Multiple, PKA-dependent and PKA-independent, signals are involved in cAMP-induced PRL expression in the eosinophilic cell line Eol-1

Gerlo, Sarah; Verdood, Peggy; Hooghe‐Peters, Elisabeth L.; Kooijman, Ron

doi:10.1016/j.cellsig.2004.11.010

Cited by 24 publications

(14 citation statements)

References 46 publications

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“…Although these results may support the function of EPAC in transcriptional modulation of T cells, lack of AP-1 elements in the promoters of genes identified suggests additional transcription factors specifically regulated by EPAC that are currently unreported (324). Indeed, EPAC activation was also implicated in induction of p38 phosphorylation in leukocytes (345,346), defining a potential link to other transcriptional regulators aside from c-Jun, but a complete list of genes regulated by this action is not defined.…”

Section: T Cellsmentioning

confidence: 81%

Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development

Robichaux

Cheng

2018

Physiological Reviews

160

226

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This review focuses on one family of the known cAMP receptors, the exchange proteins directly activated by cAMP (EPACs), also known as the cAMP-regulated guanine nucleotide exchange factors (cAMP-GEFs). Although EPAC proteins are fairly new additions to the growing list of cAMP effectors, and relatively "young" in the cAMP discovery timeline, the significance of an EPAC presence in different cell systems is extraordinary. The study of EPACs has considerably expanded the diversity and adaptive nature of cAMP signaling associated with numerous physiological and pathophysiological responses. This review comprehensively covers EPAC protein functions at the molecular, cellular, physiological, and pathophysiological levels; and in turn, the applications of employing EPAC-based biosensors as detection tools for dissecting cAMP signaling and the implications for targeting EPAC proteins for therapeutic development are also discussed.

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Section: T Cellsmentioning

confidence: 81%

Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development

Robichaux

Cheng

2018

Physiological Reviews

160

226

View full text Add to dashboard Cite

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“…In this regard, an increased expression of prolactin protein in blast populations has been observed in anecdotal cases of monocytic-lineage leukemia as well as in the eosinophilic cell line Eol-1 (25)(26)(27)(28)(29). In a recent study, prolactin expression in Eol-1 cells was shown to involve different signaling pathways induced by cyclic AMP whereas inhibition of Jak-STAT5 pathway resulted in up-regulation of prolactin (28). Interestingly, STAT5A and STAT5B genes were found to be significantly underexpressed in our MYST3-CREBBP AML samples, suggesting a negative regulatory effect between prolactin and STAT5 proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Among those genes, PRL and RET have been occasionally reported to be involved in leukemogenesis (24)(25)(26)(27)(28)(29)(30)(31)(32)(33). In this regard, an increased expression of prolactin protein in blast populations has been observed in anecdotal cases of monocytic-lineage leukemia as well as in the eosinophilic cell line Eol-1 (25)(26)(27)(28)(29). In a recent study, prolactin expression in Eol-1 cells was shown to involve different signaling pathways induced by cyclic AMP whereas inhibition of Jak-STAT5 pathway resulted in up-regulation of prolactin (28).…”

Section: Discussionmentioning

confidence: 99%

Gene Expression Profiling of Acute Myeloid Leukemia with Translocation t(8;16)(p11;p13) and MYST3-CREBBP Rearrangement Reveals a Distinctive Signature with a Specific Pattern of HOX Gene Expression

