Abstract
BackgroundThe zona pellucida (ZP) domain is part of many extracellular proteins with diverse functions from structural components to receptors. The mammalian β-tectorin is a protein of 336 amino acid residues containing a single ZP domain and a putative signal peptide at the N-terminus of the protein. It is 1 component of a gel-like structure called the tectorial membrane which is involved in transforming sound waves into neuronal signals and is important for normal auditory function. β-Tectorin is specifically expressed in the mammalian and avian inner ear.Methodology/Principal FindingsWe identified and cloned the gene encoding zebrafish β-tectorin. Through whole-mount in situ hybridization, we demonstrated that β-tectorin messenger RNA was expressed in the otic placode and specialized sensory patch of the inner ear during zebrafish embryonic stages. Morpholino knockdown of zebrafish β-tectorin affected the position and number of otoliths in the ears of morphants. Finally, swimming behaviors of β-tectorin morphants were abnormal since the development of the inner ear was compromised.Conclusions/SignificanceOur results reveal that zebrafish β-tectorin is specifically expressed in the zebrafish inner ear, and is important for regulating the development of the zebrafish inner ear. Lack of zebrafish β-tectorin caused severe defects in inner ear formation of otoliths and function.
Highlights
The zona pellucida (ZP) was first discovered as a glycoprotein surrounding the plasma membrane of an oocyte, and it is important in fertilization
Among these proteins are the mammalian ZP1, ZP2, and ZP3, and non-mammalian eggcoating proteins, Tamm-Horsfall protein (THP), glycoprotein (GP)-2, a- and b-tectorins, transforming growth factor (TGF)-b receptor III, endoglin, deleted in malignant brain tumor (DMBT)1, no-mechanoreceptor potential-A (Nomp A), Dumpy, and cuticlin-1 [1]. Each of these ZP-containing proteins is composed of a signal sequence driving these proteins to the endoplasmic reticulum (ER), and each possesses a ZP domain of approximately 260 amino acids long that is comprised of 8,10 conserved cysteine residues, a C-terminal, a hydrophobic transmembranelike region, and a short cytoplasmic tail [2,3]
A signal peptide of 16-amino acids, MAAVGLFFILLPVTWA, in the NH2-terminal was predicted by the online software, SignalP 3.0, which likewise occurs in mammalian b-tectorin proteins
Summary
The zona pellucida (ZP) was first discovered as a glycoprotein surrounding the plasma membrane of an oocyte, and it is important in fertilization. The ZP domain is a sequence shared by many extracellular proteins with diverse functions from structural components to receptors Among these proteins are the mammalian ZP1, ZP2, and ZP3, and non-mammalian eggcoating proteins, Tamm-Horsfall protein (THP), glycoprotein (GP)-2, a- and b-tectorins, transforming growth factor (TGF)-b receptor III, endoglin, deleted in malignant brain tumor (DMBT), no-mechanoreceptor potential-A (Nomp A), Dumpy, and cuticlin-1 [1]. Each of these ZP-containing proteins is composed of a signal sequence driving these proteins to the endoplasmic reticulum (ER), and each possesses a ZP domain of approximately 260 amino acids long that is comprised of 8,10 conserved cysteine residues, a C-terminal, a hydrophobic transmembranelike region, and a short cytoplasmic tail [2,3]. It is 1 component of a gel-like structure called the tectorial membrane which is involved in transforming sound waves into neuronal signals and is important for normal auditory function. b-Tectorin is expressed in the mammalian and avian inner ear
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