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PubMed1980

Frequency-domain analysis of the human electroretinogram.

Normal corneal electroretinograms (ERG) are analyzed in the frequency domain using the fast Fourier transform (FFT) and linear prediction (LP) methods. Four dominant frequencies at 18, 79, 126, and 159 Hz are found in the dark-adapted state. Light adaptation shifts the low frequency to higher frequency and the mid- and the two high-frequency components to lower frequencies. The relative amplitude of the high-frequency component resulting from the oscillatory potentials is quantified. It is shown that frequency-domain features are of a smaller variability than time-domain components, and can be extracted even from a noisy surface ERG.

Adaptation, Ocular↗
PubMed1996

Light and dark cause a shift in the spatial expression of a neuropeptide-processing enzyme in the rat retina.

Carboxypeptidase E (CPE, EC 3.4.17.10) is an essential enzyme in the post-translational processing of most neuroactive peptides. We have studied how the expression of CPE in the rat retina is modified in response to the light/dark cycle. Retinal CPE mRNA levels increase immediately after a change in lighting condition. After prolonged exposure to the dark or the light, however, CPE mRNA levels drop to comparable amounts. The increase CPE mRNA is most dramatic during the dark-to-light transition. Interestingly, during the same interval, CPE protein levels transiently decrease. This apparently contradictory change in mRNA and protein levels is attributable to a change in the spatial pattern of CPE expression in the retina in response to light and dark. Both in situ hybridization and indirect immunofluorescence studies indicate that CPE is expressed in photoreceptors in the dark. During light onset, CPE expression is rapidly induced in retinal ganglion cells, whereas expression in photoreceptors is reduced. This pattern is reversed when the animals are exposed to the dark. In contrast, CPE is apparently constitutively expressed in a subpopulation of cells in the inner nuclear layer in both the light and the dark. These changes in CPE expression are similar to light-induced changes in c-fos expression, suggesting that CPE may be a downstream target for Fos activation.

Adaptation, Ocular↗
PubMed1998

Bleached pigment produces a maintained decrease in outer segment Ca2+ in salamander rods.

A spot confocal microscope based on an argon ion laser was used to make measurements of cytoplasmic calcium concentration (Ca2+i) from the outer segment of an isolated rod loaded with the fluorescent calcium indicator fluo-3 during simultaneous suction pipette recording of the photoresponse. The decline in fluo-3 fluorescence from a rod exposed to saturating illumination was best fitted by two exponentials of approximately equal amplitude with time constants of 260 and 2,200 ms. Calibration of fluo-3 fluorescence in situ yielded Ca2+i estimates of 670 +/- 250 nM in a dark-adapted rod and 30 +/- 10 nM during response saturation after exposure to bright light (mean +/- SD). The resting level of Ca2+i was significantly reduced after bleaching by the laser spot, peak fluo-3 fluorescence falling to 56 +/- 5% (SEM, n = 9) of its value in the dark-adapted rod. Regeneration of the photopigment with exogenous 11-cis-retinal restored peak fluo-3 fluorescence to a value not significantly different from that originally measured in darkness, indicating restoration of the dark-adapted level of Ca2+i. These results are consistent with the notion that sustained activation of the transduction cascade by bleached pigment produces a sustained decrease in rod outer segment Ca2+i, which may be responsible for the bleach-induced adaptation of the kinetics and sensitivity of the photoresponse.

Adaptation, Ocular↗