Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit
A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIALPHA SUBUNIT. Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A.
Cyclic AMP-Dependent Protein Kinase Type II
Cyclic AMP-Dependent Protein Kinases
Cyclic AMP
Protein Kinases
Protein Kinase C
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
Phosphorylation
Calcium-Calmodulin-Dependent Protein Kinases
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
Enzyme Activation
Calcium-Calmodulin-Dependent Protein Kinase Type 2
A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.
Generation of a novel A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog from a single gene. (1/56)
A unique Drosophila gene encodes two novel signaling proteins. Drosophila A kinase anchor protein 200 (DAKAP200) (753 amino acids) binds regulatory subunits of protein kinase AII (PKAII) isoforms in vitro and in intact cells. The acidic DAKAP200 polypeptide (pI approximately 3.8) contains an optimal N-terminal myristoylation site and a positively charged domain that resembles the multifunctional phosphorylation site domain of vertebrate myristoylated alanine-rich C kinase substrate proteins. The 15-kilobase pair DAKAP200 gene contains six exons and encodes a second protein, DeltaDAKAP200. DeltaDAKAP200 is derived from DAKAP200 transcripts by excision of exon 5 (381 codons), which encodes the PKAII binding region and a Pro-rich sequence. DeltaDAKAP200 appears to be a myristoylated alanine-rich C kinase substrate analog. DAKAP200 and DeltaDAKAP200 are evident in vivo at all stages of Drosophila development. Thus, both proteins may play important physiological roles throughout the life span of the organism. Nevertheless, DAKAP200 gene expression is regulated. Maximal levels of DAKAP200 are detected in the pupal phase of development; DeltaDAKAP200 content is elevated 7-fold in adult head (brain) relative to other body parts. Enhancement or suppression of exon 5 excision during DAKAP200 pre-mRNA processing provides potential mechanisms for regulating anchoring of PKAII and targeting of cAMP signals to effector sites in cytoskeleton and/or organelles. (+info)Mutation of the RIIbeta subunit of protein kinase A differentially affects lipolysis but not gene induction in white adipose tissue. (2/56)
Targeted disruption of the RIIbeta subunit of protein kinase A (PKA) produces lean mice that resist diet-induced obesity. In this report we examine the effects of the RIIbeta knockout on white adipose tissue physiology. Loss of RIIbeta is compensated by an increase in the RIalpha isoform, generating an isoform switch from a type II to a type I PKA. Type I holoenzyme binds cAMP more avidly and is more easily activated than the type II enzyme. These alterations are associated with increases in both basal kinase activity and the basal rate of lipolysis, possibly contributing to the lean phenotype. However, the ability of both beta(3)-selective and nonspecific beta-adrenergic agonists to stimulate lipolysis is markedly compromised in mutant white adipose tissue. This defect was found in vitro and in vivo and does not result from reduced expression of beta-adrenergic receptor or hormone-sensitive lipase genes. In contrast, beta-adrenergic stimulated gene transcription remains intact, and the expression of key genes involved in lipid metabolism is normal under both fasted and fed conditions. We suggest that the R subunit isoform switch disrupts the subcellular localization of PKA that is required for efficient transduction of signals that modulate lipolysis but not for those that mediate gene expression. (+info)High ethanol consumption and low sensitivity to ethanol-induced sedation in protein kinase A-mutant mice. (3/56)
Both in vitro and in vivo evidence indicate that cAMP-dependent protein kinase (PKA) mediates some of the acute and chronic cellular responses to alcohol. However, it is unclear whether PKA regulates voluntary alcohol consumption. We therefore studied alcohol consumption by mice that completely lack the regulatory IIbeta (RIIbeta) subunit of PKA as a result of targeted gene disruption. Here we report that RIIbeta knockout mice (RIIbeta-/-) showed incr eased consumption of solutions containing 6, 10, and 20% (v/v) ethanol when compared with wild-type mice (RIIbeta+/+). On the other hand, RIIbeta-/- mice showed normal consumption of solutions containing either sucrose or quinine. When compared with wild-type mice, the RIIbeta-/- mice were found to be less sensitive to the sedative effects of ethanol as measured by more rapid recovery from ethanol-induced sleep, even though plasma ethanol concentrations did not differ significantly from those of controls. Finally, both RIbeta- and catylatic subunit beta1-deficient mice showed normal voluntary consumption of ethanol, indicating that increased ethanol consumption is not a general characteristic associated with deletion of PKA subunits. These data demonstrate a role for the RIIbeta subunit of PKA in regulating voluntary consumption of alcohol and sensitivity to the intoxication effects that are produced by this drug. (+info)8-chloro-cAMP inhibits smooth muscle cell proliferation in vitro and neointima formation induced by balloon injury in vivo. (4/56)
