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Human Monoclonal PRKAR1A Primary Antibody for IF, IHC - ABIN2729578
Maleszewski, Larsen, Kip, Castonguay, Edwards, Carney, Kipp: PRKAR1A in the development of cardiac myxoma: a study of 110 cases including isolated and syndromic tumors. in The American journal of surgical pathology 2014
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Human Polyclonal PRKAR1A Primary Antibody for IHC (p), ELISA - ABIN544271
Grönholm, Vossebein, Carlson, Kuja-Panula, Teesalu, Alfthan, Vaheri, Rauvala, Herberg, Taskén, Carpén: Merlin links to the cAMP neuronal signaling pathway by anchoring the RIbeta subunit of protein kinase A. in The Journal of biological chemistry 2003
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Human Polyclonal PRKAR1A Primary Antibody for WB - ABIN519180
Uys, Ramburan, Loos, Kinnear, Korkie, Mouton, Riedemann, Moolman-Smook: Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C. in BMC cell biology 2011
Human Polyclonal PRKAR1A Primary Antibody for EIA, ICC - ABIN2729579
Cao, Xia, Zhou, Yang, Hao, Peng, Liu, Zhu: Methylcrotonoyl-CoA carboxylase 1 potentiates RLR-induced NF-κB signaling by targeting MAVS complex. in Scientific reports 2016
PRKAR1A mutation is associated with Carney complex.
PRKAR1A gene mutations found in patients with primary pigmented nodular adrenocortical disease (PPNAD): c.125dupG (patient 1) and c.15dupT (patient 2). Both these defects lead to inactivation of the PRKAR1A protein and are consequently causative of PPNAD in these patients.
In Pseudohypoparathyroidism, mutations were found in PRKAR1A, PDE4D, TRPS1, and PTHLH.
A report of the occurrence of an aberrant serotonergic regulatory loop in primary pigmented nodular adrenocortical disease tissues from patients with PRKAR1A mutations.
Splice site mutation of the PRKAR1A gene is associated with Carney complex.
PRKAR1A is a potent tumor suppressor that inhibits the ERK/Snail/E-cadherin pathway in lung adenocarcinoma
t-Darpp phosphorylation at T39 seems to be crucial for t-Darpp-mediated PKA activation and this activation appears to occur through an association with RI and sequestering of RI away from PKAc. The t-Darpp-RI interaction could be a druggable target to reduce PKA activity in drug-resistant cancer.
the T allele of SNP rs60684937 located at 67,419,130 bp on chromosome 17 was associated with increased plasma EPO and a relatively increased expression of a non-coding transcript of PRKAR1A in sickle cell disease patients
In this study we demonstrate a new role of MRAP2 in the regulation of the orexin receptor 1 (OX1R) and identify the specific regions of MRAP2 required for the regulation of OX1R and PKR1. Importantly, like MC4R and PKRs, OX1R is predominately expressed in the brain where it regulates food intake
Screening of PRKAR1A and PDE4D in a Large Italian Series of Patients Clinically Diagnosed With Albright Hereditary Osteodystrophy and/or Pseudohypoparathyroidism
we used next-generation sequencing to assess 480 cancer-related genes and performed immunohistochemistry on 13 cases morphologically consistent with pigmented epithelioid melanocytoma. These results further validate the concept of pigmented epithelioid melanocytoma as a distinctive intermediate/borderline melanocytic tumor, and also illustrate its molecular heterogeneity
Found evidence for kidney and liver cystic phenotypes in the Carney complex, a tumoral syndrome caused by mutations in PRKAR1A.
immunohistochemical staining for StAR is a reliable pathological approach for the diagnosis and classification of adrenocortical adenomas with cAMP/PKA signaling-activating mutations.
Data suggest that introduction of cGMP-specific residues using site-directed mutagenesis reduces selectivity of cyclic nucleotide-binding domain (CNBD) of PRKAR1A; combination of two mutations (G316R/A336T) results in a cGMP-selective binding site in the C-terminal CNBD; introduction of corresponding mutations (T192R/A212T) into the N-terminal CNBD results in a highly cGMP-selective binding site.
Data show that ELOVL7, SOCS3, ACSL4 and CLU were upregulated while PRKAR1A and ABCG1 were downregulated in the phlegm-dampness group.
Electrostatic interactions are mediators in the allosteric activation of protein kinase A RIalpha.
The obtained data on the mechanism of cAMP-dependent activation of PKA I alpha may contribute to new approaches to designing pharmaceuticals based on cAMP analogs.
the present study reported for the first time an intronic splice site mutation in the PRKAR1A gene of a Chinese family with Carney complex, which probably caused skin pigmentation observed in affected family members.
This study reports a novel point mutation of the PRKAR1A gene in a patient with Carney complex who presented with significant osteoporosis and fractures.
Letter/Case Report: novel PRKAR1A mutation resulting in a splicing variant in a case of Carney complex.
Mice with a genetic background of Tpo-Cre;Prkar1a(flox/flox);Epac1(-/-) are aggressive, and both the thyroid-specific knockout of Prkar1a and global knockout of Epac1 likely contribute to this aggressive behavior. This study supports the hypothesis that altered thyroid signaling and aggressive behavior are linked.
