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Human Polyclonal PRKACA Primary Antibody for IHC (p), ELISA - ABIN545453
Libersan, Rousseau, Merhi: Differential regulation of P-selectin expression by protein kinase A and protein kinase G in thrombin-stimulated human platelets. in Thrombosis and haemostasis 2003
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Human Monoclonal PRKACA Primary Antibody for DB, WB - ABIN535235
Mac?rek, Zíková, Dráberová, Dráber: Monoclonal antibody BF-06 against the heavy chain of clathrin. in Folia biologica 2004
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Human Polyclonal PRKACA Primary Antibody for ELISA, WB - ABIN562366
Adachi, Kano, Saido, Murata: Visual screening and analysis for kinase-regulated membrane trafficking pathways that are involved in extensive beta-amyloid secretion. in Genes to cells : devoted to molecular & cellular mechanisms 2009
Ezrin-anchored PKA phosphorylates serine 369 and 373 on connexin 43 to enhance gap junction assembly, communication, and cell fusion.
CaV1.4 channels are indeed modulated by PKA phosphorylation within the inhibitor of Ca(2+)-dependent inactivation (ICDI) motif.
In this study, the authors linked for the first time the loss of RIIbeta protein levels to the PRKACA mutation status and found the down-regulation of RIIbeta to arise post-transcriptionally.
the presence of lipofuscin in cortisol-producing adenomas (CPAs) responsible for Cushing syndrome with and without the PRKACA (pLeu206Arg) somatic mutation, was investigated.
Mechanistically, Sirt1 expression elevates phosphorylation of the alpha subunit of protein kinase A (PKA alpha), and this event is essential for Sirt1-induced phosphorylation of beta Catenin.
PKA, under the conditions of experimental approach appears to function as a master upstream kinase that is sufficient to initiate the complex pattern of intracellular signaling pathway and gene expression profiles that accompany ovarian granulosa cells differentiation
Together, the results suggest a complex antagonistic interplay between the control of ARPP-16 by MAST3 and PKA that creates a mechanism whereby cAMP mediates PP2A disinhibition.
CTR activates AKAP2-anchored cAMP-dependent protein kinase A, which then phosphorylates tight junction proteins ZO-1 and claudin 3.
These results indicate that Mixed fibrolamellar hepatocellular carcinoma (mFL-HCC) is similar to pure FL-HCC at the genomic level and the DNAJB1:PRKACA fusion can be used as a diagnostic tool for both pure and mFL-HCC
PRKACA mutations are highly specific for cortisol over-secretion, while they are absent or very rare in the context of other adrenal diseases. Patients carrying these somatic mutations are affected by a more severe phenotype and are identified at a younger age.
Somatic mutations in PRKACA, coding for the catalytic alpha subunit of protein kinase A (PKA), have been recently identified as the most frequent genetic alteration in cortisol-secreting adrenocortical adenomas, which are responsible for adrenal Cushing's syndrome.
HIF1a transcriptional activity is stimulated by Protein kinase A-dependent phosphorylation
cigarette smoke extracts activate the PKA, CREB, and IL-13Ralpha2 axis in lung endothelial cells.
Data indicate a subpopulation of the CaV1.2 channel pore-forming subunit (alpha1C) within nanometer proximity of protein kinase A (PKA) at the sarcolemma of murine and human arterial myocytes.
we propose that the PKA-Smurf1-PIPKIgamma pathway has an important role in pulmonary tumorigenesis and imposes substantial clinical impact on development of novel diagnostic markers and therapeutic targets for lung cancer treatment.
cAMP/PKA signaling attenuated respiratory syncytial virus-induced disruption of structure and functions of the model airway epithelial barrier by mechanisms involving the stabilization of epithelial junctions and inhibition of viral biogenesis
The mutated PRKACA proteins lost their ability to bind to PRKAR1A, and thereby lead to constitutive activation of the PKA pathway. Together with previous reports of PRKAR1A mutations in syndromic cardiac myxoma, our study demonstrates the importance of the PKA pathway in the tumourigenesis of cardiac myxoma.
differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II.
Data show that the adenylate cyclase (AC) pathway as genes relating to the antitumor activity of xanthohumol (XN) against tumor cells, and the pathway regulates various cellular functions via activating protein kinase A (PKA)-dependent phosphorylation.
PRKACA mutations are present in cortisol-producing adenomas and bilateral adrenal macronodular hyperplasia. PRKACA mutation is associated with more severe autonomous cortisol secretion.
