Distinctive Properties of Dark Reversion Kinetics between Two Red/Green-Type Cyanobacteriochromes and their Application in the Photoregulation of cAMP Synthesis

2017 ◽  
Vol 93 (3) ◽  
pp. 681-691 ◽  
Author(s):  
Keiji Fushimi ◽  
Gen Enomoto ◽  
Masahiko Ikeuchi ◽  
Rei Narikawa
Keyword(s):  
Camp Synthesis ◽  
Dark Reversion

scholarly journals cAMP induces a rapid and reversible modification of the chemotactic receptor in Dictyostelium discoideum.

1985 ◽  
Vol 100 (3) ◽  
pp. 715-720 ◽  
Author(s):  
C Klein ◽  
J Lubs-Haukeness ◽  
S Simons
Keyword(s):  
Dictyostelium Discoideum ◽  
Concentration Dependence ◽  
Time Course ◽  
Camp Synthesis ◽  
Sds Page ◽  
Reversible Modification ◽  
Camp Receptor ◽  
Camp Stimulation ◽  
Stimulation Of

Stimulation, within 1 min after cAMP stimulation, of aggregation-competent Dictyostelium discoideum amebae was found to cause a rapid (within 1 min) modification of the cell's surface cAMP receptor. The modified receptor migrated on SDS PAGE as a 47,000-mol-wt protein, as opposed to a 45,000-mol-wt protein labeled on unstimulated cells. The length of time this modified receptor could be detected depended upon the strength of the cAMP stimulus: 3-4 min after treatment with 10(-7) M cAMP, cells no longer possessed the 47,000-mol-wt form of the cAMP receptor. Instead, the 45,000-mol-wt form was present. Stimulation of cells with 10(-5) M cAMP, however, resulted in the persistent (over 15 min) expression of the modified receptor. The time course, concentration dependence, and specificity of stimulus for this cAMP-induced shift in the cAMP receptor were found to parallel the cAMP-stimulated phosphorylation of a 47,000-mol-wt protein. In addition, both phenomena were shown to occur in the absence of endogenous cAMP synthesis. The possibility that the cAMP receptor is phosphorylated in response to cAMP stimulation, and the role of this event in cell desensitization, are discussed.

scholarly journals AKAP5 complex facilitates purinergic modulation of vascular L-type Ca2+ channel CaV1.2

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Maria Paz Prada ◽  
Arsalan U. Syed ◽  
Gopireddy R. Reddy ◽  
Miguel Martín-Aragón Baudel ◽  
Víctor A. Flores-Tamez ◽  
...  
Keyword(s):  
Vascular Reactivity ◽  
Vascular Complications ◽  
Channel Activity ◽  
Camp Synthesis ◽  
Anchoring Protein ◽  
Extracellular Glucose ◽  
Elevated Glucose ◽  
Underlying Mechanisms ◽  
Purinergic Modulation ◽  
Human And Mouse

Abstract The L-type Ca2+ channel CaV1.2 is essential for arterial myocyte excitability, gene expression and contraction. Elevations in extracellular glucose (hyperglycemia) potentiate vascular L-type Ca2+ channel via PKA, but the underlying mechanisms are unclear. Here, we find that cAMP synthesis in response to elevated glucose and the selective P2Y11 agonist NF546 is blocked by disruption of A-kinase anchoring protein 5 (AKAP5) function in arterial myocytes. Glucose and NF546-induced potentiation of L-type Ca2+ channels, vasoconstriction and decreased blood flow are prevented in AKAP5 null arterial myocytes/arteries. These responses are nucleated via the AKAP5-dependent clustering of P2Y11/ P2Y11-like receptors, AC5, PKA and CaV1.2 into nanocomplexes at the plasma membrane of human and mouse arterial myocytes. Hence, data reveal an AKAP5 signaling module that regulates L-type Ca2+ channel activity and vascular reactivity upon elevated glucose. This AKAP5-anchored nanocomplex may contribute to vascular complications during diabetic hyperglycemia.

scholarly journals Pharmacological and genetic activation of cAMP synthesis disrupts cholesterol utilization in Mycobacterium tuberculosis

