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PubMed1982

The effects of local anaesthetics on retinal function.

Isolated frog eyecups were incubated in Ringer containing local anaesthetics to study the effects of these drugs on dark-adaptation of the ERG. Relative to controls, dark-adaptation in eyecups treated with millimolar concentrations of MS-222, benzocaine, and procaine HCl was significantly inhibited during 10 to 120 min following the cessation of the adapting light. These drugs also prevented the recovery of the c-wave during dark-adaptation, resulting in ERG waveforms resembling those found in light-adapted eyecups. Measurements of rhodopsin in the retina were consistent with previous findings showing that rhodopsin regeneration in situ is inhibited by local anaesthetics. In vitro regeneration experiments in which bleached rod outer segment fragments were added to 11-cis retinal showed that preincubation of retinal with MS-222 in ethanol prevents rhodopsin regeneration. Evidence was obtained spectrophotometrically for the formation of a complex between MS-222 and 11-cis retinal with a gamma max of 512 nm. We propose that the formation of a Schiff's base between these two compounds blocks the recombination of rhodopsin, and in situ, leads to the inhibition of dark-adaptation.

Aminobenzoates↗
PubMed1982

Inhibition of rhodopsin regeneration by cyclohexyl derivatives.

Twenty two compounds, bearing some structural similarity either to the ring-end or aldehyde-end of 11-cis-retinal, have been screened for their effectiveness in decreasing the rate of regeneration of rhodopsin in vitro from 11-cis retinal and bovine opsin. The results of these experiments indicate that only those compounds containing a ring and having at least two methyl groups at the 1,5-ring positions are capable of decreasing the rate of regeneration of rhodopsin. Short-chain aldehydes resembling the aldehyde-end of retinal did not affect the rate of pigment formation. There was no additive effect of combining a dimethylcyclohexyl inhibitor and a short chain aldehyde. The methyl groups at the 1,5-positions may play a special role in anchoring the retinal into the protein binding site. This hypothesis is supported by the failure of the ring demethylated analogue, 11-cis, 1,1,5-desmethyl-5,6-dihydroretinal, to form pigment under the same conditions with which good pigment yields are obtained with 11-cis 5,6-dihydroretinal.

Binding Sites↗