Possible role for salivary gland protein in taste reception indicated by homology to lipophilic-ligand carrier proteins

SENSORY transduction in taste and olfaction, the principal chemical senses, seems to be mediated by membrane-associated proteins on the apical surfaces of the respective receptor cells 1,2 . The recent isolation and characterization of soluble 'odorant-binding proteins9 secreted from the nasal...

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Veröffentlicht in:Nature (London) 1990-01, Vol.343 (6256), p.366-369
Hauptverfasser: Schmale, Hartwig, Holtgreve-Grez, Heidi, Christiansen, Heidje
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description SENSORY transduction in taste and olfaction, the principal chemical senses, seems to be mediated by membrane-associated proteins on the apical surfaces of the respective receptor cells 1,2 . The recent isolation and characterization of soluble 'odorant-binding proteins9 secreted from the nasal glands of rat 3 , cow 4 and frog 5 , led to the hypothesis that these proteins function as necessary cofactors in olfactory transduction by concentrating and delivering odorants to the receptors 6 . The primary reception of taste stimuli occurs in specialized neuroepithelial receptor cells bundled in taste buds that are clustered in various types of papillae in the lingual epithelium of the tongue 7 . Small tubulo-alveolar salivary glands, the von Ebner's glands, are located beneath the circumvallate and the foliate papillae. Their ducts open exclusively into the trough at the base of the papillae 8,9 . Taste buds located in the medial and lateral walls of the papillae open with their taste pores into the trough and consequently are in direct contact with the secretions of von Ebner's glands. Here we report the molecular cloning and characterization of a protein of relative molecular mass 18,000 that is highly expressed in von Ebner's glands. Like the odorant-binding proteins, this protein shows similarity to members of a protein superfamily of hydrophobic molecule transporters, indicating that pre-receptor events could also be necessary for the concentration and delivery of sapid molecules in the gustatory system, and emphasizing the close relationship of taste and olfaction.
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The recent isolation and characterization of soluble 'odorant-binding proteins9 secreted from the nasal glands of rat 3 , cow 4 and frog 5 , led to the hypothesis that these proteins function as necessary cofactors in olfactory transduction by concentrating and delivering odorants to the receptors 6 . The primary reception of taste stimuli occurs in specialized neuroepithelial receptor cells bundled in taste buds that are clustered in various types of papillae in the lingual epithelium of the tongue 7 . Small tubulo-alveolar salivary glands, the von Ebner's glands, are located beneath the circumvallate and the foliate papillae. Their ducts open exclusively into the trough at the base of the papillae 8,9 . Taste buds located in the medial and lateral walls of the papillae open with their taste pores into the trough and consequently are in direct contact with the secretions of von Ebner's glands. Here we report the molecular cloning and characterization of a protein of relative molecular mass 18,000 that is highly expressed in von Ebner's glands. Like the odorant-binding proteins, this protein shows similarity to members of a protein superfamily of hydrophobic molecule transporters, indicating that pre-receptor events could also be necessary for the concentration and delivery of sapid molecules in the gustatory system, and emphasizing the close relationship of taste and olfaction.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/343366a0</identifier><identifier>PMID: 1689010</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Alveoli ; Amino Acid Sequence ; Amino acids ; Animals ; Base Sequence ; Binding ; Biological and medical sciences ; Carrier Proteins ; Cloning ; Cloning, Molecular ; Cofactors ; Deoxyribonucleic acid ; DNA ; DNA - genetics ; Ducts ; Epithelium ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; genes ; Gustatory system ; Homology ; Humanities and Social Sciences ; Hydrophobicity ; letter ; Ligands ; Lingual epithelium ; Lipocalin 1 ; Lipophilic ; Male ; Molecular Sequence Data ; Molecular Weight ; Molecules ; multidisciplinary ; Neurobiology ; Neurosciences ; Odorants ; Olfaction ; Olfactory system and olfaction. Gustatory system and gustation ; Oocytes - metabolism ; Organic chemistry ; Papillae ; Peptides ; Physiology ; Poly A - genetics ; Poly A - isolation &amp; purification ; Protein Biosynthesis ; Proteins ; Rats ; RNA - analysis ; RNA - genetics ; RNA - isolation &amp; purification ; RNA, Messenger ; Salivary gland ; Salivary glands ; Salivary Glands - analysis ; Salivary Glands - metabolism ; Salivary Proteins and Peptides - genetics ; Salivary Proteins and Peptides - physiology ; Science ; Science (multidisciplinary) ; Secretions ; Senses ; Sensory transduction ; Sequence Homology, Nucleic Acid ; Smell ; Taste ; Taste - physiology ; Taste buds ; Taste stimuli ; Transfection ; Trends ; Vertebrates: nervous system and sense organs ; Xenopus laevis</subject><ispartof>Nature (London), 1990-01, Vol.343 (6256), p.366-369</ispartof><rights>Springer Nature Limited 1990</rights><rights>1991 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. 