OBJECTIVES: The aims of the present study were to assess 1) the effect of 8-C1-cAMP (cyclic-3'-5'-adenosine monophosphate) on vascular smooth muscle cell (VSMC) proliferation in vitro and 2) the efficacy of systemic administration of 8-C1-cAMP on neointimal formation after balloon injury in vivo. BACKGROUND: Neointimal formation after vascular injury is responsible for restenosis after arterial stenting. Recently, 8-C1-cAMP, a cAMP analogue that induces growth arrest, has been safely administered in phase I studies in humans. METHODS: The effect of 8-C1-cAMP on cell proliferation was first assessed on SMCs in vitro. To study the effects of cAMP in vivo, balloon injury was performed in 67 rats using a 2F Fogarty balloon catheter. RESULTS: The 8-C1-cAMP markedly inhibited VSMC proliferation in vitro, reduced protein kinase A (PKA) RIalpha subunit expression, and induced PKA RIIbeta subunit expression. In addition, 8-C1-cAMP reduced, in a dose-dependent manner, neointimal area and neointima/media ratio after balloon injury. The proliferative activity, assessed by proliferating nuclear cell antigen immunostaining, revealed a reduction of proliferative activity of VSMCs in vivo in the 8-C1-cAMP group. Moreover, the systemic administration of 8-C1-cAMP did not affect renal function, blood pressure and heart rate. CONCLUSIONS: We conclude that 8-C1-cAMP potently inhibits VSMC proliferation in vitro and reduces neointima formation by balloon injury in vivo after systemic administration. These data may have a clinical relevance in designing future strategies to prevent restenosis after arterial stenting and perhaps after percutaneous transluminal coronary angioplasty. (+info)Association of deficient type II protein kinase A activity with aberrant nuclear translocation of the RII beta subunit in systemic lupus erythematosus T lymphocytes. (5/56)
Systemic lupus erythematosus (SLE) is an autoimmune disorder of indeterminate etiology characterized by abnormal T cell signal transduction and altered T cell effector functions. We have previously observed a profound deficiency of total protein kinase A (PKA) phosphotransferase activity in SLE T cells. Here we examined whether reduced total PKA activity in SLE T cells is in part the result of deficient type II PKA (PKA-II) isozyme activity. The mean PKA-II activity in SLE T cells was 61% of normal control T cells. The prevalence of deficient PKA-II activity in 35 SLE subjects was 37%. Deficient isozyme activity was persistent over time and was unrelated to SLE disease activity. Reduced PKA-II activity was associated with spontaneous dissociation of the cytosolic RIIbeta2C2 holoenzyme and translocation of the regulatory (RIIbeta) subunit from the cytosol to the nucleus. Confocal immunofluorescence microscopy revealed that the RIIbeta subunit was present in approximately 60% of SLE T cell nuclei compared with only 2-3% of normal and disease controls. Quantification of nuclear RIIbeta subunit protein content by immunoprecipitation and immunoblotting demonstrated a 54% increase over normal T cell nuclei. Moreover, the RIIbeta subunit was retained in SLE T cell nuclei, failed to relocate to the cytosol, and was associated with a persistent deficiency of PKA-II activity. In conclusion, we describe a novel mechanism of deficient PKA-II isozyme activity due to aberrant nuclear translocation of the RIIbeta subunit and its retention in the nucleus in SLE T cells. Deficient PKA-II activity may contribute to impaired signaling in SLE T cells. (+info)Compensatory stabilization of RIIbeta protein, cell cycle deregulation, and growth arrest in colon and prostate carcinoma cells by antisense-directed down-regulation of protein kinase A RIalpha protein. (6/56)
