Ultrastructural evidence for a binding substance to the sweet-tasting protein thaumatin inside taste bud pores of rhesus monkey foliate papillae.
Identifieur interne : 000506 ( Main/Corpus ); précédent : 000505; suivant : 000507Ultrastructural evidence for a binding substance to the sweet-tasting protein thaumatin inside taste bud pores of rhesus monkey foliate papillae.
Auteurs : B P Menco ; G. HellekantSource :
- Microscopy research and technique [ 1059-910X ] ; 1993.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Plant Proteins, Sweetening Agents.
- chemical : Gold Colloid.
- metabolism : Taste Buds.
- ultrastructure : Microvilli, Taste Buds.
- Animals, Freeze Etching, Macaca mulatta.
Abstract
Thaumatin is a protein that tastes intensely sweet only to Old World monkeys and to higher primates, including man. Here we used pre-embedding ultrastructural methods to study the distribution of thaumatin in apical regions of Rhesus monkey foliate papillae, using thaumatin conjugated to 5 nm gold particles. With freeze-substitution we saw that gold-labeled thaumatin bound to an electron-opaque, sponge-like secretory substance inside the taste bud pores. Labeled thaumatin was found at the surface of the secretory substance even deep inside the pore, where other, unlabeled cellular structures surrounded the substance. With freeze-fracture deep-etching the secretory substance that bound the thaumatin-gold particles appeared coarsely granular. There was no labeling of any other taste bud pore structure, including microvilli and small membrane-lined vesicles. Pre-incubation with an excess of unlabeled thaumatin inhibited binding with gold-labeled thaumatin. The results suggest that the secretory substance had the greatest affinity of all taste pore structures to the sweet-tasting compound under our experimental conditions. Therefore, gustatory reception probably involves various taste compound binding structures, microvilli, and also secretory substances like the one described here which bound thaumatin. We speculate that the secretory substance may bind taste stimuli and serve as an intermediate between stimuli and receptors. It could be involved in stimulus removal or delivery or both.
DOI: 10.1002/jemt.1070260206
PubMed: 8241549
Links to Exploration step
pubmed:8241549Le document en format XML
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Hellekant</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8241549</idno><idno type="pmid">8241549</idno><idno type="doi">10.1002/jemt.1070260206</idno><idno type="wicri:Area/Main/Corpus">000506</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000506</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Ultrastructural evidence for a binding substance to the sweet-tasting protein thaumatin inside taste bud pores of rhesus monkey foliate papillae.</title><author><name sortKey="Menco, B P" sort="Menco, B P" uniqKey="Menco B" first="B P" last="Menco">B P Menco</name><affiliation><nlm:affiliation>Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208-3520.</nlm:affiliation></affiliation></author><author><name sortKey="Hellekant, G" sort="Hellekant, G" uniqKey="Hellekant G" first="G" last="Hellekant">G. Hellekant</name></author></analytic><series><title level="j">Microscopy research and technique</title><idno type="ISSN">1059-910X</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Freeze Etching (MeSH)</term><term>Gold Colloid (MeSH)</term><term>Macaca mulatta (MeSH)</term><term>Microvilli (ultrastructure)</term><term>Plant Proteins (metabolism)</term><term>Sweetening Agents (metabolism)</term><term>Taste Buds (metabolism)</term><term>Taste Buds (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Plant Proteins</term><term>Sweetening Agents</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Gold Colloid</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Taste Buds</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Microvilli</term><term>Taste Buds</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Freeze Etching</term><term>Macaca mulatta</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thaumatin is a protein that tastes intensely sweet only to Old World monkeys and to higher primates, including man. Here we used pre-embedding ultrastructural methods to study the distribution of thaumatin in apical regions of Rhesus monkey foliate papillae, using thaumatin conjugated to 5 nm gold particles. With freeze-substitution we saw that gold-labeled thaumatin bound to an electron-opaque, sponge-like secretory substance inside the taste bud pores. Labeled thaumatin was found at the surface of the secretory substance even deep inside the pore, where other, unlabeled cellular structures surrounded the substance. With freeze-fracture deep-etching the secretory substance that bound the thaumatin-gold particles appeared coarsely granular. There was no labeling of any other taste bud pore structure, including microvilli and small membrane-lined vesicles. Pre-incubation with an excess of unlabeled thaumatin inhibited binding with gold-labeled thaumatin. The results suggest that the secretory substance had the greatest affinity of all taste pore structures to the sweet-tasting compound under our experimental conditions. Therefore, gustatory reception probably involves various taste compound binding structures, microvilli, and also secretory substances like the one described here which bound thaumatin. We speculate that the secretory substance may bind taste stimuli and serve as an intermediate between stimuli and receptors. It could be involved in stimulus removal or delivery or both.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8241549</PMID><DateCompleted><Year>1994</Year><Month>01</Month><Day>04</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1059-910X</ISSN><JournalIssue CitedMedium="Print"><Volume>26</Volume><Issue>2</Issue><PubDate><Year>1993</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>Microscopy research and technique</Title><ISOAbbreviation>Microsc Res Tech</ISOAbbreviation></Journal><ArticleTitle>Ultrastructural evidence for a binding substance to the sweet-tasting protein thaumatin inside taste bud pores of rhesus monkey foliate papillae.</ArticleTitle><Pagination><MedlinePgn>133-41</MedlinePgn></Pagination><Abstract><AbstractText>Thaumatin is a protein that tastes intensely sweet only to Old World monkeys and to higher primates, including man. Here we used pre-embedding ultrastructural methods to study the distribution of thaumatin in apical regions of Rhesus monkey foliate papillae, using thaumatin conjugated to 5 nm gold particles. With freeze-substitution we saw that gold-labeled thaumatin bound to an electron-opaque, sponge-like secretory substance inside the taste bud pores. Labeled thaumatin was found at the surface of the secretory substance even deep inside the pore, where other, unlabeled cellular structures surrounded the substance. With freeze-fracture deep-etching the secretory substance that bound the thaumatin-gold particles appeared coarsely granular. There was no labeling of any other taste bud pore structure, including microvilli and small membrane-lined vesicles. Pre-incubation with an excess of unlabeled thaumatin inhibited binding with gold-labeled thaumatin. The results suggest that the secretory substance had the greatest affinity of all taste pore structures to the sweet-tasting compound under our experimental conditions. Therefore, gustatory reception probably involves various taste compound binding structures, microvilli, and also secretory substances like the one described here which bound thaumatin. We speculate that the secretory substance may bind taste stimuli and serve as an intermediate between stimuli and receptors. It could be involved in stimulus removal or delivery or both.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Menco</LastName><ForeName>B P</ForeName><Initials>BP</Initials><AffiliationInfo><Affiliation>Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208-3520.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hellekant</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Microsc Res Tech</MedlineTA><NlmUniqueID>9203012</NlmUniqueID><ISSNLinking>1059-910X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017979">Gold Colloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005613" MajorTopicYN="N">Freeze Etching</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017979" MajorTopicYN="N">Gold Colloid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008253" MajorTopicYN="N">Macaca mulatta</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008871" MajorTopicYN="N">Microvilli</DescriptorName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013549" MajorTopicYN="N">Sweetening Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013650" MajorTopicYN="N">Taste Buds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>10</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8241549</ArticleId><ArticleId IdType="doi">10.1002/jemt.1070260206</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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