This mouse knockout model supports the role of prkar1a as a tumor suppressor gene in the pancreas and points to the PKA pathway as a possible therapeutic target for these lesions.
This model, the first describing the germline expression of a PRKAR1A mutation causing dominant repression of cAMP-dependent PKA, reproduced the main features of acrodysostosis 1 in humans.
These results therefore provide new information on the complex regulation of cellular death under endoplasmic reticulum stress conditions and bring new insights on the conditions that regulate the pro- versus anti-death functions of PKA.
This study demonstrated that loss of one Prkar1a allele was associated with a significant increase in PKA activity in the basolateral (BLA) and central (CeA) amygdala and ventromedial hypothalamus (VMH) in both Prkar1a(+/-) and Prkar1a(+/-)/Prkaca(+/-) mice.
Kidney-specific loss of Prkar1a induced renal cystic disease and markedly aggravated cystogenesis in the Pkd1(RC) models.
data demonstrate that haploinsufficiency for either one of the type-II regulatory subunits improved the bone phenotype of mice haploinsufficient for Prkar1a
PKARIalpha oxidation is an essential step in the angiogenic pathway.
PRKAR1A gene and its locus are altered in mixed odontogenic tumors. Expression is decreased in a subset of tumors, and Prkar1a(+) (/) (-) mice do not show abnormalities, which indicates that additional genes play a role in this tumor's pathogenesis.
Prkar1a activation enhances beta-catenin transcriptional activity through nuclear localization to PML bodies.
Loss of Prkar1a can only promote tumorigenesis when Prkar1a-mediated apoptosis is somehow countered.
Data show that mammary-specific loss of Prkar1a leads to elevated type-II PKA isozyme activation and this is sufficient to drive breast carcinogenesis.
Results show that mouse Prkar1a and human PRKAR2A exhibited a dynamic spatio-temporal expression in tooth development, whereas neither human PRKAR1A nor mouse Prkar2a showed their expression in odontogenesis.
Ablation of Prkar1a interferes with signaling pathways necessary for osteoblast differentiation.
This study demonstrated a critical role for cytoplasmic RI-PKA holoenzyme in gene regulation and the overall physiological function of Striatal medium spiny neurons.
hypoxia/reoxygenation (H/R)-mediated decrease in PKARIalpha protein levels leads to activation of RSK1, which via phosphorylation of NHE1 induces cardiomyocyte apoptosis.
Prkar1a was found to play a critical role in peripheral nerve development.
Dysregulated protein kinase A activity in the amygdala-prefrontal cortex circuitry in Prkar1a(+/-) mice is associated with behavioral phenotype of anxiety and a bias for threat
PKA activation through mutation in Prkar1a is sufficient to initiate Rac1 signaling, with subsequent reduction of Nf2 and schwannomagenesis.
Prkar1a is indeed a tumor suppressor in the thyroid and that loss of this gene leads to hyperthyroidism and follicular thyroid cancer
Analyses of the involvement of PKA regulation mechanism in meiotic incompetence of porcine growing oocytes.
ceramide activates plasma membrane Ca2+-ATPase from kidney-promixal tubule cells with protein kinase A as an intermediate
Results demonstrate that PKA activity regulated by Mys is indispensable for negative regulation of the Hh signaling pathway in Hh-responsive cells.
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)
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.
Thermodynamic analysis of protein kinase A (PKA) Ialpha activation was performed using Quantum 3.3.0 docking software and a Gaussian 03W quantum mechanical computational package.
Results describe the structures of the protein kinase A RIalpha subunit D/D domain alone and in complex with D-AKAP2.
Data show that RSK1 regulates PKAc activity in a cAMP-independent manner, and PKARIalpha by associating with RSK1 regulates its activation and its biological functions.
angle X-ray scattering studies indicate RIalpha, RIIalpha, and RIIbeta homodimers differ markedly in overall shape despite extensive sequence homology and similar molecular masses;cAMP binding does not cause large conformational changes(Prkar1a, Prkar2a)
the PKA RIalpha subunit dynamic C helix mediates isoform-specific domain reorganization upon C subunit binding
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. This gene encodes one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Mutations in this gene cause Carney complex (CNC). This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). Several alternatively spliced transcript variants encoding two different isoforms have been observed.
cAMP-dependent protein kinase regulatory subunit RIalpha
, cAMP-dependent protein kinase type I-alpha regulatory chain
, cAMP-dependent protein kinase type I-alpha regulatory subunit
, protein kinase A type 1a regulatory subunit
, tissue-specific extinguisher 1
, protein kinase, cAMP dependent regulatory, type 1, alpha
, protein kinase, cAMP dependent regulatory, type I, alpha
, cAMP-dependent protein kinase type I regulatory subunit
, protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1)
, cAMP-dependent protein kinase, regulatory subunit alpha 1
, cAMP-dependent protein kinase regulatory subunit alpha 1
, cAMP-dependent protein kinase type I-alpha regulatory subunit-like
, protein kinase, cAMP-dependent, regulatory subunit type I alpha S homeolog