Bitter taste receptors: Novel insights into the biochemistry and pharmacology
Bitter taste receptors (T2Rs) belong to the super family of G protein-coupled receptors (GPCRs). There are 25 T2Rs expressed in humans, and these interact with a large and diverse group of bitter ligands. T2Rs are expressed in many extra-oral tissues and can perform diverse physiological roles. Stru...
Gespeichert in:
| Veröffentlicht in: | The international journal of biochemistry & cell biology 2016-08, Vol.77 (Pt B), p.184-196 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 196 |
|---|---|
| container_issue | Pt B |
| container_start_page | 184 |
| container_title | The international journal of biochemistry & cell biology |
| container_volume | 77 |
| creator | Jaggupilli, Appalaraju Howard, Ryan Upadhyaya, Jasbir D. Bhullar, Rajinder P. Chelikani, Prashen |
| description | Bitter taste receptors (T2Rs) belong to the super family of G protein-coupled receptors (GPCRs). There are 25 T2Rs expressed in humans, and these interact with a large and diverse group of bitter ligands. T2Rs are expressed in many extra-oral tissues and can perform diverse physiological roles. Structure-function studies led to the identification of similarities and dissimilarities between T2Rs and Class A GPCRs including amino acid conservation and novel motifs. However, the efficacy of most of the T2R ligands is not yet elucidated and the biochemical pharmacology of T2Rs is poorly understood. Recent studies on T2Rs characterized novel ligands including blockers for these receptors that include inverse agonist and antagonists. In this review we discuss the techniques used for elucidating bitter blockers, concept of ligand bias, generic amino acid numbering, the role of cholesterol, and conserved water molecules in the biochemistry and pharmacology of T2Rs. |
| doi_str_mv | 10.1016/j.biocel.2016.03.005 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1807277796</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1357272516300590</els_id><sourcerecordid>1807277796</sourcerecordid><originalsourceid>FETCH-LOGICAL-c362t-bf3f88e77811f76aea9bad6bd5a2a71ca59ab76f19a07281cfb47fdd698a04303</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EoqXwBwhlySbBTupHWCBBxUsqsIG15TiTxlUSF9ut1L_HVQtLVjMj3Tt35iB0SXBGMGE3y6wyVkOX5XHKcJFhTI_QmAguUio4PY59QXma85yO0Jn3S4wxoXlxikY5K0uKGR2jtwcTArgkKB8gcaBhFazzt8m73UCXmMGbRRt8bIJNQgvJLrSF3vjgtoka6mTVKtcrbTu72J6jk0Z1Hi4OdYK-nh4_Zy_p_OP5dXY_T3XB8pBWTdEIAZwLQhrOFKiyUjWraqpyxYlWtFQVZw0pFea5ILqpprypa1YKhacFLiboer935ez3GnyQ8aDIolMD2LWXREQf57xkUTrdS7Wz3jto5MqZXrmtJFjuQMql3IOUO5ASFzKCjLarQ8K66qH-M_2Si4K7vQDinxsDTnptYNBQm0gxyNqa_xN-ANKxh1c</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1807277796</pqid></control><display><type>article</type><title>Bitter taste receptors: Novel insights into the biochemistry and pharmacology</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Jaggupilli, Appalaraju ; Howard, Ryan ; Upadhyaya, Jasbir D. ; Bhullar, Rajinder P. ; Chelikani, Prashen</creator><creatorcontrib>Jaggupilli, Appalaraju ; Howard, Ryan ; Upadhyaya, Jasbir D. ; Bhullar, Rajinder P. ; Chelikani, Prashen</creatorcontrib><description>Bitter taste receptors (T2Rs) belong to the super family of G protein-coupled receptors (GPCRs). There are 25 T2Rs expressed in humans, and these interact with a large and diverse group of bitter ligands. T2Rs are expressed in many extra-oral tissues and can perform diverse physiological roles. Structure-function studies led to the identification of similarities and dissimilarities between T2Rs and Class A GPCRs including amino acid conservation and novel motifs. However, the efficacy of most of the T2R ligands is not yet elucidated and the biochemical pharmacology of T2Rs is poorly understood. Recent studies on T2Rs characterized novel ligands including blockers for these receptors that include inverse agonist and antagonists. In this review we discuss the techniques used for elucidating bitter blockers, concept of ligand bias, generic amino acid numbering, the role of cholesterol, and conserved water molecules in the biochemistry and pharmacology of T2Rs.