TAILIEUCHUNG - Báo cáo khoa học: Inactive forms of the catalytic subunit of protein kinase A are expressed in the brain of higher primates

It is well documented that theb-gene of the catalytic (C) subunit of protein kinase A encodes a number of splice variants. These splice variants are equipped with a variable N-terminal end encoded by alternative use of sev-eral exons located 5¢ to exon 2 in the human, bovine and mouse Cbgene. | ễFEBS Journal Inactive forms of the catalytic subunit of protein kinase A are expressed in the brain of higher primates Anja C. V. Larsen1 Anne-Katrine Kvissel1 2 Tilahun T. Hafte1 Cecilia I. A. Avellan1 2 Sissel Eikvar1 2 Terje Rootwelt3 Sigurd 0rstavik1 4 and Bj0rn S. Skalhegg1 1 Department of Nutrition Institute for Basic MedicalSciences University of Oslo Norway 2 Department of Biochemistry Institute for Basic MedicalSciences University of Oslo Norway 3 The Department of Pediatric Research Rikshospitalet Oslo Norway 4 Cancer Centre Ulleval University Hospital Oslo Norway Keywords Cp splice variants exon skipping neuronal splicing NT2 neurones protein kinase A Correspondence B. S. Skalhegg Department of Nutrition Institute for Basic Medical Sciences University of Oslo PO Box 1046 Blindern N-0316 Oslo Norway Fax 47 22851531 Tel 47 22851548 E-mail Received 14 August 2007 revised 1 November 2007 accepted 16 November 2007 doi It is well documented that the p-gene of the catalytic C subunit of protein kinase A encodes a number of splice variants. These splice variants are equipped with a variable N-terminal end encoded by alternative use of several exons located 5 to exon 2 in the human bovine and mouse Cp gene. In the present study we demonstrate the expression of six novel human Cp mRNAs that lack 99 bp due to loss of exon 4. The novel splice variants designated CpA4 were identified in low amounts at the mRNA level in NTera2-N cells. We developed a method to detect CpA4 mRNAs in various cells and demonstrated that these variants were expressed in human and Rhesus monkey brain. Transient expression and characterization of the CpA4 variants demonstrated that they are catalytically inactive both in vitro against typical protein kinase A substrates such as kemptide and histone and in vivo against the cAMP-responsive element binding protein. Furthermore co-expression of CpA4 with the regulatory subunit R .

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