The cyclic AMP-dependent protein kinase (PKA) exists in two isoforms, PKA-I (type I) and PKA-II (type II), that contain an identical catalytic (C) subunit but distinct regulatory (R) subunits, RI and RII, respectively. Increased expression of RIalpha/PKA-I has been shown in human cancer cell lines, in primary tumors, in cells after transformation, and in cells upon stimulation of growth. We have shown previously that a single-injection RI, antisense treatment results in a reduction in RIalpha and PKA-I expression and sustained inhibition of human colon carcinoma growth in athymic mice (M. Nesterova and Y. S. Cho-Chung, Nat. Med., 1: 528-533, 1995). Growth inhibition accompanied reduction in RIalpha/PKA-I expression and compensatory increases in RIIbeta protein and PKA-IIbeta, the RIIbeta-containing holoenzyme. Here, we report that these in vivo findings are consistent with observations made in cancer cells in culture. We demonstrate that the antisense depletion of RIalpha in cancer cells results in increased RIIbeta protein without increasing the rate of RIIbeta synthesis or RIIbeta mRNA levels. Pulse-chase experiments revealed a 3-6-fold increase in the half-life of RIIbeta protein in antisense-treated colon and prostate carcinoma cells with little or no change in the half-lives of RIalpha, RIIalpha, and Calpha proteins. Compensation by RIIbeta stabilization may represent a novel biochemical adaptation mechanism of the cell in response to sequence-specific loss of RIalpha expression, which leads to sustained down-regulation of PKA-I activity and inhibition of tumor growth. (+info)Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit. (7/56)
BACKGROUND: Cyclic AMP binding domains possess common structural features yet are diversely coupled to different signaling modules. Each cAMP binding domain receives and transmits a cAMP signal; however, the signaling networks differ even within the same family of regulatory proteins as evidenced by the long-standing biochemical and physiological differences between type I and type II regulatory subunits of cAMP-dependent protein kinase. RESULTS: We report the first type II regulatory subunit crystal structure, which we determined to 2.45 A resolution and refined to an R factor of 0.176 with a free R factor of 0.198. This new structure of the type II beta regulatory subunit of cAMP-dependent protein kinase demonstrates that the relative orientations of the two tandem cAMP binding domains are very different in the type II beta as compared to the type I alpha regulatory subunit. Each structural unit for binding cAMP contains the highly conserved phosphate binding cassette that can be considered the "signature" motif of cAMP binding domains. This motif is coupled to nonconserved regions that link the cAMP signal to diverse structural and functional modules. CONCLUSIONS: Both the diversity and similarity of cAMP binding sites are demonstrated by this new type II regulatory subunit structure. The structure represents an intramolecular paradigm for the cooperative triad that links two cAMP binding sites through a domain interface to the catalytic subunit of cAMP-dependent protein kinase. The domain interface surface is created by the binding of only one cAMP molecule and is enabled by amino acid sequence variability within the peptide chain that tethers the two domains together. (+info)Positive regulation of cell-cell and cell-substrate adhesion by protein kinase A. (8/56)
Integrin receptor activation is an important regulatory mechanism for cell-substrate and cell-cell adhesion. In this study, we explore a signaling pathway activated by mAb 12G10, an antibody that can activate beta(1) integrins and induce integrin-mediated cell-cell and cell-substrate adhesion. We have found that the cAMP-dependent protein kinase (PKA) is required for both mAb 12G10-induced cell-cell and cell-substrate adhesion of HT-1080 cells. Binding of mAb 12G10 to beta(1) integrins stimulates an increase in intracellular cAMP levels and PKA activity, and a concomitant shift in the localization of the PKA type II regulatory subunits from the cytoplasm to areas where integrins expressing the 12G10 epitope are located. MAb 12G10-induced cell-cell adhesion was mimicked by a combination of clustering beta(1) integrins and elevating PKA activity with Sp-adenosine-3',5'-cyclic monophosphorothioate or forskolin. We also show that two processes required for HT-1080 cell-cell adhesion, integrin clustering and F-actin polymerization are both dependent on PKA. Taken together, our data suggest that PKA plays a key role in the signaling pathway, resulting from activation of beta(1) integrins, and that this enzyme may be required for upregulation of cell-substrate and cell-cell adhesion. (+info)
Pain modulators regulate the dynamics of PKA-RII phosphorylation in subgroups of sensory neurons | Journal of Cell Science
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PRKAR2A
... type-II regulatory subunit of cyclic-AMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5 ... Reverse mobilities of human RII alpha and RII beta on sodium dodecyl sulfate-polyacrylamide gel electrophoresis compared with ... "MTG8 proto-oncoprotein interacts with the regulatory subunit of type II cyclic AMP-dependent protein kinase in lymphocytes". ... "Ezrin is a cyclic AMP-dependent protein kinase anchoring protein". The EMBO Journal. 16 (1): 35-43. doi:10.1093/emboj/16.1.35. ...
