Distribution of Calcium Binding Proteins in Sensory Organs of the Ear, Nose and Throat

Yamagishi, Masuo; Ishizuka, Yoichi; Fujiwara, Mitsuru; Nakamura, Hideo; Igarashi, Syuichi; Nakano, Yuichi; Kuwano, Ryozoh

doi:10.3109/00016489309130248

Cited by 23 publications

(24 citation statements)

References 19 publications

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“…In the frog, parvalbumin is also expressed in taste cells, whereas calbindin D28k was only localized in the surrounding support cells and not in the taste cells (Kerschbaum and Hermann 1992). Therefore, parvalbumin IR in mouse taste cells corresponds to its expression in frog taste cells but not to its lack of expression in rat taste cells (Ichikawa and Helke 1997;Yamagishi et al 1993). However, the calbindin D28k expression profile in the mouse circumvallate papillae is similar to its expression in the rat taste system (Ichikawa and Helke 1997;Miyawaki et al 1996;Miyawaki et al 1998;Yamagishi et al 1993) and not to that of the frog (Kerschbaum and Hermann 1992).…”

Section: Discussionmentioning

confidence: 99%

“…Of the CBPs identified to date, calbindin D28k has been most studied in other mammalian taste systems (Ichikawa and Helke 1997;Johnson et al 1992;Miyawaki et al 1996;Miyawaki et al 1998;Ohkubo et al 2007;Yamagishi et al 1993), where it has been reported to have widespread expression within the posterior lingual papillae of the rat (Miyawaki et al 1996). Calbindin has also been reported to co-localize with gustducin and IP 3 R3 in taste receptor cells from guinea pig, where its expression was restricted to the IP 3 R3-expressing cells (Ohkubo et al 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, parvalbumin IR in mouse taste cells corresponds to its expression in frog taste cells but not to its lack of expression in rat taste cells (Ichikawa and Helke 1997;Yamagishi et al 1993). However, the calbindin D28k expression profile in the mouse circumvallate papillae is similar to its expression in the rat taste system (Ichikawa and Helke 1997;Miyawaki et al 1996;Miyawaki et al 1998;Yamagishi et al 1993) and not to that of the frog (Kerschbaum and Hermann 1992). Taken together, these data strongly suggest that the expression of CBPs can vary significantly by species, and conclusions about their potential functions in taste cells require careful attention to the particular species being studied.…”

Section: Discussionmentioning

confidence: 99%

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Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

Rebello

Aktas

Medler

2011

J Histochem Cytochem.

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SummaryIt is well established that calcium is a critical signaling molecule in the transduction of taste stimuli within the peripheral taste system. However, little is known about the regulation and termination of these calcium signals in the taste system. The authors used Western blot, immunocytochemical, and RT-PCR analyses to evaluate the expression of multiple calcium binding proteins in mouse circumvallate taste papillae, including parvalbumin, calbindin D28k, calretinin, neurocalcin, NCS-1 (or frequenin), and CaBP. They found that all of the calcium binding proteins they tested were expressed in mouse circumvallate taste cells with the exception of NCS-1. The authors correlated the expression patterns of these calcium binding proteins with a marker for type II cells and found that neurocalcin was expressed in 80% of type II cells, whereas parvalbumin was found in less than 10% of the type II cells. Calretinin, calbindin, and CaBP were expressed in about half of the type II cells. These data reveal that multiple calcium binding proteins are highly expressed in taste cells and have distinct expression patterns that likely reflect their different roles within taste receptor cells. (J Histochem Cytochem 59:530-539, 2011)

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

Rebello

Aktas

Medler

2011

J Histochem Cytochem.

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“…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%

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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Association of ecto-5?-nucleotidase with specific cell types in the adult and developing rat olfactory organ

Braun

Zimmermann

1998

J. Comp. Neurol.

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A unique feature of the olfactory epithelium is its ability to give rise to new sensory neurons throughout life and also following injury. Cells at the basal side of the epithelium serve as neurogenic progenitor cells. The enzyme ecto-5'-nucleotidase is expressed at the surface of developing nerve cells and is regarded as a marker of neural development. To study the expression pattern of the enzyme, we analyzed its distribution in the adult and developing rat olfactory organ. Labeling is restricted to specific cell types and varies between the epithelia investigated. At the basal side of the olfactory epithelium, activity of 5'-nucleotidase is associated specifically with the dark/horizontal basal cells. Neither the light/globose basal cells, which are the immediate precursors of the sensory receptor cells, nor subsets of potentially immature olfactory receptor cells are labeled. On the other hand, microvillar cells dispersed at the lumenal side of the epithelium contain 5'-nucleotidase activity. The enzyme is also present at the inner lining of the ducts of Bowman's glands as they traverse the epithelium. Within the respiratory epithelium, activity of 5'-nucleotidase is associated with basal cells as well as with the epithelial surface. During development, 5'-nucleotidase is initially limited to the respiratory epithelium, including its basal cells. Dark/horizontal basal cells of the olfactory epithelium, which are positive for 5'-nucleotidase, first appear at the border of the respiratory epithelium, suggesting that they might originate from immigrating basal cells of the respiratory epithelium. Within the vomeronasal organ, labeling is largely restricted to the receptor-free epithelium. Although the functional role of 5'-nucleotidase in the olfactory system needs to be further defined, the distribution of the enzyme can be used successfully as a marker for defined cell types.

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Distribution of Calcium Binding Proteins in Sensory Organs of the Ear, Nose and Throat

Cited by 23 publications

References 19 publications

Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

Expression of Calcium Binding Proteins in Mouse Type II Taste Cells

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

Association of ecto-5?-nucleotidase with specific cell types in the adult and developing rat olfactory organ

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