Intracellular distributions and putative functions of calcium-binding proteins in the bullfrog vestibular otolith organs

Baird, Richard A.; Steyger, Peter S.; Schuff, N. R.

doi:10.1016/s0378-5955(96)00167-0

Cited by 28 publications

(27 citation statements)

References 83 publications

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“…was not detectable in the mammalian otoconial matrix, in contradistinction to the avian and reptilian otoconial matrix as reported on the basis of immunohistochemical evidence [30][31][32]. Immunohistochemistry for calbindin D28K in the mouse inner ear revealed reactivity only in a subset of vestibular hair cells of the utricular and saccular maculae (I. Hughes, unpublished observation).…”

Section: Calbindin-calbindinmentioning

confidence: 73%

Microscale analysis of proteins in inner ear tissues and fluids with emphasis on endolymphatic sac, otoconia, and organ of Corti

Thalmann

Hughes²,

Tong

et al. 2006

Electrophoresis

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Here we describe preparatory techniques adapted for the study of proteins of inner ear tissues and fluids that have allowed us to apply state-of-the-art analytical techniques in spite of the minute size and anatomical complexities of this organ. Illustrative examples address unresolved issues of functional and clinical significance. First, we demonstrate how quick-freezing and freeze drying prevents artifacts that arise from sampling endolymphatic sac (ES) content in the liquid state. This set the stage for the generation of the first protein profile of the ES. Identification of crucial proteins will help elucidate mechanisms of endolymph volume regulation and pathogenesis of Meniere's disease. Second, we show how a unique situation allowed identification of otoconial proteins by mass spectrometric analysis without prior separation and we discuss possible roles for these minor otoconins in otoconial development and prevention of degenerative diseases that affect balance. Finally, we demonstrate techniques for the precise dissection of organ of Corti and its substructures, while preserving their near normal chemical state. We extended an earlier study in which we identified a novel calcium-binding protein by IEF, oncomodulin, localized in the outer hair cells and show here the applicability of prefractionation for the screening of calcium-binding proteins of organ of Corti. These studies demonstrate how advanced preparatory and analytical techniques can be applied to studies of the inner ear.

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Section: Calbindin-calbindinmentioning

confidence: 73%

Microscale analysis of proteins in inner ear tissues and fluids with emphasis on endolymphatic sac, otoconia, and organ of Corti

Thalmann

Hughes²,

Tong

et al. 2006

Electrophoresis

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“…Numerous Ca 2+ -binding proteins that might serve as buffers have been identi®ed in hair cells (for comprehensive studies see Kerschbaum and Hermann 1993;Slepecky and Ulfendahl 1993;Pack and Slepecky 1995;Baird et al 1997). Calbindin, which is also called cholecalcin or vitamin D-dependent calcium-binding protein (CaBP-28K), has been observed in the receptors of several organs of the inner ear (Sans et al 1986).…”

Section: Introductionmentioning

confidence: 99%

Parvalbumin 3 is an Abundant Ca2+ Buffer in Hair Cells

Heller

Bell

Denis

et al. 2002

JARO - Journal of the Association for Research in Otolaryngolog

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Ca2+ signaling serves distinct purposes in different parts of a hair cell. The Ca 2+ concentration in stereocilia regulates adaptation and, through rapid transduction-channel reclosure, underlies ampli®ca-tion of mechanical signals. In presynaptic active zones, Ca 2+ mediates the exocytotic release of afferent neurotransmitter. At efferent synapses, Ca 2+ activates the K + channels that dominate the inhibitory postsynaptic potential. A copious supply of diffusible protein buffer isolates the three signals by restricting the spread of free Ca 2+ and limiting the duration of its action. Using cDNA subtraction and a gene expression assay based on in situ hybridization, we detected abundant expression of mRNAs encoding the Ca 2+ buffer parvalbumin 3 in bullfrog saccular and chicken cochlear hair cells. We cloned cDNAs encoding this protein from the corresponding inner-ear libraries and raised antisera against recombinant bullfrog parvalbumin 3. Immunohistochemical labeling indicated that parvalbumin 3 is a prominent Ca 2+ -binding protein in the compact, cylindrical hair cells of the bullfrog's sacculus, and occurs as well in the narrow, peanut-shaped hair cells of that organ. Using quantitative Western blot analysis, we ascertained that the concentration of parvalbumin 3 in saccular hair cells is approximately 3 mM. Parvalbumin 3 is therefore a signi®cant mobile Ca 2+ buffer, and perhaps the dominant buffer, in many types of hair cell. Moreover, parvalbumin 3 provides an early marker for developing hair cells in the frog, chicken, and zebra®sh.