</description><identifier>ISSN: 1357-2725</identifier><identifier>EISSN: 1878-5875</identifier><identifier>DOI: 10.1016/j.biocel.2016.03.005</identifier><identifier>PMID: 26995065</identifier><language>eng</language><publisher>Netherlands: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Bitter blockers ; Bitter taste receptors (T2Rs) ; Cholesterol ; Constitutive active mutants ; G protein-coupled receptor (GPCR) ; Humans ; Ligand bias ; Ligands ; Receptors, G-Protein-Coupled - chemistry ; Receptors, G-Protein-Coupled - genetics ; Receptors, G-Protein-Coupled - metabolism ; Structural water molecules ; Taste Perception - drug effects</subject><ispartof>The international journal of biochemistry & cell biology, 2016-08, Vol.77 (Pt B), p.184-196</ispartof><rights>2016 Elsevier Ltd</rights><rights>Copyright © 2016 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c362t-bf3f88e77811f76aea9bad6bd5a2a71ca59ab76f19a07281cfb47fdd698a04303</citedby><cites>FETCH-LOGICAL-c362t-bf3f88e77811f76aea9bad6bd5a2a71ca59ab76f19a07281cfb47fdd698a04303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biocel.2016.03.005$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26995065$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jaggupilli, Appalaraju</creatorcontrib><creatorcontrib>Howard, Ryan</creatorcontrib><creatorcontrib>Upadhyaya, Jasbir D.</creatorcontrib><creatorcontrib>Bhullar, Rajinder P.</creatorcontrib><creatorcontrib>Chelikani, Prashen</creatorcontrib><title>Bitter taste receptors: Novel insights into the biochemistry and pharmacology</title><title>The international journal of biochemistry & cell biology</title><addtitle>Int J Biochem Cell Biol</addtitle><description>Bitter taste receptors (T2Rs) belong to the super family of G protein-coupled receptors (GPCRs). There are 25 T2Rs expressed in humans, and these interact with a large and diverse group of bitter ligands. T2Rs are expressed in many extra-oral tissues and can perform diverse physiological roles. Structure-function studies led to the identification of similarities and dissimilarities between T2Rs and Class A GPCRs including amino acid conservation and novel motifs. However, the efficacy of most of the T2R ligands is not yet elucidated and the biochemical pharmacology of T2Rs is poorly understood. Recent studies on T2Rs characterized novel ligands including blockers for these receptors that include inverse agonist and antagonists. In this review we discuss the techniques used for elucidating bitter blockers, concept of ligand bias, generic amino acid numbering, the role of cholesterol, and conserved water molecules in the biochemistry and pharmacology of T2Rs.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bitter blockers</subject><subject>Bitter taste receptors (T2Rs)</subject><subject>Cholesterol</subject><subject>Constitutive active mutants</subject><subject>G protein-coupled receptor (GPCR)</subject><subject>Humans</subject><subject>Ligand bias</subject><subject>Ligands</subject><subject>Receptors, G-Protein-Coupled - chemistry</subject><subject>Receptors, G-Protein-Coupled - genetics</subject><subject>Receptors, G-Protein-Coupled - metabolism</subject><subject>Structural water molecules</subject><subject>Taste Perception - drug effects</subject><issn>1357-2725</issn><issn>1878-5875</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EoqXwBwhlySbBTupHWCBBxUsqsIG15TiTxlUSF9ut1L_HVQtLVjMj3Tt35iB0SXBGMGE3y6wyVkOX5XHKcJFhTI_QmAguUio4PY59QXma85yO0Jn3S4wxoXlxikY5K0uKGR2jtwcTArgkKB8gcaBhFazzt8m73UCXmMGbRRt8bIJNQgvJLrSF3vjgtoka6mTVKtcrbTu72J6jk0Z1Hi4OdYK-nh4_Zy_p_OP5dXY_T3XB8pBWTdEIAZwLQhrOFKiyUjWraqpyxYlWtFQVZw0pFea5ILqpprypa1YKhacFLiboer935ez3GnyQ8aDIolMD2LWXREQf57xkUTrdS7Wz3jto5MqZXrmtJFjuQMql3IOUO5ASFzKCjLarQ8K66qH-M_2Si4K7vQDinxsDTnptYNBQm0gxyNqa_xN-ANKxh1c</recordid><startdate>201608</startdate><enddate>201608</enddate><creator>Jaggupilli, Appalaraju</creator><creator>Howard, Ryan</creator><creator>Upadhyaya, Jasbir D.</creator><creator>Bhullar, Rajinder P.