PKA and MEK (thus, also pERK) are the intracellular mediators downstream of GPR30 that induce the non-genomic suppression of GnRH-induced LH secretion from bovine AP cells by estradiol or G1
Data indicate that mitochondrial cAMP-dependent protein kinase (PKA) activity is regulated by the protease calpain.
structural basis of selectivity for protein kinase A in complex with Rho-kinase inhibitors by x-ray crystallography
Purification and characterisation of protein kinase catalytic subunit (PKAcat) from bovine lens.
These data strongly suggest that H(2)O(2) promotes the formation of an intersubunit disulfide bond, impairing cAMP-dependent PKA activation.
Data suggest that regulation of oxidative phosphorylation does not involve protein kinase A (PKA).
Analyses of the involvement of PKA regulation mechanism in meiotic incompetence of porcine growing oocytes.
ceramide as a potent physiological modulator of the Na(+)-ATPase, participating in a regulatory network in kidney cells and counteracting the stimulatory effect of PKA via PKCzeta
we demonstrate that PKA, PKC and PI3K pathways crosstalk in porcine male germ cells to crucially regulate GSK3A phosphorylation which subsequently controls cell motility.
The cooperativity mechanism of Pkaca critically depends on the presence of water in two distinct, buried hydration sites.
Study validates the DNAJB1-PRKACA fusion kinase as an oncogenic driver and candidate drug target for fibrolamellar hepatocellular carcinoma in mouse model in which tumorigenesis was significantly enhanced by genetic activation of beta-catenin.
Protein kinase A signaling explains vasopressin-mediated regulation of membrane trafficking and gene transcription.
Data suggest that the Girvan-Newman algorithm-based community maps of the kinase domain of cAMP-dependent protein kinase A (PKA) allow for a molecular explanation for the role of protein conformational entropy in its catalytic cycle.
Acute versus chronic exposure to high fat diet leads to distinct regulation of PKA.
Data suggest that the upregulation of mitochondrial respiratory chain proteins played a partial role in the protection of PKA/CREB signaling.
Generation of the Dnajb1-Prkaca fusion gene in wild-type mice to be sufficient to initiate formation of tumors that have many features of human fibrolamellar hepatocellular carcinonma.
S1928A KI mice failed to induce long-term potentiation in response to prolonged theta-tetanus (PTT-LTP), a form of synaptic plasticity that requires Cav1.2 and enhancement of its activity by the beta2-adrenergic receptor (beta2AR)-cAMP-PKA cascade.
Data show that laminin alpha2beta1gamma1 (Lm211) can inhibit neuregulin 1 type III (Nrg1III) by limiting protein kinase A (PKA) activation, which is required to initiate myelination.
study identifies a new role of Dual-AKAP1 in regulating mitochondrial trafficking through Miro-2, and supports a model in which PINK1 and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit)
cAMP dependent protein kinase A (PKA) is a key intracellular factor mediating SHH signaling through regulation of GLI3 processing.
this study shows illustrates for the first time the ability of protein kinase A to increase colony-stimulating factor 1 receptor DNA methylation resulting in macrophage maturation
these results suggest that the activation of 5-HT1D receptors selectively enhanced IA via the Gbetagamma of the Go-protein, PKA, and the sequential B-Raf-dependent p38 MAPK signaling cascade.
These data indicate that LPA increases CCN2 expression through the activation of PKC and PKA. Thus, the regulatory functions of the PKC and PKA pathways are implicated in the LPA-induced increase in CCN2 expression
PKA phosphorylates the ATPase inhibitory factor 1 and inactivates its capacity to bind and inhibit the mitochondrial H(+)-ATP synthase.
Data suggest PRKAR1A contains two structurally homologous cAMP-binding domains that exhibit marked differences in dynamic profiles in activation/inhibition of Prkaca; conservation of structure does not necessarily imply conservation of dynamics.
Data (including data from studies in transgenic mice) suggest that constitutive activation of Prkaca in osteoblasts is sufficient to increase bone mass, favorably modify bone architecture, and improve mechanical properties of bone.
support hypothesis that PRKACA activation is responsible for downstream protein tyrosine phosphorylation events in stallion sperm
Thus Ca(2+)-cAMP/PKA-dependent phosphorylation limits the rate and magnitude of increase in spontaneous action potential firing rate.
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
, cAMP-dependent protein kinase catalytic subunit alpha
, protein kinase A catalytic subunit
, cAMP-dependent protein kinase catalytic subunit C alpha
, protein kinase A
, protein kinase, cAMP-dependent, catalytic, alpha
, C-alpha subunit
, sperm cAMP-dependent protein kinase catalytic subunit
, protein kinase A alpha
, PKA catalytic subunit alpha