Abstract
Human retinal pigment epithelial cells in culture demonstrate adenylate cyclase activity. It is membrane-bound and modulated by GTP regulatory proteins. It is effectively activated only by beta-adrenergic agonists (l-isoproterenol ≥ l-epinephrine > l-norepinephrine) and some prostaglandins (PGE1 and PGE2, but not PGF1α). The adrenergic response appears to be mediated by beta-2 receptors. No inhibitory ligands could be demonstrated. Its characteristics, which are similar to functional adenylate cyclase complexes in other mammalian cells, and its selective and sensitive agonist responsiveness, suggest a possible physiologic role in the regulation of human retinal pigment epithelial-cell function.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 471-479 |
| Number of pages | 9 |
| Journal | Experimental eye research |
| Volume | 44 |
| Issue number | 4 |
| DOIs | |
| State | Published - 1987 |
| Externally published | Yes |
Keywords
- adenylate cyclase
- beta-adrenergies
- cAMP
- prostaglandins
- retinal pigment epithelium
ASJC Scopus subject areas
- Ophthalmology
- Sensory Systems
- Cellular and Molecular Neuroscience
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