In Vitro Calcite Crystal Morphology Is Modulated by Otoconial Proteins Otolin-1 and Otoconin-90

Moreland, Kirby T.; Hong, Mina; Lu, Wenfu; Rowley, Christopher W.; Ornitz, David M.; Yoreo, James J. De; Thalmann, Ruediger

doi:10.1371/journal.pone.0095333

Cited by 29 publications

(38 citation statements)

References 36 publications

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“…Oc90 and Otolin cooperate to synergistically facilitate matrix calcification in cultured cells (Yang et al, 2011b). In vitro , Oc90 requires the presence of Otolin to generate crystals with otoconia-like morphology (Moreland et al, 2014). Similarly, the normal growth of zebrafish otoliths requires OMP-1 and its incorporation of Otolin1a (Murayama et al, 2005; Murayama et al, 2004).…”

Section: Constituent Proteins In Otoconia and Otolith Developmentmentioning

confidence: 99%

Mechanisms of otoconia and otolith development

Lundberg

Thiessen

et al. 2014

Developmental Dynamics

128

134

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Otoconia are bio-crystals which couple mechanic forces to the sensory hair cells in the utricle and saccule, a process essential for us to sense linear acceleration and gravity for the purpose of maintaining bodily balance. In fish, structurally similar bio-crystals called otoliths mediate both balance and hearing. Otoconia abnormalities are common and can cause vertigo and imbalance in humans. However, the molecular etiology of these illnesses is unknown, as investigators have only begun to identify genes important for otoconia formation in recent years. To date, in-depth studies of selected mouse otoconial proteins have been performed, and about 75 zebrafish genes have been identified to be important for otolith development. This review will summarize recent findings as well as compare otoconia and otolith development. It will provide an updated brief review of otoconial proteins along with an overview of the cells and cellular processes involved. While continued efforts are needed to thoroughly understand the molecular mechanisms underlying otoconia and otolith development, it is clear that the process involves a series of temporally and spatially specific events that are tightly coordinated by numerous proteins. Such knowledge will serve as the foundation to uncover the molecular causes of human otoconia-related disorders.

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Section: Constituent Proteins In Otoconia and Otolith Developmentmentioning

confidence: 99%

Mechanisms of otoconia and otolith development

Lundberg

Thiessen

et al. 2014

Developmental Dynamics

128

134

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“…Otolin-1 requires OMP-1 in zebrafish or Oc90 in mice in order to be included into the biomineral organic matrix [12,21]. It was also shown that otolin-1 is capable of forming a filamentous network similar to that formed by collagen X [38,39]. In a vapour diffusion assay, recombinant otolin-1 had a significant effect on the shape of calcium carbonate crystals, apparently through the anisotropic acceleration of the crystallization of calcite.…”

Section: Introductionmentioning

confidence: 99%

“…These proteins have a globular C1q-like domain, which has tremendous potential to interact with other biomolecules [41][42][43]. Atomic force microscopy and electron microscopy studies have shown that mammalian otolin-1 may be involved in the formation of a hexagonal framework inside otoconia, in which otolin-1 chains may be interconnected by the C1q-like domain [39]. Atomic force microscopy and electron microscopy studies have shown that mammalian otolin-1 may be involved in the formation of a hexagonal framework inside otoconia, in which otolin-1 chains may be interconnected by the C1q-like domain [39].…”

Section: Introductionmentioning

confidence: 99%

Effect of calcium ions on structure and stability of the C1q‐like domain of otolin‐1 from human and zebrafish

et al. 2017

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Otolin-1 is a collagen-like protein expressed in the inner ear of vertebrates. It provides an organic scaffold for otoliths in fish and otoconia in land vertebrates. In this study, the expression and purification procedure of C1q-like domain of otolin-1 from human and zebrafish was developed. The structure and stability of the proteins were investigated. The results of sedimentation velocity analytical ultracentrifugation and small-angle X-ray scattering indicated that the C1q-like domain of otolin-1 forms stable trimers in solution in the presence of calcium ions. It was also observed that calcium ions influenced the secondary structure of the proteins. C1q-like domains were stabilized by the calcium ions. The human variant was especially affected by the calcium ions. The results indicate the importance of the C1q-like domain for the assembly of the organic matrix of otoliths and otoconia.

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“…These proteins include otoconin‐90 (OC90), collagenous scaffold protein otolin‐1, otopetrin, fetuin‐A, and cerebellin‐1 . Otoconin‐90 accounts for 90% of the total protein in the organic core of the otoconia, and together with otolin, forms iso‐oriented columns of nano‐crystals, which then results in the complex mosaic of native otoconia . Fetuin‐A and osteopontin are also believed to regulate nucleation and growth of calcite .…”

Section: Introductionmentioning

confidence: 99%

“…13 From the Department of Otolaryngology (W.T.K.K., R Otoconin-90 accounts for 90% of the total protein in the organic core of the otoconia, [12][13][14]16,18 and together with otolin, forms iso-oriented columns of nano-crystals, which then results in the complex mosaic of native otoconia. 16,19 Fetuin-A and osteopontin are also believed to regulate nucleation and growth of calcite. 20 Otopetrin 1 has been demonstrated to regulate cytosolic concentrations of calcium during otoconial mineralization.…”

Section: Introductionmentioning

confidence: 99%

Otoconia and otolithic membrane fragments within the posterior semicircular canal in benign paroxysmal positional vertigo

2016

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Objective Benign paroxysmal positional vertigo (BPPV) is the most common vestibular disorder with an incidence between 10.7 and 17.3 per 100,000 persons per year. The mechanism for BPPV has been postulated to involve displaced otoconia resulting in canalithiasis. While particulate matter has been observed in the endolymph of affected patients undergoing posterior canal occlusion surgery, an otoconial origin for the disease is still questioned. Study Design In this study, particulate matter was extracted from the posterior semicircular canal of two patients and examined with the scanning electron microscopy. Methods The samples were obtained from two patients intraoperatively during posterior semicircular canal occlusion. The particles were fixed, stored in ethanol and chemically dehydrated. The samples were and sputter coated and viewed under a scanning electron microscope. Digital images were obtained. Results Intact and degenerating otoconia with and without linking filaments were found attached to amorphous particulate matter. Many otoconia appeared to be partially embedded in a gel matrix, presumably that which encases and anchors the otoconia within the otolith membrane, while others stood alone with no attached filaments and matrix. The otoconia measured roughly 2 to 8 μm in length and displayed a uniform outer shape with a cylindrical bulbous body and a 3+3 rhombohedral plane at each end. Conclusion These findings suggest that the source of the particulate matter in the semicircular canals of patients with BPPV is broken off fragments of the utricular otolithic membrane with attached and detached otoconia. Level of Evidence NA

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In Vitro Calcite Crystal Morphology Is Modulated by Otoconial Proteins Otolin-1 and Otoconin-90

Cited by 29 publications

References 36 publications

Mechanisms of otoconia and otolith development

Mechanisms of otoconia and otolith development

Effect of calcium ions on structure and stability of the C1q‐like domain of otolin‐1 from human and zebrafish

Otoconia and otolithic membrane fragments within the posterior semicircular canal in benign paroxysmal positional vertigo

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