The influence of cyclic AMP upon Na,K-ATPase activity in rabbit ciliary epithelium.
ATPase activity was measured in samples of freshly dissected rabbit ciliary epithelium. The epithelium was ruptured in distilled water, frozen briefly, and incubated at 37 degrees C in a buffer containing 100 mM NaCl and 32P-labeled adenosine triphosphate (ATP). The rate of ATP hydrolysis by the epithelium was linear for as long as 45 min. Ouabain (1 mM) reduced the ATP hydrolysis rate by approximately 50%. When the epithelium was preincubated for 10 min. in the presence of 1 mM dibutyryl cyclic adenosine monophosphate (cAMP), the ouabain-sensitive (Na,K-ATPase) activity was diminished; ouabain-insensitive ATPase activity was not reduced. Preincubation of the epithelium with forskolin with isobutylmethylxanthine also reduced ouabain-sensitive ATPase activity. These observations suggest that the ciliary epithelium may have a mechanism for short-term modulation of Na,K-ATPase activity by cAMP. Such a mechanism could be linked to the ability of cAMP-dependent protein kinase to reduce Na,K-ATPase activity in the tissue.
Delamere
N A
NA
Department of Ophthalmology and Visual Sciences, Kentucky Lions Eye Research Institute, University of Louisville School of Medicine.
King
K L
KL
D000255:Adenosine Triphosphate / Q000037:antagonists & inhibitors / Q000378:metabolism; D000818:Animals; D003994:Bucladesine / Q000494:pharmacology*; D002924:Ciliary Body / Q000187:drug effects* / Q000201:enzymology / Q000648:ultrastructure; D005576:Colforsin / Q000494:pharmacology; D004848:Epithelium / Q000187:drug effects / Q000201:enzymology / Q000648:ultrastructure; D006868:Hydrolysis; D010042:Ouabain / Q000494:pharmacology; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D005576:Colforsin; D010042:Ouabain; D003994:Bucladesine; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase