Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 486, Issue 1, Pages 44-50Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2009.03.008
Keywords
Inosine; Adenosine; Renal tissue; Proximal tubule; Kidney; Protein kinase; Purine receptor; cAMP; Cell signaling; Adenosine deaminase
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Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico - CNPq
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior - CAPES
- Fundacao Carlos Chagas Filho de Amparo a Pesquisa do Estado do Rio de Janeiro - FAPERJ
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In this work, the metabolism of adenosine by isolated BLM associated-enzymes and the implications of this process for the cAMP-signaling pathway are investigated. Inosine was identified as the major metabolic product, suggesting the presence of adenosine deaminase (ADA) activity in the BLM. This was confirmed by immunoblotting and ADA-specific enzyme assay. Implications for the enzymatic deamination of adenosine on the receptor-modulated cAMP-signaling pathway were also investigated. We observed that inosine induced a 2-fold increase in [S-35] GTP gamma S binding to the BLM and it was inhibited by 10(-6) M DPCPX, and A(1) receptor-selective antagonist. Inosine (10(-7) M) inhibited protein kinase A activity in a DPCPX-sensitive manner. Molecular association between ADA and G(alpha i-3) protein-coupled A(1) receptor was demonstrated by co-immunoprecipitation assay. These data show that adenosine is deaminated by A(1) receptor-associated ADA to inosine, which in turn modulates PKA in the BLM through A(1) receptor-mediated inhibition of adenylyl cyclase. (C) 2009 Elsevier Inc. All rights reserved.
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