Relationship of cyclic AMP to secretin stimulation of the pancreas

1973 ◽  
Vol 14 (2) ◽  
pp. 172-176 ◽  
Author(s):  
Ronald K. Tompkins ◽  
Stephen L. Kuchenbecker
Keyword(s):  
Cyclic Amp ◽  
Secretin Stimulation ◽  
Relationship Of ◽  
Stimulation Of

scholarly journals MEDIATION OF IMMUNOLOGIC DISCHARGE OF LYSOSOMAL ENZYMES FROM HUMAN NEUTROPHILS BY GUANOSINE 3',5'-MONOPHOSPHATE

1974 ◽  
Vol 140 (1) ◽  
pp. 225-238 ◽  
Author(s):  
L. J. Ignarro ◽  
W. J. George
Keyword(s):  
Cyclic Amp ◽  
Cyclic Gmp ◽  
Lysosomal Enzymes ◽  
Extracellular Calcium ◽  
Human Neutrophils ◽  
Enzyme Release ◽  
Dibutyryl Cyclic Amp ◽  
Relationship Of ◽  
The Relationship ◽  
Stimulation Of

The purpose of this investigation was to elucidate the relationship of cyclic GMP and calcium to the immunologic discharge of lysosomal enzymes from purified human neutrophils. Contact of neutrophils with a variety of immunologic stimuli, including zymosan particles treated with either normal or rheumatoid arthritic (RA) serum, heat-aggregated (agg) IgG, particulate and immobilized agg IgG each treated with RA serum, and zymosan-treated serum, provoked the discharge of ß-glucuronidase, but not cytoplasmic lactate dehydrogenase, and stimulated the accumulation of cyclic GMP. Both enzyme release and elevation of cyclic GMP levels required the presence of extracellular calcium as neither cellular event proceeded in its absence. Cholinergic enhancement of the immunologic secretion of ß-glucuronidase from neutrophils by acetylcholine was associated with a concomitant accumulation of cyclic GMP. These actions of acetylcholine on neutrophils did not proceed in the absence of extracellular calcium. Whereas the concentrations of cyclic GMP in neutrophils were elevated by both immune reactants and a combination of the latter and acetylcholine, cyclic AMP levels remained unaltered. Thus, cyclic GMP, but not cyclic AMP, was associated with the immunologic and pharmacologic discharge of lysosomal enzymes from neutrophils. Contrariwise, cyclic AMP, but not cyclic GMP, was associated with inhibition of lysosomal enzyme release. For example, dibutyryl cyclic AMP and epinephrine inhibited the release of ß-glucuronidase from neutrophils that was elicited by each of the immune reactants tested. Moreover, cyclic AMP levels in the cells were elevated markedly in every instance that enzyme discharge was inhibited by epinephrine. Epinephrine did not alter the neutrophil concentrations of cyclic GMP at times when those of cyclic AMP were elevated. The data in this report constitute partial evidence that the immunologic discharge of lysosomal enzymes from human neutrophils is mediated or signaled by intracellular cyclic GMP and that calcium is linked to this stimulation of enzyme secretion.

Stimulation of cyclic AMP formation and nerve electrical activity by octopamine in the terminal abdominal ganglion of the female gypsy moth Lymantria dispar

2006 ◽  
Vol 1071 (1) ◽  
pp. 63-74 ◽  
Author(s):  
Maria C. Olianas ◽  
Paolo Solari ◽  
Luciana Garau ◽  
Anna Liscia ◽  
Roberto Crnjar ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Electrical Activity ◽  
Gypsy Moth ◽  
Lymantria Dispar ◽  
Abdominal Ganglion ◽  
Stimulation Of

scholarly journals Interactional mechanisms of Paenibacillus polymyxa SC2 and pepper (Capsicum annuum L.) suggested by transcriptomics

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Hu Liu ◽  
Yufei Li ◽  
Ke Ge ◽  
Binghai Du ◽  
Kai Liu ◽  
...  
Keyword(s):  
Capsicum Annuum ◽  
Biofilm Formation ◽  
Rhizosphere Soil ◽  
Paenibacillus Polymyxa ◽  
Systemic Resistance ◽  
Expression Of Genes ◽  
Transcription Factor Genes ◽  
Transcription Regulators ◽  
Relationship Of ◽  
Stimulation Of

Abstract Background Paenibacillus polymyxa SC2, a bacterium isolated from the rhizosphere soil of pepper (Capsicum annuum L.), promotes growth and biocontrol of pepper. However, the mechanisms of interaction between P. polymyxa SC2 and pepper have not yet been elucidated. This study aimed to investigate the interactional relationship of P. polymyxa SC2 and pepper using transcriptomics. Results P. polymyxa SC2 promotes growth of pepper stems and leaves in pot experiments in the greenhouse. Under interaction conditions, peppers stimulate the expression of genes related to quorum sensing, chemotaxis, and biofilm formation in P. polymyxa SC2. Peppers induced the expression of polymyxin and fusaricidin biosynthesis genes in P. polymyxa SC2, and these genes were up-regulated 2.93- to 6.13-fold and 2.77- to 7.88-fold, respectively. Under the stimulation of medium which has been used to culture pepper, the bacteriostatic diameter of P. polymyxa SC2 against Xanthomonas citri increased significantly. Concurrently, under the stimulation of P. polymyxa SC2, expression of transcription factor genes WRKY2 and WRKY40 in pepper was up-regulated 1.17-fold and 3.5-fold, respectively. Conclusions Through the interaction with pepper, the ability of P. polymyxa SC2 to inhibit pathogens was enhanced. P. polymyxa SC2 also induces systemic resistance in pepper by stimulating expression of corresponding transcription regulators. Furthermore, pepper has effects on chemotaxis and biofilm formation of P. polymyxa SC2. This study provides a basis for studying interactional mechanisms of P. polymyxa SC2 and pepper.

scholarly journals Interactions between adenylate cyclase and the yeast GTPase-activating protein IRA1.

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Adenylate Cyclase System ◽  
Gtpase Activating Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Strong Candidate ◽  
Sepharose 4B ◽  
Stimulation Of ◽  
Cyclic Amp Synthesis

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.

scholarly journals Stimulation of Cyclic AMP Formation by Pituitary Adenylate Cyclase-Activating Polypeptide Is Attenuated by Glutamate in Rat Brain Slices

1995 ◽  
Vol 67 (4) ◽  
pp. 399-402
Author(s):  
Kaoru Kondo ◽  
Hitoshi Hashimoto ◽  
Kazuko Sakata ◽  
Hiroshi Saga ◽  
Jun-ichi Kitanaka ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Rat Brain ◽  
Brain Slices ◽  
Pituitary Adenylate Cyclase ◽  
Stimulation Of
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