Lipid biosynthesis mediated by the cyclic adenosine monophosphate (cAMP) signaling pathway in Chlorella pyrenoidosa under salt-induced osmotic stress

ABSTRACTThe last decade has seen a shift in the theoretical framework addressing the pathophysiology of psychiatric disorders. During this period, research endeavors have been directed toward investigating the biochemical mechanisms involved in the transduction of information from the cell surface to the cell interior. The emerging picture, supported by growing evidence, is that in addition to neurotransmitters and their receptors, various signal transduction pathways may be linked to the pathophysiology of major psychiatric disorders. In this review, the role of one such pathway—the cyclic adenosine monophosphate (cAMP) signaling pathway—will be highlighted. We review data suggesting the involvement of the upstream and downstream components of this system in the pathophysiology of psychiatric disorders.

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Argania Spinosa Fruit Shell Extract-Induced Melanogenesis via cAMP Signaling Pathway Activation

International Journal of Molecular Sciences ◽

10.3390/ijms21072539 ◽

2020 ◽

Vol 21 (7) ◽

pp. 2539 ◽

Cited By ~ 2

Author(s):

Rachida Makbal ◽

Myra O. Villareal ◽

Chemseddoha Gadhi ◽

Abdellatif Hafidi ◽

Hiroko Isoda

Keyword(s):

Signaling Pathway ◽

Press Cake ◽

Ethanol Extract ◽

Adenosine Monophosphate ◽

Camp Signaling ◽

Melanin Content ◽

Argania Spinosa ◽

B16f10 Cells ◽

Camp Signaling Pathway

We have previously reported that argan oil and argan press-cake from the kernels of Argania spinosa have an anti-melanogenesis effect. Here, the effect of argan fruit shell ethanol extract (AFSEE) on melanogenesis in B16F10 cells was determined, and the mechanism underlying its effect was elucidated. The proliferation of AFSEE-treated B16F10 cells was evaluated using the 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide (MTT) assay, while the melanin content was quantified using a spectrophotometric method. The expression of melanogenesis-related proteins was determined by Western blot and real-time PCR, while global gene expression was determined using a DNA microarray. In vitro analysis results showed that the melanin content of B16F10 cells was significantly increased by AFSEE, without cytotoxicity, by increasing the melanogenic enzyme tyrosinase (TRY), tyrosinase related-protein 1 (TRP1), and dopachrome tautomerase (DCT) protein and mRNA expression, as well as upregulating microphthalmia-associated transcription factor (MITF) expression through mitogen-activated protein kinases (MAPKs) extracellular signal-regulated kinase (ERK) and p38, and the cyclic adenosine monophosphate (cAMP) signaling pathway, as indicated by the microarray analysis results. AFSEE’s melanogenesis promotion effect is primarily attributed to its polyphenolic components. In conclusion, AFSEE promotes melanogenesis in B16F10 cells by upregulating the expression of the melanogenic enzymes through the cAMP–MITF signaling pathway.AFSEE may be used as a cosmetics product component to promote melanogenesis, or as a therapeutic against hypopigmentation disorders.

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cAMP-signaling pathway acts in selective synergism with glucose or tolbutamide to increase cytosolic Ca2+ in rat pancreatic beta-cells

Diabetes ◽

10.2337/diabetes.45.3.295 ◽

1996 ◽

Vol 45 (3) ◽

pp. 295-301 ◽

Cited By ~ 8

Author(s):

K. Yaekura ◽

M. Kakei ◽

T. Yada

Keyword(s):

Signaling Pathway ◽

Beta Cells ◽

Pancreatic Beta Cells ◽

Camp Signaling ◽

Camp Signaling Pathway

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Role of cAMP in Double Switch of Glucagon Secretion

Cells ◽

10.3390/cells10040896 ◽

2021 ◽

Vol 10 (4) ◽

pp. 896

Author(s):

Jan Zmazek ◽

Vladimir Grubelnik ◽

Rene Markovič ◽

Marko Marhl

Keyword(s):

Glucose Metabolism ◽

Signaling Pathway ◽

Cell Model ◽

Dominant Role ◽

Glucagon Secretion ◽

Camp Signaling ◽

Independent Manner ◽

Metabolic Switch ◽

Camp Signaling Pathway ◽

Double Switch

Glucose metabolism plays a crucial role in modulating glucagon secretion in pancreatic alpha cells. However, the downstream effects of glucose metabolism and the activated signaling pathways influencing glucagon granule exocytosis are still obscure. We developed a computational alpha cell model, implementing metabolic pathways of glucose and free fatty acids (FFA) catabolism and an intrinsically activated cAMP signaling pathway. According to the model predictions, increased catabolic activity is able to suppress the cAMP signaling pathway, reducing exocytosis in a Ca2+-dependent and Ca2+ independent manner. The effect is synergistic to the pathway involving ATP-dependent closure of KATP channels and consequent reduction of Ca2+. We analyze the contribution of each pathway to glucagon secretion and show that both play decisive roles, providing a kind of “secure double switch”. The cAMP-driven signaling switch plays a dominant role, while the ATP-driven metabolic switch is less favored. The ratio is approximately 60:40, according to the most recent experimental evidence.

