title: Expression and Localization of CaBP Ca2+ Binding Proteins in the Mouse Cochlea.
abstract: CaBPs are a family of EF-hand Ca2+ binding proteins that are structurally similar to calmodulin. CaBPs can interact with, and yet differentially modulate, effectors that are regulated by calmodulin, such as Cav1 voltage-gated Ca2+ channels. Immunolabeling studies suggest that multiple CaBP family members (CaBP1, 2, 4, and 5) are expressed in the cochlea. To gain insights into the respective auditory functions of these CaBPs, we characterized the expression and cellular localization of CaBPs in the mouse cochlea. By quantitative reverse transcription PCR, we show that CaBP1 and CaBP2 are the major CaBPs expressed in mouse cochlea both before and after hearing onset. Of the three alternatively spliced variants of CaBP1 (caldendrin, CaBP1-L, and CaBP1-S) and CaBP2 (CaBP2-alt, CaBP2-L, CaBP2-S), caldendrin and CaBP2-alt are the most abundant. By in situ hybridization, probes recognizing caldendrin strongly label the spiral ganglion, while probes designed to recognize all three isoforms of CaBP1 weakly label both the inner and outer hair cells as well as the spiral ganglion. Within the spiral ganglion, caldendrin/CaBP1 labeling is associated with cells resembling satellite glial cells. CaBP2-alt is strongly expressed in inner hair cells both before and after hearing onset. Probes designed to recognize all three variants of CaBP2 strongly label inner hair cells before hearing onset and outer hair cells after the onset of hearing. Thus, CaBP1 and CaBP2 may have overlapping roles in regulating Ca2+ signaling in the hair cells, and CaBP1 may have an additional function in the spiral ganglion. Our findings provide a framework for understanding the role of CaBP family members in the auditory periphery.
authors.affiliation: Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa, United States of America.|Department of Otolaryngology Head-Neck Surgery, University of Iowa, Iowa City, Iowa, United States of America.|Department of Neurology, University of Iowa, Iowa City, Iowa, United States of America.
authors.forename: Tian
authors.initials: T
authors.lastname: Yang
authors.affiliation: Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa, United States of America.|Department of Otolaryngology Head-Neck Surgery, University of Iowa, Iowa City, Iowa, United States of America.|Department of Neurology, University of Iowa, Iowa City, Iowa, United States of America.
authors.forename: Elizabeth S
authors.initials: ES
authors.lastname: Scholl
authors.affiliation: Department of Biology, University of Iowa, Iowa City, Iowa, United States of America.
authors.forename: Ning
authors.initials: N
authors.lastname: Pan
authors.affiliation: Department of Otolaryngology Head-Neck Surgery, University of Iowa, Iowa City, Iowa, United States of America.|Department of Biology, University of Iowa, Iowa City, Iowa, United States of America.
authors.forename: Bernd
authors.initials: B
authors.lastname: Fritzsch
authors.affiliation: Department of Physiology and Biophysics, University of Washington, Seattle, Washington, United States of America.
authors.forename: Françoise
authors.initials: F
authors.lastname: Haeseleer
authors.affiliation: Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa, United States of America.|Department of Otolaryngology Head-Neck Surgery, University of Iowa, Iowa City, Iowa, United States of America.|Department of Neurology, University of Iowa, Iowa City, Iowa, United States of America.
