Ca2+-binding proteins (CaBP) alter Ca2+ signals, triggering cellular processes such as gene transcription regulation in neurons. CaBP1/CD is a calmodulin (CaM)-like Ca2+ binding protein that may regulate neuronal functions through interactions with effectors such as voltage-gated Ca2+ (Cav) channels and inositol trisphosphate receptors (InsP3Rs). To gain insight into the potential cellular functions of CaBP1/CD, we analyzed the expression and localization of CaBP1/CD variants in mouse brain. Of the three CaBP1/CD splice variants that have been characterized (CaBP1-S, CaBP1-L, and caldendrin (CD)), CD was the major variant expressed in mouse brain by western blot and quantitative polymerase chain reaction. These results reflected the expression of CaBP1/CD since they were not reproduced in mice with targeted disruption of the gene encoding CaBP1/CD (CaBP1 knock-out). By immunoperoxidase labeling, CaBP1/CD was localized in multiple cell-types including pyramidal cells in the cerebral cortex and hippocampal CA3 neurons and inhibitory neurons in the cerebellum. In the cerebellum, CaBP1/CD was not detected in Purkinje neurons but strongly colocalized with voltage-sensitive Shaker-type potassium channel, Kv1.2, in the pinceau formation formed between basket cells and the Purkinje cell axon initial segment. We conclude that CaBP1/CD is expressed in a subset of principal neurons where it may regulate Ca2+ signaling and neuronal excitability.
Thesis
Characterization of calcium binding protein 1 (CaBP1/CD) expression and localization in the mouse brain
University of Iowa
Master of Science (MS), University of Iowa
Spring 2013
DOI: 10.17077/etd.idp2t7s8
Free to read and download, Open Access
Abstract
Details
- Title: Subtitle
- Characterization of calcium binding protein 1 (CaBP1/CD) expression and localization in the mouse brain
- Creators
- Kristin Kim - University of Iowa
- Contributors
- Amy Lee (Advisor)N. Charles Harata (Committee Member)C. Andrew Frank (Committee Member)
- Resource Type
- Thesis
- Degree Awarded
- Master of Science (MS), University of Iowa
- Degree in
- Molecular Physiology and Biophysics
- Date degree season
- Spring 2013
- Publisher
- University of Iowa
- DOI
- 10.17077/etd.idp2t7s8
- Number of pages
- vii, 38 pages
- Copyright
- Copyright © 2013 Kristin Kim
- Comment
This thesis has been optimized for improved web viewing. If you require the original version, contact the University Archives at the University of Iowa: https://www.lib.uiowa.edu/sc/contact/.
- Language
- English
- Description illustrations
- illustrations (some col.)
- Description bibliographic
- Includes bibliographical references (pages 34-38).
- Academic Unit
- Molecular Physiology and Biophysics
- Record Identifier
- 9983777240902771
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