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Hydrogen Sulfide Stimulates Cyclic AMP Formation In Mammalian Retina Through the Adenylyl Cyclase Pathway
Author(s) -
NjieMbye Ya Fatou,
Kulkarni Madhura,
Opere Catherine A,
Ohia Sunny E
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.962.2
Subject(s) - forskolin , ibmx , adenylyl cyclase , cyclase , chemistry , adenylate kinase , medicine , endocrinology , activator (genetics) , phosphodiesterase , biochemistry , biology , signal transduction , enzyme , receptor
We tested the hypothesi s that Hydrogen sulfide (H 2 S) stimulates the formation of cyclic AMP (cAMP) in neural retina of pigs and cows via activation of the adenylyl cyclase pathway. Methods Isolated bovine and porcine retina were exposed to H 2 S donors, NaHS, Na 2 S, the cyclic nucleotide phosphodiesterase (PDE) inhibitor, IBMX and/or the diterpene activator of adenylate cyclase, forskolin and prepared for cAMP content by EIA. Results The PDE inhibitor, IBMX (2 mM) caused a two‐three fold increase in basal cAMP levels in bovine and porcine retina respectively. The combination of both IBMX and forskolin (10 μM) produced a synergistic increase ( p < 0.001) in cAMP levels over basal. NaHS (10 nM‐1 μM), and Na 2 S (10 nM‐100 μM) increased cAMP in both tissues. For instance, 100 nM NaHS caused an increase of 20% in bovine retina whilst 1 μM NaHS produced a 15% increase in porcine retina. In bovine and porcine retina, the effects caused by forskolin on cAMP production were not potentiated by addition of low or high concentrations of NaHS or Na 2 S. Conclusions Both NaHS and Na 2 S significantly increased cAMP levels in bovine and porcine retinae indicating that this nucleotide serves as a mediator of effects caused by H 2 S. Furthermore, effects produced by forskolin on cAMP formation were not additive with those elicited by H 2 S donors postulating that these agents may share a common mechanism in their action on the adenylyl cyclase pathway.