authors.forename: Amy
authors.initials: A
authors.lastname: Lee
mesh_terms: D000818:Animals; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D003051:Cochlea / Q000378:metabolism*; D006199:Hair Cells, Auditory, Inner / Q000378:metabolism; D018072:Hair Cells, Auditory, Outer / Q000378:metabolism; D017403:In Situ Hybridization; D051379:Mice; D020033:Protein Isoforms / Q000378:metabolism*; D013136:Spiral Ganglion / Q000378:metabolism
chemical_list: D002135:Calcium-Binding Proteins; D020033:Protein Isoforms; C085577:Ca2+-binding protein-1
references.citation: Nat Neurosci. 2004 Oct;7(10):1079-87
references.pmid: 15452577
references.citation: J Neurosci. 2004 May 12;24(19):4698-708
references.pmid: 15140941
references.citation: J Biol Chem. 1998 Aug 14;273(33):21324-31
references.pmid: 9694893
references.citation: Brain Res Brain Res Rev. 2005 Jun;48(3):457-76
references.pmid: 15914252
references.citation: J Biol Chem. 2005 Aug 19;280(33):29612-9
references.pmid: 15980432
references.citation: J Neurosci. 2006 Oct 18;26(42):10677-89
references.pmid: 17050707
references.citation: J Biol Chem. 2007 Mar 16;282(11):8464-73
references.pmid: 17224447
references.citation: J Neurosci. 2007 Jun 13;27(24):6442-51
references.pmid: 17567805
references.citation: J Physiol. 2007 Sep 15;583(Pt 3):909-22
references.pmid: 17656437
references.citation: J Physiol. 2007 Dec 15;585(Pt 3):791-803
references.pmid: 17947313
references.citation: J Neurophysiol. 2008 May;99(5):2183-93
references.pmid: 18322004
references.citation: Nature. 2009 Oct 22;461(7267):1126-9
references.pmid: 19847265
references.citation: PLoS One. 2010;5(7):e11661
references.pmid: 20661473
references.citation: Int J Dev Biol. 2011;55(3):297-303
references.pmid: 21553382
references.citation: Hear Res. 2011 Aug;278(1-2):52-68
references.pmid: 21281707
references.citation: Am J Hum Genet. 2012 Oct 5;91(4):636-45
references.pmid: 22981119
references.citation: Channels (Austin). 2013 May-Jun;7(3):171-81
references.pmid: 23510940
references.citation: BMC Cell Biol. 2013;14:50
references.pmid: 24256100
references.citation: Nat Chem Biol. 2014 Mar;10(3):231-8
references.pmid: 24441587
references.citation: Neuroscience. 2014 May 30;268:33-47
references.pmid: 24631676
references.citation: J Neurosci Res. 2014 Jul;92(7):893-903
references.pmid: 24753179
references.citation: J Gen Physiol. 2014 Jun;143(6):679-92
references.pmid: 24863929
references.citation: J Neurosci. 2014 Aug 13;34(33):11085-95
references.pmid: 25122905
references.citation: Exp Neurol. 2015 Mar;265:69-83
references.pmid: 25542980
references.citation: J Biol Chem. 2000 Jan 14;275(2):1247-60
references.pmid: 10625670
references.citation: Trends Cell Biol. 2000 Aug;10(8):322-8
references.pmid: 10884684
references.citation: Cell. 2000 Jul 7;102(1):89-97
references.pmid: 10929716
references.citation: Biochem Biophys Res Commun. 2002 Jan 18;290(2):615-23
references.pmid: 11785943
references.citation: Mol Cell Neurosci. 2002 Mar;19(3):459-75
references.pmid: 11906216
references.citation: Proc Natl Acad Sci U S A. 2002 May 28;99(11):7711-6
references.pmid: 12032348
references.citation: J Histochem Cytochem. 2003 Jun;51(6):809-19
references.pmid: 12754292
references.citation: J Physiol. 2003 Jun 15;549(Pt 3):697-717
references.pmid: 12740421
references.citation: J Physiol. 2003 Dec 15;553(Pt 3):747-58
references.pmid: 14514878
references.citation: J Biol Chem. 2004 Jan 2;279(1):547-55
references.pmid: 14570872
references.citation: J Neurosci Res. 2004 Feb 1;75(3):371-83
references.pmid: 14743450
references.citation: EMBO J. 2004 Jan 28;23(2):312-21
references.pmid: 14685260
references.citation: Protein Profile. 1995;2(4):297-490
references.pmid: 7553064