Biochemical evidence for a P2Y-like receptor in Tetrahymena thermophila
Extracellular nucleotides are ubiquitous signaling molecules. ATP signals through two receptor types: the ionotropic P2X receptors, and the metabotropic P2Y receptors. ATP acts as a chemorepellent in Tetrahymena thermophila, where it causes a distinct avoidance response. The intracellular mechanisms...
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Veröffentlicht in: | Journal of Comparative Physiology 2003-10, Vol.189 (10), p.781-789 |
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description | Extracellular nucleotides are ubiquitous signaling molecules. ATP signals through two receptor types: the ionotropic P2X receptors, and the metabotropic P2Y receptors. ATP acts as a chemorepellent in Tetrahymena thermophila, where it causes a distinct avoidance response. The intracellular mechanisms by which ATP causes avoidance in this organism, however, are unknown. In this study, we use in vivo pharmacological assays along with enzyme immuno-assays to obtain information about the ATP chemorepellent pathway and its associated second messenger systems. Our data show strong similarities between the presumed ATP receptor of T. thermophila and members of the P2Y family of receptors. The ATP response of T. thermophila appears to be coupled to phospholipase C, a defining characteristic of the P2Y receptor family. In addition, the ATP chemoresponse appears to be linked to a G(i/o) protein, nitric oxide synthase, and adenylyl cyclase, all of which are characteristic of some P2Y receptors. This is an important first step in describing the pathways involved in ATP chemoresponse of this organism. |
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ATP signals through two receptor types: the ionotropic P2X receptors, and the metabotropic P2Y receptors. ATP acts as a chemorepellent in Tetrahymena thermophila, where it causes a distinct avoidance response. The intracellular mechanisms by which ATP causes avoidance in this organism, however, are unknown. In this study, we use in vivo pharmacological assays along with enzyme immuno-assays to obtain information about the ATP chemorepellent pathway and its associated second messenger systems. Our data show strong similarities between the presumed ATP receptor of T. thermophila and members of the P2Y family of receptors. The ATP response of T. thermophila appears to be coupled to phospholipase C, a defining characteristic of the P2Y receptor family. In addition, the ATP chemoresponse appears to be linked to a G(i/o) protein, nitric oxide synthase, and adenylyl cyclase, all of which are characteristic of some P2Y receptors. This is an important first step in describing the pathways involved in ATP chemoresponse of this organism.</description><identifier>ISSN: 0340-7594</identifier><identifier>EISSN: 1432-1351</identifier><identifier>DOI: 10.1007/s00359-003-0453-8</identifier><identifier>PMID: 13680132</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>Adenosine Triphosphate - analogs & derivatives ; Adenosine Triphosphate - metabolism ; Adenosine Triphosphate - pharmacology ; Animals ; Behavior, Animal ; Chelating Agents - pharmacology ; Dose-Response Relationship, Drug ; Egtazic Acid - analogs & derivatives ; Egtazic Acid - pharmacology ; Enzyme Inhibitors - pharmacology ; Enzyme-Linked Immunosorbent Assay ; Escape Reaction - drug effects ; Guanosine Diphosphate - analogs & derivatives ; Guanosine Diphosphate - pharmacology ; Nitric oxide ; Pertussis Toxin - pharmacology ; Proteins ; Receptors, Purinergic P2 - chemistry ; Receptors, Purinergic P2 - metabolism ; Rodents ; Second Messenger Systems - drug effects ; Tetrahymena thermophila - cytology ; Tetrahymena thermophila - metabolism ; Thionucleotides - pharmacology</subject><ispartof>Journal of Comparative Physiology, 2003-10, Vol.189 (10), p.781-789</ispartof><rights>Springer-Verlag 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c324t-3398c7acfef50985006997c5dee5745915fc2bcec8e3c4a549fc1421309d34d13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13680132$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rosner, B N</creatorcontrib><creatorcontrib>Bartholomew, J N</creatorcontrib><creatorcontrib>Gaines, C D</creatorcontrib><creatorcontrib>Riddle, M L</creatorcontrib><creatorcontrib>Everett, H