Retinoid Treatment of Human Psoriatic Fibroblasts Induces an Increase in Cyclic AMP-Dependent Protein Kinase Activity

Raynaud, Françoise; Leduc, Claire; Anderson, Wayne B.; Évain-Brion, Danièle

doi:10.1111/1523-1747.ep12580448

Cited by 34 publications

(19 citation statements)

References 23 publications

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“…For example, the rapid (2-5 min) inhibitory effect of RA on the increase in cytosolic CAMP-PK activity induced by the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13 acetate does not appear to involve the RARs (Plet et al, 1988). Other studies have established that retinoid treatment of psoriatic fibrclblasts (which exhibit a deficiency in CAMP-PK) rapidly restores CAMP-PK to a normal level (Raynaud et al, 1987). Moreover, we recently have found that RA trleatment of erythrocyte membranes prepared from psoriatic patients caused a rapid (within 15 min) increase in 8-azid0-['~P]-cAMP binding to the RI regulatory subunit (Raynaud et al, 1993).…”

Section: Resultsmentioning

confidence: 75%

“…It was of interest to relate this observed increase in the retinoylation of the type I1 regulatory subunit in psoriatic cells with the previously described effect of retinoic acid on CAMP binding to the regulatory subunit (Raynaud et al, 1987(Raynaud et al, ,1993. Thus, studies were carried out to compare the time course for enhanced cellular protein retinoylation with the time course for increased binding of the CAMP analogue, the 8-a~ido-E~~Pl-cAMP to RI and RII, in response to treatment with retinoic acid.…”

Section: Resultsmentioning

confidence: 98%

“…Retinoic acid treatment of numerous cell types has been observed to increase CAMP-PK activity (Plet et al, 1986a,b). In psoriatic cells, we have shown that the noted deficit in cAMP-PK can be reversed by retinoid treatment in vitro (fibroblasts, erythrocyte membranes) and in vivo (Raynaud et al, 1987(Raynaud et al, , 1989). …”

Section: Wiley-liss Incmentioning

confidence: 95%

“…RI and RII regulatory subunits were photoaffinity labeled as described previously (Raynaud et al, 1987) in a reaction mixture (80 pl) containin 10 mM MES, with 100 pg of cell extract. Where indicated, 100 mM CAMP was included to block 8-azid0-1~~Pl-cAMP binding to determine nonspecific labeling.…”

Section: Photoaffinity Labeling With S-azid~[~~pl Campmentioning

confidence: 99%

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Retinoylation of the type II cAMP-binding regulatory subunit of cAMP-dependent protein kinase is increased in psoriatic human fibroblasts

et al. 1996

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Previously, we have reported a defect in the cAMP-dependent protein kinases (cAMP-PK) in psoriatic cells (i.e., a decrease in 8-azido-[32P]cAMP binding to the regulatory subunits and a decrease in phosphotransferase activity) which is rapidly reversed with retinoic acid (RA) treatment of these cells. This led us to examine a possible direct interaction between retinoids and the RI and RII regulatory subunits through retinoylation. Retinoylation of RI and RII present in normal and psoriatic human fibroblasts was analysed by [3H]RA treatment of these cells, followed either by chromatographic separation of the regulatory subunits or by their specific immunoprecipitation. These studies indicated that RI and RII can be retinoylated. [3H]RA labeling of the RII subunit was significantly (P < 0.005) greater in psoriatic fibroblasts (nine subjects; mean 7.47 relative units +/- 1.37 SEM) compared to normal fibroblasts (eight subjects; mean 2.46 relative +/- 0.49 SEM). [3H]RA labeling of and the increase in 8-azido-[32P]-binding to the RI and RII subunit in psoriatic fibroblasts showed a similar time course. This suggests that the rapid effect of retinoic acid treatment to enhance 8-azido-[32P]-cAMP binding to the RI and RII in psoriatic fibroblasts may be due, in part, to covalent modification of the regulatory subunits by retinoylation.

