Mechanoelectrical transduction by hair cells

Pickles, James O.; Corey, David P.

doi:10.1016/0166-2236(92)90066-h

Cited by 156 publications

(79 citation statements)

References 34 publications

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“…Displace- ments of the calcified mass (masses) relative to the sensory epithelium results in hair cell stereocilia displacement and subsequent hair cell depolarization or hyperpolarization (reviewed in refs. [17][18][19][20].…”

Section: Discussionmentioning

confidence: 99%

Identification of a structural constituent and one possible site of postembryonic formation of a teleost otolithic membrane

Davis

Burns

Navaratnam

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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A gelatinous otolithic membrane (OM) couples a single calcified otolith to the sensory epithelium in the bluegill sunfish (Lepomis macrochirus) saccule, one of the otolithic organs in the inner ear. Though the OM is an integral part of the anatomic network of endorgan structures that result in vestibular function in the inner ear, the identity of the proteins that make up this sensory accessory membrane in teleosts, or in any vertebrate, is not fully known. Previously, we identified a cDNA from the sunfish saccular otolithic organ that encoded a new member of the collagen family of structural proteins. In this study, we examined biochemical features and the localization of the saccular collagen (SC) protein in vivo using polyclonal antisera that recognize the noncollagenous domains of the SC protein. The otolithic endorgans are part of the vestibular portion of the vertebrate inner ear and consist of a single or many calcified masses coupled to an underlying hair cell-containing sensory epithelium. A gelatinous otolithic͞otoconial membrane is attached to both the otolith and the underlying sensory epithelium and serves to couple the calcified mass(es) to the receptor epithelium. Displacement of the overlying otolith͞ otoconial mass(es) relative to the underlying receptor epithelium results in the displacement of hair cell stereociliary bundles that are critical to the mechanoelectrical transduction process in the inner ear (1).The teleost saccule is an otolithic organ involved in aspects of both vestibular (1) and acoustic function in certain fish (1, 2). The number of saccular sensory cells in certain teleosts (3) and cartilagenous fish (4) can be much larger than the number found in the human saccule (1). We took advantage of the large number of saccular hair cells found in certain teleosts to construct cDNA libraries in efforts to identify genes involved in vestibular function (5).Differential screening of the teleost saccular cDNA libraries led to the identification of candidate saccule-specific cDNAs. One of these was found to encode a unique form of collagen that was termed saccular collagen (SC). The 2.0-kb SC transcript was highly abundant in saccular RNA and appears unique to the saccule because it was not detected in several other sunfish tissues (6). A similar domain organization and homology of a conserved region within the carboxyl-terminal noncollagenous domain identified the SC as a new member of the family of collagens that includes collagens type VIII and type X (7-9). Expression of the SC gene was localized by in situ hybridization to secretory supporting cells located around the periphery of the saccular macula (6). In teleosts, supporting cells such as these have been correlated with the developmental appearance of the otolithic membrane (OM) (10) suggesting that the SC may be a component of the teleost OM. To date, the molecular identity of the proteins that comprise the teleost OM remains unknown.In this report, polyclonal SC-specific antisera were used to study the localization and...

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Section: Discussionmentioning

confidence: 99%

Identification of a structural constituent and one possible site of postembryonic formation of a teleost otolithic membrane

Davis

Burns

Navaratnam

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…Because of the correlation between tip-link and MET current as well as the unique location of the link, it has been posited that the tip-link may serve to directly gate the MET channel (Fig. 2a), either being the physical correlate of the gating spring (see below) or directly being attached to the channel to be in series with this gating element (Pickles & Corey, 1992). Tip-links are approximately 200 nm long and 5 nm wide, existing in a coiled helical structure ( Fig.…”

Section: Channel Gatingmentioning

confidence: 99%

Mechano-electrical Transduction: New Insights into Old Ideas

et al. 2006

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The gating-spring theory of hair cell mechanotransduction channel activation was first postulated over twenty years ago. The basic tenets of this hypothesis have been reaffirmed in hair cells from both auditory and vestibular systems and across species. In fact, the basic findings have been reproduced in every hair cell type tested. A great deal of information regarding the structural, mechanical, molecular and biophysical properties of the sensory hair bundle and the mechanotransducer channel has accumulated over the past twenty years. The goal of this review is to investigate new data, using the gating spring hypothesis as the framework for discussion. Mechanisms of channel gating are presented in reference to the need for a molecular gating spring or for tethering to the intra-or extracellular compartments. Dynamics of the sensory hair bundle and the presence of motor proteins are discussed in reference to passive contributions of the hair bundle to gating compliance. And finally, the molecular identity of the channel is discussed in reference to known intrinsic properties of the native transducer channel.

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“…Models of mechanotransduction, supported by ample physiological and anatomical evidence, imply the presence of one or two mechanosensory channel complexes at or near the top of each stereocilia, connected with each other via an extracellular structure called the tip link and to the actin cytoskeleton via myosin motor proteins. The deflection of stereocilia results in tension to gate the channels and thus generates the mechanoreceptor current (Pickles and Corey, 1992;Gillespie and Walker, 2001).…”

Section: Introductionmentioning

confidence: 99%

Nociceptor and Hair Cell Transducer Properties of TRPA1, a Channel for Pain and Hearing

Nagata¹,

Duggan²,

Kumar³

et al. 2005

J. Neurosci.

561

515

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Mechanosensory channels of sensory cells mediate the sensations of hearing, touch, and some forms of pain. The TRPA1 (a member of the TRP family of ion channel proteins) channel is activated by pain-producing chemicals, and its inhibition impairs hair cell mechanotransduction. As shown here and previously, TRPA1 is expressed by hair cells as well as by most nociceptors (small neurons of dorsal root, trigeminal, and nodose ganglia) and localizes to their sensory terminals (mechanosensory stereocilia and peripheral free nerves, respectively). Thus, TRPA1 channels are proposed to mediate transduction in both hair cells and nociceptors. Accordingly, we find that heterologously expressed TRPA1 display channel behaviors expected for both auditory and nociceptive transducers. First, TRPA1 and the hair cell transducer share a unique set of pore properties not described for any other channel (block by gadolinium, amiloride, gentamicin, and ruthenium red, a ranging conductance of ϳ100 pS that is reduced to 54% by calcium, permeating calcium-induced potentiation followed by closure, and reopening by depolarization), supporting a direct role of TRPA1 as a pore-forming subunit of the hair cell transducer. Second, TRPA1 channels inactivate in hyperpolarized cells but remain open in depolarized cells. This property provides a mechanism for the lack of desensitization, coincidence detection, and allodynia that characterize pain by allowing a sensory neuron to respond constantly to sustained stimulation that is suprathreshold (i.e., noxious) and yet permitting the same cell to ignore sustained stimulation that is subthreshold (i.e., innocuous). Our results support a TRPA1 role in both nociceptor and hair cell transduction.

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Mechanoelectrical transduction by hair cells

Cited by 156 publications

References 34 publications

Identification of a structural constituent and one possible site of postembryonic formation of a teleost otolithic membrane

Identification of a structural constituent and one possible site of postembryonic formation of a teleost otolithic membrane

Mechano-electrical Transduction: New Insights into Old Ideas

Nociceptor and Hair Cell Transducer Properties of TRPA1, a Channel for Pain and Hearing

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