A</creatorcontrib><creatorcontrib>Rulapaugh, K G</creatorcontrib><creatorcontrib>Nickerson, L E</creatorcontrib><creatorcontrib>Marshall, M R</creatorcontrib><creatorcontrib>Kuruvilla, H G</creatorcontrib><title>Biochemical evidence for a P2Y-like receptor in Tetrahymena thermophila</title><title>Journal of Comparative Physiology</title><addtitle>J Comp Physiol A Neuroethol Sens Neural Behav Physiol</addtitle><description>Extracellular nucleotides are ubiquitous signaling molecules. ATP signals through two receptor types: the ionotropic P2X receptors, and the metabotropic P2Y receptors. ATP acts as a chemorepellent in Tetrahymena thermophila, where it causes a distinct avoidance response. The intracellular mechanisms by which ATP causes avoidance in this organism, however, are unknown. In this study, we use in vivo pharmacological assays along with enzyme immuno-assays to obtain information about the ATP chemorepellent pathway and its associated second messenger systems. Our data show strong similarities between the presumed ATP receptor of T. thermophila and members of the P2Y family of receptors. The ATP response of T. thermophila appears to be coupled to phospholipase C, a defining characteristic of the P2Y receptor family. In addition, the ATP chemoresponse appears to be linked to a G(i/o) protein, nitric oxide synthase, and adenylyl cyclase, all of which are characteristic of some P2Y receptors. 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Academic</collection><jtitle>Journal of Comparative Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rosner, B N</au><au>Bartholomew, J N</au><au>Gaines, C D</au><au>Riddle, M L</au><au>Everett, H A</au><au>Rulapaugh, K G</au><au>Nickerson, L E</au><au>Marshall, M R</au><au>Kuruvilla, H G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical evidence for a P2Y-like receptor in Tetrahymena thermophila</atitle><jtitle>Journal of Comparative Physiology</jtitle><addtitle>J Comp Physiol A Neuroethol Sens Neural Behav Physiol</addtitle><date>2003-10</date><risdate>2003</risdate><volume>189</volume><issue>10</issue><spage>781</spage><epage>789</epage><pages>781-789</pages><issn>0340-7594</issn><eissn>1432-1351</eissn><abstract>Extracellular nucleotides are ubiquitous signaling molecules. ATP signals through two receptor types: the ionotropic P2X receptors, and the metabotropic P2Y receptors. ATP acts as a chemorepellent in Tetrahymena thermophila, where it causes a distinct avoidance response. The intracellular mechanisms by which ATP causes avoidance in this organism, however, are unknown. In this study, we use in vivo pharmacological assays along with enzyme immuno-assays to obtain information about the ATP chemorepellent pathway and its associated second messenger systems. Our data show strong similarities between the presumed ATP receptor of T. thermophila and members of the P2Y family of receptors. The ATP response of T. thermophila appears to be coupled to phospholipase C, a defining characteristic of the P2Y receptor family. In addition, the ATP chemoresponse appears to be linked to a G(i/o) protein, nitric oxide synthase, and adenylyl cyclase, all of which are characteristic of some P2Y receptors. This is an important first step in describing the pathways involved in ATP chemoresponse of this organism.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>13680132</pmid><doi>10.1007/s00359-003-0453-8</doi><tpages>9</tpages></addata></record> |
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subjects | Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Adenosine Triphosphate - pharmacology Animals Behavior, Animal Chelating Agents - pharmacology Dose-Response Relationship, Drug Egtazic Acid - analogs & derivatives Egtazic Acid - pharmacology Enzyme Inhibitors - pharmacology Enzyme-Linked Immunosorbent Assay Escape Reaction - drug effects Guanosine Diphosphate - analogs & derivatives Guanosine Diphosphate - pharmacology Nitric oxide Pertussis Toxin - pharmacology Proteins Receptors, Purinergic P2 - chemistry Receptors, Purinergic P2 - metabolism Rodents Second Messenger Systems - drug effects Tetrahymena thermophila - cytology Tetrahymena thermophila - metabolism Thionucleotides - pharmacology |
title | Biochemical evidence for a P2Y-like receptor in Tetrahymena thermophila |
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