DeCS
Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit Descripteur en anglais: Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit ... Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit [D12.776.476.563.150.125.875.875] Cyclic AMP-Dependent Protein Kinase ... Cyclic AMP-Dependent Protein Kinase Catalytic Subunits [D12.776.476.563.150.125.875.500] Cyclic AMP-Dependent Protein Kinase ... Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit [D12.776.476.563.150.125.875.750] Cyclic AMP-Dependent Protein Kinase ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... Protein Kinase A, Type II BX - Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
Winnie Eskild - Institutt for biovitenskap
Cyclic AMP increases the mRNA levels for the regulatory subunit (R-II51) of type II cAMP-dependent protein kinase in rat ... cyclic adenosine monophosphate-dependent protein kinases (RII beta and RI alpha) via multiple and distinct mechanisms. ... Hormonal regulation and age dependent changes in mRNA levels for regulatory subunits of cAMP-dependent protein kinases in rat ... Cellular localization and age-dependent changes in mRNA for cyclic adenosine 3,5-monophosphate-dependent protein kinases in ...
Josep Planas , Ph.D. | IPHC | IPHC
Mutation of the RIIbeta subunit of protein kinase A differentially affects lipolysis but not gene induction in white adipose ... Cyclic AMP, PKA, and the physiological regulation of adiposity. Recent Prog Horm Res. 1998, 53:139-59. ... Activation of the cAMP-dependent protein kinase signaling pathway by luteinizing hormone in trout theca layers. Mol Cell ... Genetically lean mice result from targeted disruption of the RII beta subunit of protein kinase A. Nature. 1996, 382(6592):622- ...
Búsqueda | BVS Bolivia
Cyclic AMP-dependent protein kinase A (PKA) is a ubiquitous enzymatic complex that is involved in a broad spectrum of ... The RIIß subunit of cAMP-dependent protein kinase A (PKA) is expressed in the brain and adipose tissue. RIIß-knockout mice show ... Subunidad RIIbeta de la Proteína Quinasa Dependiente de AMP Cíclico/metabolismo , Proteínas Quinasas Dependientes de AMP ... Interaction between A-kinase anchoring protein 5 and protein kinase A mediates CaMKII/HDAC signaling to inhibit cardiomyocyte ...
No data available that match "cyclic amp dependent protein kinase riibeta subunit"
Depends2
- The lysosomal transporter mfsd1 is essential for liver homeostasis and critically depends on its accessory subunit glmp. (uio.no)
- The activity of PKA depends on A-kinase anchoring proteins (AKAPs) that attach to PKAs close to their substrates to control signaling. (bvsalud.org)
Activity2
- A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. (bvsalud.org)
- Additionally, western blot analysis showed that WP and UroA treatment significantly increased the activity of cAMP-dependent protein kinase A (PKA) and the expression of pCREB (Ser133) and its downstream molecule brain-derived neurotrophic factor (BDNF), which were decreased by H2O2 treatment. (bvsalud.org)
CAMP3
- In 1957, cyclic adenosine monophosphate (cAMP) was identified as the first secondary messenger, and the first signaling cascade discovered was the cAMP-protein kinase A (PKA) pathway. (bvsalud.org)
- Not long ago, a new cAMP effector named exchange protein directly activated by cAMP (Epac) emerged as a critical mediator of cAMP's actions. (bvsalud.org)
- In the present study, we evaluated the protective effect of WP and urolithin A (UroA) on H2O2-induced damage in human neuroblastoma (SH-SY5Y) cells, and investigated its mechanisms in the cAMP-response element binding protein (CREB)-mediated signaling pathway, which is tightly involved in neurodegenerative and neurological diseases. (bvsalud.org)