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“…In the lamprey, as in other more recent species, CBPs are expressed more abundantly earlier in the formation of otoconia and otolith than later in development and when animals reach adulthood. Thus, CBP contribution to inner ear maturation started very early in the evolutionary ladder, as suggested by their presence in the organic matrix of this old fish and newer teleosts as well as higher vertebrates (Rhoten et al 1986;Drescher et al 1989;Foster et al 1993;Baird et al 1997;Abbate et al 2002;Heller et al 2002;Piscopo et al 2003Piscopo et al , 2004.…”

Section: Discussionmentioning

confidence: 93%

“…The greatest difference between the otolith of lampreys and of more recent species is the mode of cation accumulation, which is in turn dictated by refinement of the endolymphatic fluid, its molecular composition, and/or ionic concentration (Peterson et al 1978;Hara et al 1989;Wroblewski 1993;Lychakov & Lavrova 1994;Payan et al 1997). While the nature of the extracellular receptors to which calcium binding proteins (CBPs) attach remains elusive, there is consensus among many investigators that CBPs are important components of sensory and non-sensory structures (Braun 1990;Celio 1990;Kevetter & Leonard 2002), vestibular organs (Yamagishi et al 1993;Baird et al 1997;Fermin et al 1997;Balsamo et al 2000;Abbate et al 2002), and inner ear in general (Winsky et al 1989;Kerschbaum & Hermann 1993;Balsamo et al 2000;Nakazawa 2001). All CBPs are homologous proteins sharing high sequence identity (Braun 1990;Moncrief et al 1990;Kerschbaum & Hermann 1993;Yamagishi et al 1993;Zimmer et al 1995;Kawasaki et al 1998), and cross-react with polyclonal antisera produced from different species.…”

Section: Introductionmentioning

confidence: 99%

“…All these molecules are made by nonsensory cells of the end organs (Tachibana & Morioka 1992;Davis et al 1997;Borelli et al 2001;Thalmann et al 2001). Various isoforms of the same family or differing types of CBP react with cellular and non-cellular components of the otoliths in older and younger species such as cichlid fish (Presson 1994), other teleosts (Abbate et al 2002), amphibians (Hackney et al 1993Kerschbaum & Hermann 1993;Baird et al 1997;Steyger et al 1997;Heller et al 2002), lizard (Piscopo et al 2004), rodents (Chard et al 1993;Dememes et al 1993;Raymond et al 1993;Yamagishi et al 1993;Nakazawa et al 1995;Karita et al 1999;Furness et al 2002), birds (Fermin & Igarashi 1985;Heil & Scheich 1986;Hiel et al 2002), other mammals (Pack & Slepecky 1995;Imamura & Adams 1996;Coppens et al 2000Coppens et al , 2001Coppens et al , 2003, primates (Usami et al 1995), and humans (Yamashita et al 1995).…”

Section: Introductionmentioning

confidence: 99%

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Morphogenesis of otoliths during larval development in brook lamprey,Lampetra planeri

Avallone

Fascio

Balsamo

et al. 2007

Italian Journal of Zoology

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Otolith morphogenesis of the brook lamprey, Lampetra planeri, was analysed from larval to adult stages. The brook lamprey remains juvenile for about 4 years, facilitating analysis of otoliths maturation that permits to identify relevant evolutionary traits in this primitive species and to compare our results with more evoluted species of vertebrate taxa. We combined histochemical, immunohistochemical, scanning electron microscopy, elemental analysis and X-ray diffraction of lamprey otoliths to establish possible relationships between otolithic mass, individual crystals, the otolithic organic substance that binds individual otoconia together and the inorganic elements that mineralize the lamprey otoliths. Histochemical analysis of the otoliths suggests that mineralization occurs gradually, beginning near the apex of the secretory epithelium. Then, the otoconia increase in size by deposition of layers of a dense crystalline substance. Immunohistochemical reactivity of calcium binding proteins indicates that calmodulin, calbindin, S-100 and parvalbumin are parts of the uncalcified organic mass that holds otoconia together. Imaging of the immunoreactivity of each protein by Confocal Laser Scanning Microscopy in ammocoete at the first year of the larval stage shows weak reaction products which, however, gradually increase in intensity, with peak value in ammocoete at the fourth year of the larval stage.

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Intracellular distributions and putative functions of calcium-binding proteins in the bullfrog vestibular otolith organs

Cited by 28 publications

References 83 publications

Microscale analysis of proteins in inner ear tissues and fluids with emphasis on endolymphatic sac, otoconia, and organ of Corti

Microscale analysis of proteins in inner ear tissues and fluids with emphasis on endolymphatic sac, otoconia, and organ of Corti

Parvalbumin 3 is an Abundant Ca2+ Buffer in Hair Cells

Morphogenesis of otoliths during larval development in brook lamprey,Lampetra planeri

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