽  
Intracellular Camp ◽  
Soluble Adenylyl Cyclase

scholarly journals Spatial resolution of cAMP signaling by soluble adenylyl cyclase

2016 ◽  
Vol 214 (2) ◽  
pp. 125-127 ◽  
Author(s):  
Giusi Caldieri ◽  
Sara Sigismund
Keyword(s):  
Plasma Membrane ◽  
Adenylyl Cyclase ◽  
G Protein ◽  
Spatial Resolution ◽  
Camp Signaling ◽  
Receptor Signaling ◽  
Soluble Adenylyl Cyclase ◽  
Spatial Encoding ◽  
Cell Biol ◽  
G Protein Coupled

G protein–coupled receptor signaling starts at the plasma membrane and continues at endosomal stations. In this issue, Inda et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201512075) show that different forms of adenylyl cyclase are activated at the plasma membrane versus endosomes, providing a rationale for the spatial encoding of cAMP signaling.

scholarly journals Protective role of soluble adenylyl cyclase against reperfusion-induced injury of cardiac cells

2019 ◽  
Vol 1865 (1) ◽  
pp. 252-260 ◽  
Author(s):  
Laura Rinaldi ◽  
Sofya Pozdniakova ◽  
Vignesh Jayarajan ◽  
Christian Troidl ◽  
Yaser Abdallah ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Protective Role ◽  
Cardiac Cells ◽  
Soluble Adenylyl Cyclase

scholarly journals The role of soluble adenylyl cyclase in neurite outgrowth

2014 ◽  
Vol 1842 (12) ◽  
pp. 2561-2568 ◽  
Author(s):  
Travis L. Stiles ◽  
Michael S. Kapiloff ◽  
Jeffrey L. Goldberg
Keyword(s):  
Adenylyl Cyclase ◽  
Neurite Outgrowth ◽  
Soluble Adenylyl Cyclase

scholarly journals Effect of Soluble Adenylyl Cyclase (ADCY10) Inhibitors on the LH-Stimulated cAMP Synthesis in Mltc-1 Leydig Cell Line

2021 ◽  
Vol 22 (9) ◽  
pp. 4641
Author(s):  
Thi Mong Diep Nguyen ◽  
Laura Filliatreau ◽  
Danièle Klett ◽  
Nong Van Hai ◽  
Nguyen Thuy Duong ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Leydig Cells ◽  
Intracellular Camp ◽  
Camp Accumulation ◽  
Adenylyl Cyclases ◽  
High Concentration ◽  
Soluble Adenylyl Cyclase ◽  
Bicarbonate Ions ◽  
Intracellular Camp Accumulation

In contrast to all transmembrane adenylyl cyclases except ADCY9, the cytosolic soluble adenylyl cyclase (ADCY10) is insensitive to forskolin stimulation and is uniquely modulated by calcium and bicarbonate ions. In the present paper, we focus on ADCY10 localization and a kinetic analysis of intracellular cAMP accumulation in response to human LH in the absence or presence of four different ADCY10 inhibitors (KH7, LRE1, 2-CE and 4-CE) in MTLC-1 cells. ADCY10 was immuno-detected in the cytoplasm of MLTC-1 cells and all four inhibitors were found to inhibit LH-stimulated cAMP accumulation and progesterone level in MLTC-1 and testosterone level primary Leydig cells. Interestingly, similar inhibitions were also evidenced in mouse testicular Leydig cells. In contrast, the tmAC-specific inhibitors ddAdo3′ and ddAdo5′, even at high concentration, exerted weak or no inhibition on cAMP accumulation, suggesting an important role of ADCY10 relative to tmACs in the MLTC-1 response to LH. The strong synergistic effect of HCO3− under LH stimulation further supports the involvement of ADCY10 in the response to LH.

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