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the present study reported for the first time an intronic splice site mutation in the PRKAR1A (show PRKAR1A Proteins) 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 (show PRKAR1A Proteins) gene in a patient with Carney complex who presented with significant osteoporosis and fractures.
a significant association between PKR2 rs6053283 polymorphism and Recurrent pregnancy loss (RPL)(P=0.003), whereas no association was observed between PKR1 rs4627609 polymorphism and RPL (P=0.929) in the Chinese Han population.
Letter/Case Report: novel PRKAR1A (show PRKAR1A Proteins) mutation resulting in a splicing variant in a case of Carney complex.
Data suggest that prokineticins (PROK1 (show Prok1 Proteins) and PROK2 (show PROK2 Proteins)) and prokineticin receptors (PROKR1 and PROKR2 (show PROKR2 Proteins)) act as main regulators of physiological functions of ovary, uterus, placenta, and testis. [REVIEW]
EG-VEGF (show Prok1 Proteins) and its receptor PKR1 might play a role in the pathogenesis of adrenocortical tumors and could serve as prognostic markers for this rare malignant disease.
P-Rex1 contributes to the spatiotemporal localization of type I PKA, which tightly regulates this guanine exchange factor by a multistep mechanism.
In the absence of a PRKAR1A (show PRKAR1A Proteins) gene mutation, our Cushing's syndrome patients do not fit the criteria for Carney's complex
Case Report: although there was no family history of any of the Carney complex features and no mutations in the PRKAR1A (show PRKAR1A Proteins) gene were found, findings lead to the diagnosis of sporadic Carney complex.
this study evaluated the functional characteristics of PRKAR1A (show PRKAR1A Proteins) regulatory subunits carrying eight different mutations identified in patients with acrodysostosis and compared the results with those obtained for the two alternative mutations involved in the Carney complex
show that MRAP2 significantly and specifically inhibits PKR1 signaling.
Data show that the prokineticins and their receptors PROK2 (show PROK2 Proteins), PKR1 and PKR2 (show PROKR2 Proteins) contributes to altered sensitivity in diabetic neuropathy and its inhibition blocked both allodynia and inflammatory events underlying disease.
These results suggest PKR1 to be a crucial player in the preadipocyte proliferation and differentiation.
Loss of PKR1 causes renal and cardiac structural and functional changes because of deficits in survival signaling, mitochondrial, and progenitor cell functions in found both organs.
The functional characteristics of coronary endothelial cells depend on the expression of PKR1 and PKR2 (show PROKR2 Proteins) levels and the divergent signaling pathways used by these receptors.
Identification and molecular characterization of two closely related G protein-coupled receptors (prokineticin receptor)
PKR1 protein was localised to the labyrinth layer and showed the same pattern of expression as EG-VEGF (show Prok1 Proteins) in mouse placenta.
Cardiomyocyte-PKR1 signaling upregulates its own ligand prokineticin-2 (show PROK2 Proteins) that acts as a paracrine factor, triggering epicardial-derived progenitor cell proliferation/differentiation.
Data show that the inflammation-induced up-regulation of PK2 (show PROK2 Proteins) was significantly less in pkr1 null mice than in WT and pkr2 (show PROKR2 Proteins) null mice, demonstrating a role of PKR1 in setting PK2 (show PROK2 Proteins) levels during inflammation.
PROK1 (show Prok1 Proteins), acting via PROKR1, may be involved in the recruitment of monocytes to regressing CL and atretic follicles and their consequent activation therein.
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.
prokineticin receptor 1
, G protein-coupled receptor 73
, prokineticin receptor 1-like
, G protein-coupled receptor ZAQ
, G-protein coupled receptor 73
, G-protein coupled receptor ZAQ
, 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