High impact information on Prkar1b

• Surprisingly, all stimulate tyrosine phosphorylation of Fc epsilon RI beta, Syk, and linker for activation of T cells to similar extents as multivalent Ag at optimal ligand concentrations [1].
• Several of the same proteins including Fc epsilon RI beta, Fc epsilon RI gamma, p72syk, and phospholipase C-gamma 1 were tyrosine-phosphorylated by mAb AA4 binding and by the activation of the high affinity IgE receptor, Fc epsilon RI [2].
• Mast cells in the skin of +/+ rats express messenger RNA of Fc epsilon RI beta-subunit and c-kit protein [3].
• Furthermore, the purified recombinant RI beta protein was shown to exist as a dimer that was able to form holoenzyme with the catalytic subunit C alpha [4].
• The subcellular localization of RI beta was analyzed in quiescent REF-52 fibroblasts and Wistar rat thyroid (WRT) cells after microinjection of fluorescently labeled proteins into the cytoplasm [4].

Biological context of Prkar1b

• The largest open reading frame was preceded by a short out-of-phase open reading frame, which is not seen in the corresponding mouse RI beta cDNA due to a single base substitution [5].
• A tentative explanation is related to the different biochemical properties of the four regulatory subunit isoforms (RI alpha and RI beta, RII alpha and RII beta) and to their differential cell and tissue distribution [6].
• In this study, we document the presence of significant mRNA levels for 5 different PKA subunits (RI alpha, RI beta, RII alpha, RII beta, and C alpha) in germ cells and demonstrate differential expression patterns for these subunits during spermatogenesis [7].
• Messenger RNAs for RI (RI alpha and RI beta) and C alpha appear to be induced at premeiotic germ cell stages, whereas mRNAs for RII (RII alpha and RII beta) are first expressed at haploid stages [7].
• Cells also were treated with either phorbol-12-myristate-13-acetate or dibutyryl-cAMP, and the gene expression for RI alpha, RI beta, RII alpha and RII beta of PKA was examined [8].

Anatomical context of Prkar1b

• Rat RI beta mRNA was abundant in adult rat brain and testis but was undetectable in other rat tissues [5].
• C alpha, C beta, RI alpha, RI beta, RII alpha, and RII beta mRNAs were all present in the anterior pituitary gland and cultured cells, but in different proportions; C alpha was the most abundant, and RII alpha was the least [9].
• RI beta mRNA was detected over late pachytene spermatocytes and round spermatids of stages VII-XIII [10].

Associations of Prkar1b with chemical compounds

• Rat RI beta isoform of type I regulatory subunit of cyclic adenosine monophosphate-dependent protein kinase: cDNA sequence analysis, mRNA tissue specificity, and rat/mouse difference in expression in testis [5].

Regulatory relationships of Prkar1b

• CONCLUSIONS: The reduction of the RI beta subunit in the rat DF at day 3 may result in an elevated PKA activity to trigger the maximal burst of gene expression of MCP-1 and CSF-1 seen at this time [8].

Other interactions of Prkar1b

• None of the antipsychotics caused any change in the expression of the Cat alpha-, RI alpha-, or RI beta-subunit isoform [11].
• However, aggregation of TEC-21 did not induce changes in density of IgE-Fc epsilon RI complexes, tyrosine phosphorylation of Fc epsilon RI beta and gamma subunits, and co-aggregation of Lyn kinase [12].
• Based upon recent reports that the rat testis exhibits mRNAs for cAMP-dependent protein kinase (A-kinase) regulatory (R) subunits RI alpha, RI beta, RII alpha, and RII beta, this study was designed to identify R proteins present in extracts of germ cell-rich testis from adult and Sertoli cell-enriched, germ cell-poor testis from 14-15-day-old rats [13].

Analytical, diagnostic and therapeutic context of Prkar1b

• Moreover no Fc epsilon RI beta-subunit-expressing and no c-kit-expressing cells were detectable in the skin of Ws/Ws rats by in situ hybridization histochemistry [3].
• Because c-kit messenger RNA was normally expressed at least in the brain of Ws/Ws rats despite the small deletion, we examined the expression of Fc epsilon RI beta-subunit and c-kit messenger RNA in the skin and stomach of Ws/Ws rats by reverse transcriptase modification of polymerase chain reaction [3].
• The human recombinant RI beta protein migrated at 55 kDa on SDS-PAGE and displayed immunoreactivity with an anti-human RI beta antiserum [4].
• For C alpha, C beta, RI beta, and RII alpha, Northern blot analysis revealed single mRNAs with sizes of 2.4, 4.5, 2.8, and 6.0 kilobases (kb), respectively [9].
• The 53 kDa RI beta protein predicted by mRNA studies was only tentatively identified by Western blot analysis [13].

References