Abstract:
:In previous work we identified a basilar papilla protein (BPP23) that appears to be one of the most abundant soluble proteins in the basilar papilla of the chick cochlea. Here we report the purification of protein BPP23 from chick cochlea and the generation of a specific antiserum. Immunoblotting and immunoprecipitation experiments with this antiserum indicate that BPP23 is a calcium-binding protein very similar, if not identical, to avian calbindin, the 28-kDa vitamin D-dependent calcium-binding protein. Although the basilar papilla contains both receptor hair cells and supporting cells, immunocytochemical studies by others have localized calbindin-like immunoreactivity to the hair cells in the rat auditory receptor epithelium. Our estimates of the abundance of protein BPP23, assuming exclusive localization within the hair cell, indicate a concentration of at least 1 mM. Avian calbindin has four high-affinity (Kd = 0.5 X 10(-6)) calcium-binding sites. The presence of a specific calcium-binding activity at such high levels suggests an important function for cochlear calbindin (BPP23) in hair cell calcium homeostasis and auditory transduction.
journal_name
Proc Natl Acad Sci U S Aauthors
Oberholtzer JC,Buettger C,Summers MC,Matschinsky FMdoi
10.1073/pnas.85.10.3387subject
Has Abstractpub_date
1988-05-01 00:00:00pages
3387-90issue
10eissn
0027-8424issn
1091-6490journal_volume
85pub_type
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