An Adenosine 3′,5′-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle

Walsh, Donal A.; Perkins, John P.; Krebs, Edwin G.

doi:10.1016/s0021-9258(19)34204-8

Cited by 1,323 publications

(150 citation statements)

References 8 publications

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“…Our results disagree with recent reports which have claimed that PKB␣ is activated directly by PtdIns(3,4)P 2 [19][20][21]. Contamination of PKB␣ preparations with PDK1 activity may explain this discrepancy; it is worth recalling that the activation of phosphorylase kinase by cyclic AMP [22] was later shown to result from contamination with a separate cyclic AMP-dependent protein kinase [23]. It has also been reported that PKB␣ is inhibited by PtdIns(3,4,5)P 3 [19,21], but none of the four PtdIns(3,4,5)P 3 derivatives we tested inhibited the basal PKB␣ activity at all, while all four were capable of activating PDK1.…”

Section: Discussioncontrasting

confidence: 99%

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

et al. 1997

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We have purified 500 000-fold from rabbit skeletal muscle extracts a protein kinase which phosphorylates PKBalpha at Thr308 and increases its activity over 30-fold. We tested the kinase in the presence of several inositol phospholipids and found that only low micromolar concentrations of the D enantiomers of either phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) or PtdIns(3,4)P2 were effective in potently activating the kinase, which has been named PtdIns(3,4,5)P3-dependent protein kinase-1 (PDK1). None of the inositol phospholipids tested activated or inhibited PKBalpha or induced its phosphorylation under the conditions used. PDK1 activity was not affected by wortmannin, indicating that it is not likely to be a member of the phosphoinositide 3-kinase family. CONLCUSIONS: PDK1 is likely to be one of the protein kinases that mediate the activation of PKB by insulin and growth factors. PDK1 may, therefore, play a key role in mediating many of the actions of the second messenger(s) PtdIns(3,4, 5)P3 and/or PtdIns(3,4)P2.

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Section: Discussioncontrasting

confidence: 99%

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

et al. 1997

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“…14,15 Those coupled to Gs lead to the activation of cell membrane-located adenylyl cyclases (ACs). Cyclic adenosine 3′,5′-monophosphate (cAMP), which is synthesized from adenosine triphosphate (ATP) by membrane-located ACs, exerts its effects through activation of cAMP-dependent protein kinase A (PKA) to directly phosphorylate target proteins 16,17 or through actions on cyclic nucleotide-gated ion channels. 18…”

Section: Introductionmentioning

confidence: 99%

Epac and nociceptor sensitization

Huang¹,

2017

Mol Pain

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Primary sensory neurons are responsible for transmitting sensory information from the peripheral to the central nervous system. Their responses to incoming stimulation become greatly enhanced and prolonged following inflammation, giving rise to exaggerated nociceptive responses and chronic pain. The inflammatory mediator, prostaglandin E2 (PGE2), released from the inflamed tissue surrounding the terminals of sensory neurons contributes to the abnormal pain responses. PGE2 acts on G protein-coupled EP receptors to activate adenylyl cyclase, which catalyzes the conversion of adenosine triphosphate to cyclic adenosine 3′,5′-monophosphate (cAMP). Under normal conditions, cAMP activates primarily protein kinase A. After inflammation, cAMP also activates the exchange proteins activated by cAMP (Epacs) to produce exaggerated PGE2-mediated hyperalgesia. The role of cAMP-Epac signaling in the generation of hypersensitivity is the topic of this review.

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“…22 In eukaryotic cells, protein kinase A (PKA) is widely known to be the primary effector of cAMP, controlling many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation. 23,24 In addition, the guanine nucleotide exchange factor Epac1 has also been identified as a receptor for cAMP. 25 The mediated control of these pathways may be key to overcoming inhibitory antiviral mechanisms.…”

Section: Introductionmentioning

confidence: 99%

Activation of Cyclic Adenosine Monophosphate Pathway Increases the Sensitivity of Cancer Cells to the Oncolytic Virus M1

Zhang

Qiu

et al. 2016

Molecular Therapy

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Oncolytic virotherapy is a novel and emerging treatment modality that uses replication-competent viruses to destroy cancer cells. Although diverse cancer cell types are sensitive to oncolytic viruses, one of the major challenges of oncolytic virotherapy is that the sensitivity to oncolysis ranges among different cancer cell types. Furthermore, the underlying mechanism of action is not fully understood. Here, we report that activation of cyclic adenosine monophosphate (cAMP) signaling significantly sensitizes refractory cancer cells to alphavirus M1 in vitro, in vivo, and ex vivo. We find that activation of the cAMP signaling pathway inhibits M1-induced expression of antiviral factors in refractory cancer cells, leading to prolonged and severe endoplasmic reticulum (ER) stress, and cell apoptosis. We also demonstrate that M1-mediated oncolysis, which is enhanced by cAMP signaling, involves the factor, exchange protein directly activated by cAMP 1 (Epac1), but not the classical cAMP-dependent protein kinase A (PKA). Taken together, cAMP/Epac1 signaling pathway activation inhibits antiviral factors and improves responsiveness of refractory cancer cells to M1-mediated virotherapy.

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An Adenosine 3′,5′-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle

Cited by 1,323 publications

References 8 publications

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

Epac and nociceptor sensitization

Activation of Cyclic Adenosine Monophosphate Pathway Increases the Sensitivity of Cancer Cells to the Oncolytic Virus M1

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