Calcium-binding protein Caldendrin and CaMKII are localized in spinules of the carp retina

The Journal of Comparative Neurology
K SchultzR Weiler

Abstract

Calcium-binding proteins translate the influx of Ca(2+) at excitatory synapses into spatiotemporal signals that regulate a variety of processes underlying synaptic plasticity. In the fish retina, the synaptic connectivity between photoreceptors and horizontal cells undergoes a remarkable plasticity, triggered by the ambient light conditions. With increasing light, the synaptic dendrites of horizontal cells form numerous spinules that are dissolved during dark adaptation. The dynamic regulation of this process is calcium-dependent and involves the Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), but astonishingly its principal regulator Calmodulin (CaM) could not be localized to spinules. Here, we show that antibodies directed against Caldendrin (CaBP1), a member of the EF-hand calcium-binding protein family, strongly label the terminal dendrites of horizontal cells invaginating cone pedicles. Double-labeling experiments revealed that this label is closely associated with label for CaMKII. This association was confirmed at the ultrastructural level. Caldendrin immunoreactivity and CaMKII immunoreactivity are both present in horizontal cell dendrites flanking the synaptic ribbon within the cone pedicle and in particular in...Continue Reading

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Oct 24, 2006·Biochimica Et Biophysica Acta·Marina MikhaylovaMichael R Kreutz
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