A stereochemical investigation of the hydrolysis of cyclic AMP and the (<i>S</i>p)-and (<i>R</i>p)-diastereoisomers of adenosine cyclic 3′:5′-phosphorothioate by bovine heart and baker's-yeast cyclic AMP phosphodiesterases

Jarvest, Richard L.; Lowe, Gordoǹ; Baraniak, Janina; Stec, Wojciech J.

doi:10.1042/bj2030461

Cited by 59 publications

(16 citation statements)

References 17 publications

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“…As depicted in Fig. 9a, RpcAMP-S could almost eliminate the inhibitory effect the cAMP analogue SpcAMP-S (200 PM) which is a known PKA activator [20]. This further substantiate our assumption that the inhibition of the IL-2 induced CD69 expression is due to the action of CAMP through PKA activity.…”

Section: Il-2 Induce Expression Of Cd69 On Ys T Cells Both In the Presupporting

confidence: 61%

Selective activation of resting human γδ T lymphocytes by interleukin‐2

et al. 1993

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In rheumatoid arthritis and other inflammatory diseases we and others have found that gamma delta T cells express activation antigens, suggesting that they are involved in the pathogenesis of these disorders. In this study we have stimulated peripheral blood mononuclear cells from normal donors with recombinant interleukin-2 (rIL-2) to see whether such a stimulus alone could activate gamma delta T cells. Short-term exposure (24-96 h) to rIL-2 selectively stimulated the gamma delta but not the alpha beta T cells to express activation antigens (CD69, CD25 and HLA-DR). Long-term culture (2 weeks) in rIL-2-containing medium caused a selective increase in the proportion of the gamma delta T cells and a corresponding reduction of the fraction of alpha beta T cells. Limiting dilution analysis revealed that approximately 1/60 of the gamma delta T cells responded to IL-2 in contrast to only 1/250 of the alpha beta T cells. Comparison of the expression of the IL-2 receptor (IL-2R) alpha and beta chains showed that there was a similar expression of the alpha chain on gamma delta and alpha beta T cells whereas the relative density of the beta chain was more than twice as high on gamma delta T cells. Both the IL-2-induced proliferation of gamma delta T cells and the expression of activation antigens on these cells could be inhibited by an anti-IL-2R beta monoclonal antibody (mAb) but not by an anti-IL-2R alpha mAb. Expression of CD69 on gamma delta T cells was dependent neither on the presence of B cells, monocytes, nor alpha beta T cells. Finally, we found that the IL-2-induced expression of CD69 was inhibited by activation of cAMP-dependent protein kinase and by inhibition of the Src-family of the tyrosine protein kinase, but not by inhibition of protein kinase C or by activation of the CD45 associated tyrosine phosphatase. The ability of gamma delta T cells to be activated by IL-2 is a feature which they have in common with natural killer cells. Moreover, it may be possible that the expression of activation antigens on gamma delta T cells in inflammatory diseases is an epiphenomenon secondary to IL-2 produced by activated alpha beta T cells.

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Section: Il-2 Induce Expression Of Cd69 On Ys T Cells Both In the Presupporting

confidence: 61%

Selective activation of resting human γδ T lymphocytes by interleukin‐2

et al. 1993

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“…2). This hypothesis is in agreement with elegant biochemical studies and mechanistic interpretations derived from early studies using H 218 O and cN analogs (Burgers et al 1979;Goldberg et al 1980;Jarvest et al 1982). For PDE5, the rate-limiting step of catalysisn has been determined to be the hydrolytic reaction (Morris, Z., Francis, S., Corbin, J., unpublished results).…”

Section: Factors That Provide For Catalysis and Inhibitor Actionsupporting

confidence: 75%

Cyclic GMP-Hydrolyzing Phosphodiesterases

Francis

Corbin

Bischoff

2009

Handbook of Experimental Pharmacology

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“…Rp-cAMPS is a distereomer of an analogue of natural cAMP which binds to the regulatory subunit of both type I and type H cAMPdependent protein kinase without dissociating the catalytic subunit (41). Rp-cAMPS is also a poor substrate for several phosphodiesterases (42). In rat hepatocytes, Rp-cAMPS inhibited glucagon-induced glycogenolysis, a cAMP-mediated effect (43 involved in glucagon stimulation of the exchanger.…”

Section: Discussionmentioning

confidence: 99%

Effect of glucagon on intracellular pH regulation in isolated rat hepatocyte couplets.

Alvaro¹,

Guardia²,

Bini³

et al. 1995

J. Clin. Invest.

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To elucidate mechanisms of glucagon-induced bicarbonaterich choleresis, we investigated the effect of glucagon on ion transport processes involved in the regulation of intracellular pH (pH1) in isolated rat hepatocyte couplets. It was found that glucagon (200 nM), without influencing resting pH1, significantly stimulates the Cl-/HCO3 exchange activity.The effect of glucagon was associated with a sevenfold increase in cAMP levels in rat hepatocytes. The activity of the Cl-/HCO3-exchanger was also stimulated by DBcAMP + forskolin. The effect of glucagon on the Cl-/HCO3 exchange was individually blocked by two specific and selective inhibitors of protein kinase A, uM) and H-89 (30 ,uM), the latter having no influence on the glucagon-induced cAMP accumulation in isolated rat hepatocytes. The Cl -channel blocker, NPPB (10 pmM), showed no effect on either the basal or the glucagon-stimulated Cl-/ HCO3 exchange. In contrast, the protein kinase C agonist, PMA (10 jpM), completely blocked the glucagon stimulation of the C1-/HCO3 exchange; however, this effect was achieved through a significant inhibition of the glucagonstimulated cAMP accumulation in rat hepatocytes. Colchicine pretreatment inhibited the basal as well as the glucagon-stimulated Cl-/HCO3 exchange activity. The Na+/H+ exchanger was unaffected by glucagon either at basal pH1 or at acid pH, values. In contrast, glucagon, at basal pH1, stimulated the Na+-HCO-symport. The main findings of this study indicate that glucagon, through the cAMP-dependent protein kinase A pathway, stimulates the activity of the Cl-/HCO3 exchanger in isolated rat hepatocyte couplets, a mechanism which could account for the in vivo induced bicarbonate-rich choleresis. (J. Clin. Invest. 1995.

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A stereochemical investigation of the hydrolysis of cyclic AMP and the (Sp)-and (Rp)-diastereoisomers of adenosine cyclic 3′:5′-phosphorothioate by bovine heart and baker's-yeast cyclic AMP phosphodiesterases

Cited by 59 publications

References 17 publications

Selective activation of resting human γδ T lymphocytes by interleukin‐2

Selective activation of resting human γδ T lymphocytes by interleukin‐2

Cyclic GMP-Hydrolyzing Phosphodiesterases

Effect of glucagon on intracellular pH regulation in isolated rat hepatocyte couplets.

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