Camós

Esteve²,

Jares³

et al. 2006

Cancer Research

116

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Acute myeloid leukemia (AML) with translocation t(8;16)-(p11;p13) is an infrequent leukemia subtype with characteristic clinicobiological features. This translocation leads to fusion of MYST3 (MOZ) and CREBBP (CBP) genes, probably resulting in a disturbed transcriptional program of a myelomonocytic precursor. Nonetheless, its gene expression profile is unknown. We have analyzed the gene expression profile of 23 AML patients, including three with molecularly confirmed MYST3-CREBBP fusion gene, using oligonucleotide U133A arrays (Affymetrix). MYST3-CREBBP cases clustered together and clearly differentiated from samples with PML-RARa, RUNX1-RUNX1T1, and CBFb-MYH11 rearrangements. The relative expression of 46 genes, selected according to their differential expression in the high-density array study, was analyzed by low-density arrays in an additional series of 40 patients, which included 7 MYST3-CREBBP AML cases. Thus, genes such as prolactin (PRL) and protooncogene RET were confirmed to be specifically overexpressed in MYST3-CREBBP samples whereas genes such as CCND2, STAT5A, and STAT5B were differentially underexpressed in this AML category. Interestingly, MYST3-CREBBP AML exhibited a characteristic pattern of HOX expression, with up-regulation of HOXA9, HOXA10, and cofactor MEIS1 and marked down-regulation of other homeobox genes. This profile, with overexpression of FLT3, HOXA9, MEIS1, AKR7A2, CHD3, and APBA2, partially resembles that of AML with MLL rearrangement. In summary, this study shows the distinctive gene expression profile of MYST3-CREBBP AML, with overexpression of RET and PRL and a specific pattern of HOX gene expression. (Cancer Res 2006; 66(14): 6947-54)

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“…EPACs are guanine nucleotide exchange factors for the small G protein Rap1 (26). cAMP-dependent and phorbol ester/ PKC-dependent activations of p38, JNK, and ERK have been reported (18,21,(27)(28)(29)(30)(31). For example, h-adrenergic stimulation of p38 is blocked by a PKA inhibitor in brown adipocytes.…”

Section: Introductionmentioning

confidence: 99%

Prostaglandin E2 Induces Breast Cancer–Related Aromatase Promoters via Activation of p38 and c-Jun NH2-Terminal Kinase in Adipose Fibroblasts

et al. 2007

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Aromatase is the key enzyme for estrogen biosynthesis. A distal promoter, PI.4, maintains baseline levels of aromatase in normal breast adipose tissue. In contrast, malignant breast epithelial cells secrete prostaglandin E 2 (PGE 2 ), which stimulates aromatase expression via proximal promoters PI.3/PII in a cyclic AMP (cAMP)-and protein kinase C (PKC)-dependent manner in adjacent breast adipose fibroblasts (BAF), leading to increased local concentrations of estrogen. Although an effective treatment for breast cancer, aromatase inhibitors indiscriminately abolish estrogen synthesis in all tissues, causing major side effects. To identify drug targets to selectively block aromatase and estrogen production in breast cancer, we investigated PGE 2 -stimulated signaling pathways essential for aromatase induction downstream of cAMP and PKC in human BAFs. Here, we show that PGE 2 or its surrogate hormonal mixture dibutyryl cAMP (Bt 2 cAMP) + phorbol diacetate (PDA) stimulated the p38, c-jun NH 2 -terminal kinase (JNK)-1, and extracellular signalregulated kinase (ERK) mitogen-activated protein kinase pathways. Inhibition or small interfering RNA-mediated knockdown of p38 or JNK1, but not ERK, inhibited PGE 2 -or Bt 2 cAMP + PDA-induced aromatase activity and expression via PI.3/PII. Conversely, overexpression of wildtype p38A or JNK1 enhanced PGE 2 -stimulated aromatase expression via PII. PGE 2 or Bt 2 cAMP + PDA stimulated c-Jun and activating transcription factor-2 (ATF2) phosphorylation and binding to the PI.3/PII region. Specific activation of protein kinase A (PKA) or EPAC with cAMP analogues stimulated p38 and JNK1; however, only PKAactivating cAMP analogues induced aromatase expression. The PKC activator PDA effectively stimulated p38 and JNK1 phosphorylation but not aromatase expression. Taken together, PGE 2 activation of p38 and JNK1 via PKA and PKC is necessary for aromatase induction in BAFs, and p38 and JNK1 are potential new drug targets for tissue-specific ablation of aromatase expression in breast cancer. [Cancer Res 2007;67(18):8914-22]

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Multiple, PKA-dependent and PKA-independent, signals are involved in cAMP-induced PRL expression in the eosinophilic cell line Eol-1

Cited by 24 publications

References 46 publications

Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development

Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development

Gene Expression Profiling of Acute Myeloid Leukemia with Translocation t(8;16)(p11;p13) and MYST3-CREBBP Rearrangement Reveals a Distinctive Signature with a Specific Pattern of HOX Gene Expression

Prostaglandin E2 Induces Breast Cancer–Related Aromatase Promoters via Activation of p38 and c-Jun NH2-Terminal Kinase in Adipose Fibroblasts

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