We investigated by immunohistochemistry (IHC) the distribution of caldendrin, the founding member of a novel family of neuronal calcium-binding proteins closely related to calmodulin, in human forebrain. Caldendrin immunoreactivity was unevenly distributed, with prominent staining in the paleo- and neocortex, hippocampus, and hypothalamus. With the exception of the hypothalamus, labeling was restricted to the somato-dendritic compartment of neurons. This distribution completely matches that reported in rat, indicating that the cellular function is most likely conserved among species. Therefore, one prerequisite for functional studies in rodent models aimed at elucidation of mechanisms with relevance for humans can be based on the present findings.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1177/002215540305100816 | DOI Listing |
Schizophr Res
November 2007
Department of Psychiatry, Faculty of Medicine, Otto-von-Guericke University, Leipziger Str. 44, 39120 Magdeburg, Germany.
Caldendrin is a neuronal calcium sensor protein that is tightly associated with the postsynaptic density (PSD) of excitatory synapses. It has an established role in synapto-dendritic Ca(2+)-signaling as a multifunctional regulator of intracellular Ca(2+) levels. Previous work has shown that expression levels of protein components involved in signaling processes at excitatory synapses are significantly altered in the brains of schizophrenic patients.
View Article and Find Full Text PDFJ Comp Neurol
November 2004
Department Biology, University of Oldenburg, 26111 Oldenburg, Germany.
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.
View Article and Find Full Text PDFJ Histochem Cytochem
August 2003
Department of Psychiatry, Otto-von-Guericke-University, Magdeburg, Germany.
We investigated by immunohistochemistry (IHC) the distribution of caldendrin, the founding member of a novel family of neuronal calcium-binding proteins closely related to calmodulin, in human forebrain. Caldendrin immunoreactivity was unevenly distributed, with prominent staining in the paleo- and neocortex, hippocampus, and hypothalamus. With the exception of the hypothalamus, labeling was restricted to the somato-dendritic compartment of neurons.
View Article and Find Full Text PDFAdv Exp Med Biol
July 2003
AG Molecular of Plasicity, Department of Neurochemistry/Molecular Biology, Leibnitz Institute for Neurobiology, 39118 Magdeburg, Germany.
Caldendrin is the first member of a novel family of Ca2+-binding proteins (CaBPs). Its unique two-domain structure is composed of a calmodulin-homologous teminus and an unrelated N-terminal part. The latter is thought to mediate the tight association of caldendrin with the subsynaptic cytoskeleton.
View Article and Find Full Text PDFJ Comp Neurol
January 2003
Max-Planck-Institut für Hirnforschung, D-60528 Frankfurt/Main, Germany.
With the ever-growing number of transgenic mice being used in vision research, a precise knowledge of the cellular organization of the mouse retina is required. As with the cat, rabbit, rat, and primate retinae, as many as 10 cone bipolar types and one rod bipolar type can be expected to exist in the mouse retina; however, they still have to be defined. In the current study, several immunocytochemical markers were applied to sections of mouse retina, and the labeling of bipolar cells was studied using confocal microscopy and electron microscopy.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!