Perireceptor events in taste.

H. Schmale, C. Ahlers, M. Bläker, K. Kock, Andrew Spielman

Research output: Contribution to journalArticle

Abstract

The microenvironment at chemical receptor sites is important for ligand-receptor interaction as it can influence the entry, residence time or exit of odorant and sapid molecules. The perireceptor milieu at apical taste cell microvilli consists of taste pore mucus and secretions from salivary glands. The majority of taste buds are sheltered in epithelial folds of the foliate and circumvallate papillae where saliva is provided predominantly by the lingual von Ebner's glands (VEGs). To investigate possible saliva-tastant interactions, we have characterized a prominent 18 kDa secretory protein expressed in human, rat and pig VEGs. The human and rat VEG proteins share 60% sequence identity and, by virtue of their protein and gene structure, can be assigned to the lipocalin superfamily of lipophilic ligand carrier proteins. VEG proteins might function as transporters of hydrophobic molecules, for example bitter substances, like the nasal odorant-binding proteins that belong to the same protein family. Because binding experiments using various bitter substances have so far failed, and in light of the species-specific expression, other functions for VEG proteins must be considered. These include the protection of taste epithelia, pheromone transport and lipid binding.

Original languageEnglish (US)
Pages (from-to)167-180
Number of pages14
JournalCiba Foundation symposium
Volume179
StatePublished - 1993

Fingerprint

von Ebner Glands
Lipocalin 1
Saliva
Taste Buds
Ligands
Lipocalins
Proteins
Pheromones
Mucus
Microvilli
Salivary Glands
Nose
Tongue
Carrier Proteins
Swine
Epithelium
Lipids

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Schmale, H., Ahlers, C., Bläker, M., Kock, K., & Spielman, A. (1993). Perireceptor events in taste. Ciba Foundation symposium, 179, 167-180.

Perireceptor events in taste. / Schmale, H.; Ahlers, C.; Bläker, M.; Kock, K.; Spielman, Andrew.

In: Ciba Foundation symposium, Vol. 179, 1993, p. 167-180.

Research output: Contribution to journalArticle

Schmale, H, Ahlers, C, Bläker, M, Kock, K & Spielman, A 1993, 'Perireceptor events in taste.', Ciba Foundation symposium, vol. 179, pp. 167-180.
Schmale H, Ahlers C, Bläker M, Kock K, Spielman A. Perireceptor events in taste. Ciba Foundation symposium. 1993;179:167-180.
Schmale, H. ; Ahlers, C. ; Bläker, M. ; Kock, K. ; Spielman, Andrew. / Perireceptor events in taste. In: Ciba Foundation symposium. 1993 ; Vol. 179. pp. 167-180.
@article{2e5a3c2518814070b9a8cc3409a4c08a,
title = "Perireceptor events in taste.",
abstract = "The microenvironment at chemical receptor sites is important for ligand-receptor interaction as it can influence the entry, residence time or exit of odorant and sapid molecules. The perireceptor milieu at apical taste cell microvilli consists of taste pore mucus and secretions from salivary glands. The majority of taste buds are sheltered in epithelial folds of the foliate and circumvallate papillae where saliva is provided predominantly by the lingual von Ebner's glands (VEGs). To investigate possible saliva-tastant interactions, we have characterized a prominent 18 kDa secretory protein expressed in human, rat and pig VEGs. The human and rat VEG proteins share 60{\%} sequence identity and, by virtue of their protein and gene structure, can be assigned to the lipocalin superfamily of lipophilic ligand carrier proteins. VEG proteins might function as transporters of hydrophobic molecules, for example bitter substances, like the nasal odorant-binding proteins that belong to the same protein family. Because binding experiments using various bitter substances have so far failed, and in light of the species-specific expression, other functions for VEG proteins must be considered. These include the protection of taste epithelia, pheromone transport and lipid binding.",
author = "H. Schmale and C. Ahlers and M. Bl{\"a}ker and K. Kock and Andrew Spielman",
year = "1993",
language = "English (US)",
volume = "179",
pages = "167--180",
journal = "Ciba Foundation symposium",
issn = "0300-5208",
publisher = "Wiley Subscription Services",

}

TY - JOUR

T1 - Perireceptor events in taste.

AU - Schmale, H.

AU - Ahlers, C.

AU - Bläker, M.

AU - Kock, K.

AU - Spielman, Andrew

PY - 1993

Y1 - 1993

N2 - The microenvironment at chemical receptor sites is important for ligand-receptor interaction as it can influence the entry, residence time or exit of odorant and sapid molecules. The perireceptor milieu at apical taste cell microvilli consists of taste pore mucus and secretions from salivary glands. The majority of taste buds are sheltered in epithelial folds of the foliate and circumvallate papillae where saliva is provided predominantly by the lingual von Ebner's glands (VEGs). To investigate possible saliva-tastant interactions, we have characterized a prominent 18 kDa secretory protein expressed in human, rat and pig VEGs. The human and rat VEG proteins share 60% sequence identity and, by virtue of their protein and gene structure, can be assigned to the lipocalin superfamily of lipophilic ligand carrier proteins. VEG proteins might function as transporters of hydrophobic molecules, for example bitter substances, like the nasal odorant-binding proteins that belong to the same protein family. Because binding experiments using various bitter substances have so far failed, and in light of the species-specific expression, other functions for VEG proteins must be considered. These include the protection of taste epithelia, pheromone transport and lipid binding.

AB - The microenvironment at chemical receptor sites is important for ligand-receptor interaction as it can influence the entry, residence time or exit of odorant and sapid molecules. The perireceptor milieu at apical taste cell microvilli consists of taste pore mucus and secretions from salivary glands. The majority of taste buds are sheltered in epithelial folds of the foliate and circumvallate papillae where saliva is provided predominantly by the lingual von Ebner's glands (VEGs). To investigate possible saliva-tastant interactions, we have characterized a prominent 18 kDa secretory protein expressed in human, rat and pig VEGs. The human and rat VEG proteins share 60% sequence identity and, by virtue of their protein and gene structure, can be assigned to the lipocalin superfamily of lipophilic ligand carrier proteins. VEG proteins might function as transporters of hydrophobic molecules, for example bitter substances, like the nasal odorant-binding proteins that belong to the same protein family. Because binding experiments using various bitter substances have so far failed, and in light of the species-specific expression, other functions for VEG proteins must be considered. These include the protection of taste epithelia, pheromone transport and lipid binding.

UR - http://www.scopus.com/inward/record.url?scp=0027861321&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027861321&partnerID=8YFLogxK

M3 - Article

VL - 179

SP - 167

EP - 180

JO - Ciba Foundation symposium

JF - Ciba Foundation symposium

SN - 0300-5208

ER -