March 1991
Volume 32, Issue 3
Free
Articles  |   March 1991
Lens beta-adrenergic receptors. Functional coupling to adenylate cyclase and photoaffinity labeling.
Author Affiliations
  • M E Ireland
    Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, MI 48201.
  • S Shanbom
    Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, MI 48201.
Investigative Ophthalmology & Visual Science March 1991, Vol.32, 541-548. doi:
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      M E Ireland, S Shanbom; Lens beta-adrenergic receptors. Functional coupling to adenylate cyclase and photoaffinity labeling.. Invest. Ophthalmol. Vis. Sci. 1991;32(3):541-548.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Beta-adrenergic drugs affect lens epithelial and fiber cells. The regulation and cellular integration of lens beta-adrenergic responses are largely unknown. These studies further characterize beta-adrenergic receptors in lens cells with respect to cyclic adenosine monophosphate (cAMP) production and identification of receptor polypeptides. Stimulation of beta-adrenergic receptors in organ-cultured chick lenses resulted in dose-dependent increases in intracellular cAMP levels. Isoproterenol-elicited cAMP accumulation was found in both epithelial/superficial fiber cells and cortical fiber cells. Hormonal stimulation also apparently initiated additional mechanisms involved in the regulation of cAMP levels (ie, phosphodiesterase activation/receptor desensitization). Individual receptor polypeptides were identified in epithelial and fiber membranes with the photoaffinity probe 125I-iodocyanopindolol diazarine. The probe specifically labeled distinct populations of receptor polypeptides in the two cell types. Lens beta-adrenergic receptors were also shown to bind (-) stereoisomers of adrenergic ligands preferentially. These results indicate that differentiating fiber cells are hormonally sensitive to beta-adrenergic stimulation and that epithelial and fiber cells may respond differentially to beta-adrenergic drugs, at least in part, because of their distinct receptor polypeptides.

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