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Assessment of cellular mechanisms contributing to cAMP compartmentalization in pulmonary microvascular endothelial cells

AJP Cell Physiology ◽

10.1152/ajpcell.00361.2011 ◽

2012 ◽

Vol 302 (6) ◽

pp. C839-C852 ◽

Cited By ~ 38

Author(s):

Wei P. Feinstein ◽

Bing Zhu ◽

Silas J. Leavesley ◽

Sarah L. Sayner ◽

Thomas C. Rich

Keyword(s):

Endothelial Cells ◽

Adenylyl Cyclase ◽

Signaling Pathway ◽

Camp Signaling ◽

Microvascular Endothelial Cells ◽

Camp Production ◽

Barrier Integrity ◽

Pulmonary Microvascular Endothelial Cells ◽

Camp Signaling Pathway ◽

Microvascular Endothelial

Cyclic AMP signals encode information required to differentially regulate a wide variety of cellular responses; yet it is not well understood how information is encrypted within these signals. An emerging concept is that compartmentalization underlies specificity within the cAMP signaling pathway. This concept is based on a series of observations indicating that cAMP levels are distinct in different regions of the cell. One such observation is that cAMP production at the plasma membrane increases pulmonary microvascular endothelial barrier integrity, whereas cAMP production in the cytosol disrupts barrier integrity. To better understand how cAMP signals might be compartmentalized, we have developed mathematical models in which cellular geometry as well as total adenylyl cyclase and phosphodiesterase activities were constrained to approximate values measured in pulmonary microvascular endothelial cells. These simulations suggest that the subcellular localizations of adenylyl cyclase and phosphodiesterase activities are by themselves insufficient to generate physiologically relevant cAMP gradients. Thus, the assembly of adenylyl cyclase, phosphodiesterase, and protein kinase A onto protein scaffolds is by itself unlikely to ensure signal specificity. Rather, our simulations suggest that reductions in the effective cAMP diffusion coefficient may facilitate the formation of substantial cAMP gradients. We conclude that reductions in the effective rate of cAMP diffusion due to buffers, structural impediments, and local changes in viscosity greatly facilitate the ability of signaling complexes to impart specificity within the cAMP signaling pathway.

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Increased Rho-kinase-mediated prostate contractions associated with impairment of β-adrenergic-cAMP-signaling pathway by chronic nitric oxide deficiency

European Journal of Pharmacology ◽

10.1016/j.ejphar.2015.03.057 ◽

2015 ◽

Vol 758 ◽

pp. 24-30 ◽

Cited By ~ 4

Author(s):

Fabiano Beraldi Calmasini ◽

Luiz Osório Silveira Leiria ◽

Marcos José Alves ◽

Fernando Ricardo Báu ◽

Eduardo Costa Alexandre ◽

...

Keyword(s):

Nitric Oxide ◽

Signaling Pathway ◽

Rho Kinase ◽

Camp Signaling ◽

Camp Signaling Pathway ◽

Nitric Oxide Deficiency

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ChemInform Abstract: Ansellone A (I), a Sesterterpenoid Isolated from the Nudibranch Cadlina luteromarginata and the Sponge Phorbas sp., Activates the cAMP Signaling Pathway.

ChemInform ◽

10.1002/chin.201048185 ◽

2010 ◽

Vol 41 (48) ◽

pp. no-no

Author(s):

Julie Daoust ◽

Angelo Fontana ◽

Catherine E. Merchant ◽

Nicole J. de Voogd ◽

Brian O. Patrick ◽

...

Keyword(s):

Signaling Pathway ◽

Camp Signaling ◽

Camp Signaling Pathway

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The nucleoporin RanBP2 tethers the cAMP effector Epac1 and inhibits its catalytic activity

The Journal of Cell Biology ◽

10.1083/jcb.201011126 ◽

2011 ◽

Vol 193 (6) ◽

pp. 1009-1020 ◽

Cited By ~ 33

Author(s):

Martijn Gloerich ◽

Marjolein J. Vliem ◽

Esther Prummel ◽

Lars A.T. Meijer ◽

Marije G.A. Rensen ◽

...

Keyword(s):

Catalytic Activity ◽

Cyclic Adenosine Monophosphate ◽

Adenosine Monophosphate ◽

Negative Regulator ◽

Camp Signaling ◽

Nuclear Pore ◽

Nucleotide Exchange ◽

Nucleotide Exchange Factor ◽

Wide Range

Cyclic adenosine monophosphate (cAMP) is a second messenger that relays a wide range of hormone responses. In this paper, we demonstrate that the nuclear pore component RanBP2 acts as a negative regulator of cAMP signaling through Epac1, a cAMP-regulated guanine nucleotide exchange factor for Rap. We show that Epac1 directly interacts with the zinc fingers (ZNFs) of RanBP2, tethering Epac1 to the nuclear pore complex (NPC). RanBP2 inhibits the catalytic activity of Epac1 in vitro by binding to its catalytic CDC25 homology domain. Accordingly, cellular depletion of RanBP2 releases Epac1 from the NPC and enhances cAMP-induced Rap activation and cell adhesion. Epac1 also is released upon phosphorylation of the ZNFs of RanBP2, demonstrating that the interaction can be regulated by posttranslational modification. These results reveal a novel mechanism of Epac1 regulation and elucidate an unexpected link between the NPC and cAMP signaling.

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