Intracellular distributions and putative functions of calcium-binding proteins in the bullfrog vestibular otolith organs.
Hair cells in the bullfrog vestibular otolith organs were immunolabeled by monoclonal and polyclonal antisera against calbindin (CaB), calmodulin (CaM), calretinin (CaR), and parvalbumin (PA). S-100, previously shown to immunolabel striolar hair cells in fish vestibular organs, only weakly immunolabeled hair cells in the bullfrog vestibular otolith organs. Immunolabeling was not detected in supporting cells. With the exception of CaR, myelinated axons and unmyelinated nerve terminals were immunolabeled by all of the above antisera. Immunolabeling was seen in all saccular hair cells, although hair cells at the macular margins were immunolabeled more intensely for CaB, CaM, and PA than more centrally located hair cells. As the macula margins are known to be a growth zone, this labeling pattern suggests that marginal hair cells up-regulate their calcium-binding proteins during hair cell development. In the utriculus, immunolabeling for CaM and PA was generally restricted to striolar hair cells. CaR immunolabeling was restricted to the stereociliary array. Immunolabeling for other calcium-binding proteins was generally seen in both the cell body and hair bundles of hair cells, although this labeling was often localized to the stereociliary array and the apical portion of the cell body. CaM and PA immunolabeling in the stereociliary array in saccular and utricular striolar cells suggests a functional role for these proteins in mechanoelectric transduction and adaptation.
Baird
R A
RA
R.S. Dow Neurological Sciences Institute, Legacy Good Samaritan Hospital, Portland, OR 97209, USA. bairdr@ohsu.edu
Steyger
P S
PS
Schuff
N R
NR
D000222:Adaptation, Physiological; D000818:Animals; D064032:Calbindin 2; D064026:Calbindins; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism* / Q000502:physiology; D002147:Calmodulin / Q000378:metabolism; D018069:Hair Cells, Vestibular / Q000378:metabolism; D007150:Immunohistochemistry; D010037:Otolithic Membrane / Q000166:cytology / Q000378:metabolism* / Q000502:physiology; D010320:Parvalbumins / Q000378:metabolism; D011892:Rana catesbeiana / Q000033:anatomy & histology / Q000378:metabolism* / Q000502:physiology; D064030:S100 Calcium Binding Protein G / Q000378:metabolism; D009418:S100 Proteins / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism
D064032:Calbindin 2; D064026:Calbindins; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D010320:Parvalbumins; D064030:S100 Calcium Binding Protein G; D009418:S100 Proteins; D002118:Calcium