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The recent isolation and characterization of soluble 'odorant-binding proteins9 secreted from the nasal glands of rat 3 , cow 4 and frog 5 , led to the hypothesis that these proteins function as necessary cofactors in olfactory transduction by concentrating and delivering odorants to the receptors 6 . The primary reception of taste stimuli occurs in specialized neuroepithelial receptor cells bundled in taste buds that are clustered in various types of papillae in the lingual epithelium of the tongue 7 . Small tubulo-alveolar salivary glands, the von Ebner's glands, are located beneath the circumvallate and the foliate papillae. Their ducts open exclusively into the trough at the base of the papillae 8,9 . Taste buds located in the medial and lateral walls of the papillae open with their taste pores into the trough and consequently are in direct contact with the secretions of von Ebner's glands. 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Psychology</subject><subject>Gene Expression</subject><subject>genes</subject><subject>Gustatory system</subject><subject>Homology</subject><subject>Humanities and Social Sciences</subject><subject>Hydrophobicity</subject><subject>letter</subject><subject>Ligands</subject><subject>Lingual epithelium</subject><subject>Lipocalin 1</subject><subject>Lipophilic</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Molecules</subject><subject>multidisciplinary</subject><subject>Neurobiology</subject><subject>Neurosciences</subject><subject>Odorants</subject><subject>Olfaction</subject><subject>Olfactory system and olfaction. 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The recent isolation and characterization of soluble 'odorant-binding proteins9 secreted from the nasal glands of rat 3 , cow 4 and frog 5 , led to the hypothesis that these proteins function as necessary cofactors in olfactory transduction by concentrating and delivering odorants to the receptors 6 . The primary reception of taste stimuli occurs in specialized neuroepithelial receptor cells bundled in taste buds that are clustered in various types of papillae in the lingual epithelium of the tongue 7 . Small tubulo-alveolar salivary glands, the von Ebner's glands, are located beneath the circumvallate and the foliate papillae. Their ducts open exclusively into the trough at the base of the papillae 8,9 . Taste buds located in the medial and lateral walls of the papillae open with their taste pores into the trough and consequently are in direct contact with the secretions of von Ebner's glands. Here we report the molecular cloning and characterization of a protein of relative molecular mass 18,000 that is highly expressed in von Ebner's glands. Like the odorant-binding proteins, this protein shows similarity to members of a protein superfamily of hydrophobic molecule transporters, indicating that pre-receptor events could also be necessary for the concentration and delivery of sapid molecules in the gustatory system, and emphasizing the close relationship of taste and olfaction.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>1689010</pmid><doi>10.1038/343366a0</doi><tpages>4</tpages></addata></record>
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identifier ISSN: 0028-0836
ispartof Nature (London), 1990-01, Vol.343 (6256), p.366-369
issn 0028-0836
1476-4687
language eng
recordid cdi_proquest_miscellaneous_79601574
source MEDLINE; Nature; SpringerLink Journals - AutoHoldings
subjects Alveoli
Amino Acid Sequence
Amino acids
Animals
Base Sequence
Binding
Biological and medical sciences
Carrier Proteins
Cloning
Cloning, Molecular
Cofactors
Deoxyribonucleic acid
DNA
DNA - genetics
Ducts
Epithelium
Fundamental and applied biological sciences. Psychology
Gene Expression
genes
Gustatory system
Homology
Humanities and Social Sciences
Hydrophobicity
letter
Ligands
Lingual epithelium
Lipocalin 1
Lipophilic
Male
Molecular Sequence Data
Molecular Weight
Molecules
multidisciplinary
Neurobiology
Neurosciences
Odorants
Olfaction
Olfactory system and olfaction. Gustatory system and gustation
Oocytes - metabolism
Organic chemistry
Papillae
Peptides
Physiology
Poly A - genetics
Poly A - isolation & purification
Protein Biosynthesis
Proteins
Rats
RNA - analysis
RNA - genetics
RNA - isolation & purification
RNA, Messenger
Salivary gland
Salivary glands
Salivary Glands - analysis
Salivary Glands - metabolism
Salivary Proteins and Peptides - genetics
Salivary Proteins and Peptides - physiology
Science
Science (multidisciplinary)
Secretions
Senses
Sensory transduction
Sequence Homology, Nucleic Acid
Smell
Taste
Taste - physiology
Taste buds
Taste stimuli
Transfection
Trends
Vertebrates: nervous system and sense organs
Xenopus laevis
title Possible role for salivary gland protein in taste reception indicated by homology to lipophilic-ligand carrier proteins
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