Lack of CaBP1/Caldendrin or CaBP2 Leads to Altered Ganglion Cell Responses
Calcium-binding proteins (CaBPs) form a subfamily of calmodulin-like proteins that were cloned from the retina. CaBP4 and CaBP5 have been shown to be important for normal visual function. Although CaBP1/caldendrin and CaBP2 have been shown to modulate various targets , it is not known whether they c...
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Published in | eNeuro Vol. 3; no. 5; p. ENEURO.0099-16.2016 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Society for Neuroscience
01.09.2016
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Subjects | |
Online Access | Get full text |
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Summary: | Calcium-binding proteins (CaBPs) form a subfamily of calmodulin-like proteins that were cloned from the retina. CaBP4 and CaBP5 have been shown to be important for normal visual function. Although CaBP1/caldendrin and CaBP2 have been shown to modulate various targets
, it is not known whether they contribute to the transmission of light responses through the retina. Therefore, we generated mice that lack CaBP2 or CaBP1/caldendrin (
and
) to test whether these CaBPs are essential for normal retinal function. By immunohistochemistry, the overall morphology of
and
retinas and the number of synaptic ribbons appear normal; transmission electron microscopy shows normal tethered ribbon synapses and synaptic vesicles as in wild-type retinas. However, whole-cell patch clamp recordings showed that light responses of retinal ganglion cells of
and
mice differ in amplitude and kinetics from those of wild-type mice. We conclude that CaBP1/caldendrin and CaBP2 are not required for normal gross retinal and synapse morphology but are necessary for the proper transmission of light responses through the retina; like other CaBPs, CaBP1/caldendrin and CaBP2 likely act by modulating presynaptic Ca
-dependent signaling mechanisms. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 The authors report no conflict of interest. The research was supported by a University of Washington Royalty Research Fund, University of Washington bridge funding, and National Institutes of Health (NIH) grant R01 EY020850 to F.H.; the Howard Hughes Medical Institute and NIH grant EY11850 to F.R.; NIH grants NS084190 and DC009433 and a Carver Research Program of Excellence to A.L.; and a long-term fellowship by Human Frontier Science Program to R.S. Author Contributions: R.S., F.R., and F.H. designed and performed research and analyzed the data. A.L. contributed unpublished reagents. All authors contributed to writing and approval of the final manuscript. |
ISSN: | 2373-2822 2373-2822 |
DOI: | 10.1523/ENEURO.0099-16.2016 |