Adenosine attenuates oxidant injury in human proximal tubular cells via A(1) and A(2a) adenosine receptors

Am J Physiol Renal Physiol. 2002 May;282(5):F844-52. doi: 10.1152/ajprenal.00195.2001.

Abstract

We have recently demonstrated protection against renal ischemic-reperfusion injury in vivo by A(1)- and A(2a)-adenosine receptor (AR) modulations. To further elucidate the signaling cascades of AR-induced cytoprotection against reperfusion/oxidant-mediated injury, immortalized human proximal tubule (HK-2) cells were treated with H(2)O(2). H(2)O(2) caused dose- and time-dependent HK-2 cell death that was measured by lactate dehydrogenase release and trypan blue dye uptake. Adenosine protected against H(2)O(2)-induced HK-2 cell death by means of A(1)- and A(2a)-AR activation. A(1)-AR-mediated protection involves pertussis toxin-sensitive G proteins and protein kinase C, whereas A(2a)-AR-mediated protection involves protein kinase A activation by means of cAMP and activation of the cAMP response element binding protein. Moreover, protein kinase A activators (forskolin and Sp-isomer cAMP) also protected HK-2 cells against H(2)O(2) injury. De novo gene transcription and protein synthesis are required for both A(1)- and A(2a)-AR-mediated cytoprotection as actinomycin D and cycloheximide, respectively, blocked cytoprotection. Chronic treatments with a nonselective AR agonist abolished the protection by adenosine. Moreover, chronic treatments with a nonselective AR antagonist increased the endogenous tolerance of HK-2 cells against H(2)O(2). We concluded that A(1)- and A(2a)-AR activation protects HK-2 cells against H(2)O(2)-induced injury by means of distinct signaling pathways that require new gene transcription and new protein synthesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine / pharmacology*
  • Cell Death / drug effects*
  • Cell Line, Transformed
  • Coloring Agents
  • Cyclic AMP Response Element-Binding Protein / physiology
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Cycloheximide / pharmacology
  • Dactinomycin / pharmacology
  • Enzyme Activation / drug effects
  • Humans
  • Hydrogen Peroxide / pharmacology
  • Kidney Tubules, Proximal / cytology*
  • L-Lactate Dehydrogenase / metabolism
  • Nucleic Acid Synthesis Inhibitors / pharmacology
  • Oxidative Stress*
  • Protein Kinase C / metabolism
  • Protein Synthesis Inhibitors / pharmacology
  • Purinergic P1 Receptor Antagonists
  • Receptor, Adenosine A2A
  • Receptors, Purinergic P1 / physiology*
  • Reperfusion Injury / prevention & control
  • Signal Transduction
  • Trypan Blue / metabolism

Substances

  • Coloring Agents
  • Cyclic AMP Response Element-Binding Protein
  • Nucleic Acid Synthesis Inhibitors
  • Protein Synthesis Inhibitors
  • Purinergic P1 Receptor Antagonists
  • Receptor, Adenosine A2A
  • Receptors, Purinergic P1
  • Dactinomycin
  • Cycloheximide
  • Hydrogen Peroxide
  • L-Lactate Dehydrogenase
  • Cyclic AMP-Dependent Protein Kinases
  • Protein Kinase C
  • Trypan Blue
  • Adenosine