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Protein kinase A type I activates a CRE-element more efficiently than protein kinase A type II regardless of C subunit isoform

DOI: 10.1186/1471-2091-12-7

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Abstract:

We show that PKAI when expressed at equal levels as PKAII was significantly (p < 0.01) more efficient in inducing Cre-luciferace activity at saturating concentrations of cAMP. This result was obtained regardless of catalytic subunit identity.We suggest that differential effects of PKAI and PKAII in inducing Cre-luciferace activity depend on R and not C subunit identity.Cyclic 3', 5'-adenosine monophosphate (cAMP) is a key intracellular signaling molecule, which main function is to activate the cAMP-dependent protein kinases (PKA) [1,2]. PKA is a heterotetrameric holoenzyme composed of two regulatory (R) and two catalytic (C) subunits, which is enzymatically inactive in the absence of cAMP. When two molecules of cAMP bind to each of the R subunits [3], the C subunits are released and activated to phosphorylate serine and threonine residues on specific intracellular target proteins [4,5]. Several PKA substrates have been identified of which the synthetic peptide Kemptide [6] and the naturally occurring substrate cAMP responsive element binding protein (CREB) are of the best characterized [7,8]. In primates, four genes encoding the R subunit and four genes encoding the C subunit, have been identified and designated RIα, RIβ, RIIα, RIIβ and Cα, Cβ, Cγ and X-chromosome encoded protein kinase X (PrKX) [9].Whereas no splice variants for RIβ and RIIβ have been described, RIα is transcribed from at least two different promoters. The first exons of the RIα gene, exon 1a and 1b, give rise to alternatively spliced but identical proteins RIα1a and RIα1b [10]. RIα 1a and 1b mRNAs have been identified in most tissues and are differentially regulated by cAMP [11-13]. In the case of RII, it has been shown that RIIα in the human testis but no other tissues examined, is encoded with an alternative amino-terminal region [14]. No functional consequences of alternative splicing of RI and RII have been reported.Several splice variants are transcribed from the Cα and the Cβ genes (PRKCA an

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