2021 ◽  
Author(s):  
Kaley M. Wilburn ◽  
Christine R. Montague ◽  
Bo Qin ◽  
Ashley K. Woods ◽  
Melissa S. Love ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Adenylyl Cyclase ◽  
Cholesterol Metabolism ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Camp Signaling ◽  
Camp Synthesis ◽  
Pharmacokinetic Properties ◽  
Bacterial Utilization

There is a growing appreciation for the idea that bacterial utilization of host-derived lipids, including cholesterol, supports Mycobacterium tuberculosis (Mtb) pathogenesis. This has generated interest in identifying novel antibiotics that can disrupt cholesterol utilization by Mtb in vivo. Here we identify a novel small molecule agonist (V-59) of the Mtb adenylyl cyclase Rv1625c, which stimulates 3’, 5’-cyclic adenosine monophosphate (cAMP) synthesis and inhibits cholesterol utilization by Mtb. Similarly, using a complementary genetic approach that induces bacterial cAMP synthesis independent of Rv1625c, we demonstrate that inducing cAMP synthesis is sufficient to inhibit cholesterol utilization in Mtb. Although the physiological roles of individual adenylyl cyclase enzymes in Mtb are largely unknown, here we demonstrate that the transmembrane region of Rv1625c is required for cholesterol metabolism. Finally, in this work the pharmacokinetic properties of Rv1625c agonists are optimized, producing an orally-available Rv1625c agonist that impairs Mtb pathogenesis in infected mice. Collectively, this work demonstrates a novel role for Rv1625c and cAMP signaling in controlling cholesterol metabolism in Mtb and establishes that cAMP signaling can be pharmacologically manipulated for the development of new antibiotic strategies.

Agonist-induced polarized trafficking and surface expression of the adenosine 2b receptor in intestinal epithelial cells: role of SNARE proteins

2004 ◽  
Vol 287 (5) ◽  
pp. G1100-G1107 ◽  
Author(s):  
Lixin Wang ◽  
Vasantha Kolachala ◽  
Baljit Walia ◽  
Srividya Balasubramanian ◽  
Randy A. Hall ◽  
...  
Keyword(s):  
Adenosine Receptor ◽  
Intestinal Inflammation ◽  
Apical Membrane ◽  
Snare Proteins ◽  
Cell Fractionation ◽  
Camp Synthesis ◽  
Agonist Stimulation ◽  
A2b Receptor ◽  
In Cells

Adenosine, acting through the A2b receptor, induces vectorial chloride and IL-6 secretion in intestinal epithelia and may play an important role in intestinal inflammation. We have previously shown that apical or basolateral adenosine receptor stimulation results in the recruitment of the A2b receptor to the plasma membrane. In this study, we examined domain specificity of recruitment and the role of soluble N-ethylmaleimide (NEM) attachment receptor (SNARE) proteins in the agonist-mediated recruitment of the A2b receptor to the membrane. The colonic epithelial cell line T84 was used because it only expresses the A2b-subtype adenosine receptor. Cell fractionation, biotinylation, and electron microscopic studies showed that the A2b receptor is intracellular at rest and that apical or basolateral adenosine stimulation resulted in the recruitment of the receptor to the apical membrane. Upon agonist stimulation, the A2b receptor is enriched in the vesicle fraction containing vesicle-associated membrane protein (VAMP)-2. Furthermore, in cells stimulated with apical or basolateral adenosine, we demonstrate a complex consisting of VAMP-2, soluble NEM-sensitive factor attachment protein (SNAP)-23, and A2b receptor that is coimmunoprecipitated in cells stimulated with adenosine within 5 min and is no longer detected within 15 min. Inhibition of trafficking with NEM or nocodazole inhibits cAMP synthesis induced by apical or basolateral adenosine by 98 and 90%, respectively. cAMP synthesis induced by foskolin was not affected, suggesting that generalized signaling is not affected under these conditions. Collectively, our data suggest that 1) the A2b receptor is intracellular at rest; 2) apical or basolateral agonist stimulation induces recruitment of the A2b receptor to the apical membrane; 3) the SNARE proteins, VAMP-2 and SNAP-23, participate in the recruitment of the A2b receptor; and 4) the SNARE-mediated recruitment of the A2b receptor may be required for its signaling.