</creator><creator>Chelikani, Prashen</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201608</creationdate><title>Bitter taste receptors: Novel insights into the biochemistry and pharmacology</title><author>Jaggupilli, Appalaraju ; Howard, Ryan ; Upadhyaya, Jasbir D. ; Bhullar, Rajinder P. ; Chelikani, Prashen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c362t-bf3f88e77811f76aea9bad6bd5a2a71ca59ab76f19a07281cfb47fdd698a04303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bitter blockers</topic><topic>Bitter taste receptors (T2Rs)</topic><topic>Cholesterol</topic><topic>Constitutive active mutants</topic><topic>G protein-coupled receptor (GPCR)</topic><topic>Humans</topic><topic>Ligand bias</topic><topic>Ligands</topic><topic>Receptors, G-Protein-Coupled - chemistry</topic><topic>Receptors, G-Protein-Coupled - genetics</topic><topic>Receptors, G-Protein-Coupled - metabolism</topic><topic>Structural water molecules</topic><topic>Taste Perception - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jaggupilli, Appalaraju</creatorcontrib><creatorcontrib>Howard, Ryan</creatorcontrib><creatorcontrib>Upadhyaya, Jasbir D.</creatorcontrib><creatorcontrib>Bhullar, Rajinder P.</creatorcontrib><creatorcontrib>Chelikani, Prashen</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The international journal of biochemistry & cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jaggupilli, Appalaraju</au><au>Howard, Ryan</au><au>Upadhyaya, Jasbir D.</au><au>Bhullar, Rajinder P.</au><au>Chelikani, Prashen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bitter taste receptors: Novel insights into the biochemistry and pharmacology</atitle><jtitle>The international journal of biochemistry & cell biology</jtitle><addtitle>Int J Biochem Cell Biol</addtitle><date>2016-08</date><risdate>2016</risdate><volume>77</volume><issue>Pt B</issue><spage>184</spage><epage>196</epage><pages>184-196</pages><issn>1357-2725</issn><eissn>1878-5875</eissn><abstract>Bitter taste receptors (T2Rs) belong to the super family of G protein-coupled receptors (GPCRs). There are 25 T2Rs expressed in humans, and these interact with a large and diverse group of bitter ligands. T2Rs are expressed in many extra-oral tissues and can perform diverse physiological roles. Structure-function studies led to the identification of similarities and dissimilarities between T2Rs and Class A GPCRs including amino acid conservation and novel motifs. However, the efficacy of most of the T2R ligands is not yet elucidated and the biochemical pharmacology of T2Rs is poorly understood. Recent studies on T2Rs characterized novel ligands including blockers for these receptors that include inverse agonist and antagonists. In this review we discuss the techniques used for elucidating bitter blockers, concept of ligand bias, generic amino acid numbering, the role of cholesterol, and conserved water molecules in the biochemistry and pharmacology of T2Rs.</abstract><cop>Netherlands</cop><pub>Elsevier Ltd</pub><pmid>26995065</pmid><doi>10.1016/j.biocel.2016.03.005</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1357-2725 |
| ispartof | The international journal of biochemistry & cell biology, 2016-08, Vol.77 (Pt B), p.184-196 |
| issn | 1357-2725 1878-5875 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1807277796 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Bitter blockers Bitter taste receptors (T2Rs) Cholesterol Constitutive active mutants G protein-coupled receptor (GPCR) Humans Ligand bias Ligands Receptors, G-Protein-Coupled - chemistry Receptors, G-Protein-Coupled - genetics Receptors, G-Protein-Coupled - metabolism Structural water molecules Taste Perception - drug effects |
| title | Bitter taste receptors: Novel insights into the biochemistry and pharmacology |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T16%3A00%3A03IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Bitter%20taste%20receptors:%20Novel%20insights%20into%20the%20biochemistry%20and%20pharmacology&rft.jtitle=The%20international%20journal%20of%20biochemistry%20&%20cell%20biology&rft.au=Jaggupilli,%20Appalaraju&rft.date=2016-08&rft.volume=77&rft.issue=Pt%20B&rft.spage=184&rft.epage=196&rft.pages=184-196&rft.issn=1357-2725&rft.eissn=1878-5875&rft_id=info:doi/10.1016/j.biocel.2016.03.005&rft_dat=%3Cproquest_cross%3E1807277796%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1807277796&rft_id=info:pmid/26995065&rft_els_id=S1357272516300590&rfr_iscdi=true |