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Section: Resultsmentioning

confidence: 75%

Section: Resultsmentioning

confidence: 98%

Section: Wiley-liss Incmentioning

confidence: 95%

Section: Photoaffinity Labeling With S-azid~[~~pl Campmentioning

confidence: 99%

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Retinoylation of the type II cAMP-binding regulatory subunit of cAMP-dependent protein kinase is increased in psoriatic human fibroblasts

et al. 1996

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“…These observations are not limited to β adrenergic signaling; differences in intracellular cAMP accumulation induced by various tmAC agonists (e.g., cholera toxin, forskolin) were also observed in psoriatic versus uninvolved or normal epidermis [62]. In addition, several studies have also reported deficiencies in cAMP effectors, including decreased expression of and cAMP binding to PKA in psoriatic fibroblasts and erythrocytes [9], which appears responsive to retinoid treatment [63,64] and has been hypothesized to result from altered posttranslational modification of PKA [65,66] or oxidative states in these cells [67]. Further, highly decreased binding of cAMP to PKA in erythrocytes was found by one group to be specific for active psoriasis [68].…”

Section: Camp Signaling In Psoriasismentioning

confidence: 88%

Cyclic Adenosine Monophosphate Signalling in Inflammatory Skin Disease

Levy¹,

Zhou²

2015

J Clin Exp Dermatol Res

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The second messenger cyclic adenosine monophosphate (cAMP) regulates numerous key pathways that impact the immune system. Distinct cellular cAMP signaling pathways can lead to both pro-and anti-inflammatory effects depending upon the cell type. When dysregulated, these cAMP pathways can influence the pathogenesis of inflammatory cutaneous diseases, such as atopic dermatitis and psoriasis. In psoriasis and atopic dermatitis, cAMP and/or its effector proteins (e.g., protein kinase A) are downregulated suggesting that elevation of cAMP might be a therapeutic option. cAMP levels are the result of balance between synthesis by adenylyl cyclases and degradation by phosphodiesterases (PDEs). Pharmacologically inhibiting PDEs represents one effective mechanism to raise intracellular cAMP levels perhaps leading to targeted immune suppression. Several drugs have been developed to target PDEs and while some toxicities (e.g., nausea and emesis) exist these drugs are generally well tolerated. Perhaps the best characterized is Apremilast, a PDE4 specific inhibitor, which has been FDA approved for the treatment of psoriasis and shows great promise as a safe and novel immunosuppressive medication. Following on the heels of Apremilast are numerous oral and topical PDE inhibitors in various stages of clinical trials. In this review, we examine the role of cAMP signaling in inflammatory cutaneous diseases and the development of PDE inhibitors as therapeutics.

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Effect of retinyl acetate on cAMP‐dependent protein kinase in transformed mouse 10t1/2 cells

Hohmann

1989

Intl Journal of Cancer

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The effect of retinyl acetate (RAC) on the activity of cAMP-dependent protein kinase (PKA) was studied in mouse 10T1/2 cells. The studies revealed that normal 10T1/2 cells had about 13-fold more PKA activity than did methylcholanthrene-transformed cells (MCA cells). The addition of RAC to MCA cells increased the activity of PKA about 3-fold as measured by the in vitro phosphorylation of a specific site in H1 histone (site A) or Kemptide. The increased PKA activity coincided with a reduction in the rate of cell replication of MCA cells, about 24 hr after exposure to the retinoid. Addition of forskolin to RAC-treated MCA cells resulted in a further reduction in the rate of cell replication, and this suggested that the enhanced PKA activity was also capable of action in vivo. To test this notion, MCA cells were grown with and without RAC, and the phosphorylation of the H1 histone at site A, a site known to be phosphorylated by PKA in cells treated with hormones or other agonists which activate PKA, was studied in vivo. RAC, by itself, was capable of causing an increase in the phosphorylation of the H1 histone at site A, demonstrating that the retinoid-mediated increase in PKA activity was sufficient to cause the enhanced phosphorylation of a known substrate.

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Retinoid Treatment of Human Psoriatic Fibroblasts Induces an Increase in Cyclic AMP-Dependent Protein Kinase Activity

Cited by 34 publications

References 23 publications

Retinoylation of the type II cAMP-binding regulatory subunit of cAMP-dependent protein kinase is increased in psoriatic human fibroblasts

Retinoylation of the type II cAMP-binding regulatory subunit of cAMP-dependent protein kinase is increased in psoriatic human fibroblasts

Cyclic Adenosine Monophosphate Signalling in Inflammatory Skin Disease

Effect of retinyl acetate on cAMP‐dependent protein kinase in transformed mouse 10t1/2 cells

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