PROSTAGLANDIN-INDUCED cAMP SYNTHESIS IN PERIPHERAL NERVE

Abstracts ◽  
1978 ◽  
pp. 625
Author(s):  
Peter Kalix
Keyword(s):  
Peripheral Nerve ◽  
Camp Synthesis

scholarly journals Affinity for [3H]Iloprost Binding Sites and cAMP Synthesis Activity of a 3-Oxa-methano Prostaglandin I1 Analog, SM-10906, in Human Platelets and Endothelial Cells

1997 ◽  
Vol 74 (1) ◽  
pp. 37-43
Author(s):  
Takashi Hiroi ◽  
Keiko Maruyama ◽  
Kaoru Hattori ◽  
Toshio Ohnuki ◽  
Takafumi Nagatomo ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Binding Sites ◽  
Human Platelets ◽  
Camp Synthesis ◽  
Synthesis Activity

Effects of ANF on cGMP synthesis in inner medullary collecting duct subsegments of rats

1990 ◽  
Vol 259 (3) ◽  
pp. F535-F538
Author(s):  
K. Ujiie ◽  
H. Nonoguchi ◽  
K. Tomita ◽  
F. Marumo
Keyword(s):  
Atrial Natriuretic Factor ◽  
Collecting Duct ◽  
Target Site ◽  
Cyclic Monophosphate ◽  
Inner Medullary Collecting Duct ◽  
Camp Synthesis ◽  
Target Sites ◽  
Medullary Collecting Duct ◽  
Cgmp Synthesis ◽  
Major Target

The inner medullary collecting duct (IMCD) is thought to be a major target site for atrial natriuretic factor (ANF) action. The IMCD is divided into two subsegments (IMCD1, outer third; and IMCD2,3, inner two-thirds) based on differences in urea and water permeability. IMCD1 has similar characteristics to the outer medullary collecting duct (OMCD). To elucidate whether there are any differences among these segments in ANF actions, we investigated the effects of ANF on guanosine 3',5'-cyclic monophosphate (cGMP) synthesis in IMCD subsegments and the OMCD. We also examined the effects of arginine vasopressin (AVP) on adenosine 3',5'-cyclic monophosphate (cAMP) synthesis. IMCD subsegments (IMCD1,2,3) and OMCD were microdissected; and ANF-stimulated cGMP synthesis and AVP-stimulated cAMP synthesis were measured. cGMP synthesis stimulated by 10(-6) M ANF in IMCD1,2,3 (0.78 +/- 0.15, 0.81 +/- 0.19, 0.62 +/- 0.10 fmol.mm-1 x 3 min-1, mean +/- SE respectively, n = 10-11) was significantly (greater than 20-fold) higher than that in OMCD (0.03 +/- 0.02 fmol.mm-1 x 3 min-1, n = 7), and there was no difference among IMCD subsegments. On the other hand, cAMP synthesis stimulated by 10(-7) M AVP in IMCD subsegments was similar to that in OMCD. We conclude that IMCD is homogenous as a target site of ANF and is clearly distinguished from OMCD. In addition, more than half of ANF-stimulated cGMP synthesis in IMCD are considered to occur in IMCD1, simply because IMCD1 is dominant in population among IMCD subsegments. As target sites of AVP, IMCD subsegments are similar to OMCD.

scholarly journals Phosphorylation of Phytochrome B Inhibits Light-Induced Signaling via Accelerated Dark Reversion in Arabidopsis

2013 ◽  
Vol 25 (2) ◽  
pp. 535-544 ◽  
Author(s):  
Mátyás Medzihradszky ◽  
János Bindics ◽  
Éva Ádám ◽  
András Viczián ◽  
Éva Klement ◽  
...  
Keyword(s):  
Phytochrome B ◽  
Dark Reversion

ON THE PHYSIOLOGICAL SIGNIFICANCE OF DARK REVERSION OF PHYTOCHROME IN THE MUSTARD SEEDLING

1976 ◽  
Vol 23 (1) ◽  
pp. 55-59 ◽  
Author(s):  
H. Oelze-Karow ◽  
E. Scháfer ◽  
H. Mohr
Keyword(s):  
Physiological Significance ◽  
Mustard Seedling ◽  
Dark Reversion
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