{"corpus_id":262936361,"paper_sha":"b1ceca9db01e931a292f2b12b7c5b5e487497c8e","doi":"10.1038/srep07795","arxiv_id":null,"pmid":25589229,"pmcid":"4295104","mag_id":2015523353,"dblp_id":null,"acl_id":null,"title":"Functional characterization of aquaporins and aquaglyceroporins of the yellow fever mosquito, Aedes aegypti","year":2015,"publication_date":"2015-01-15","venue":"Scientific Reports","journal":{"name":"Scientific Reports","pages":null,"volume":"5"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article"],"s2_fields_of_study":["Biology","Medicine","Environmental Science"],"reference_count":50,"citation_count":58,"influential_citation_count":5,"is_open_access":true,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Aedes","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D000330"},{"d":"Animals","mj":false,"ui":"D000818"},{"d":"Aquaglyceroporins","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D051397"},{"d":"Aquaporins","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D020346"},{"d":"Biological Assay","mj":false,"ui":"D001681"},{"d":"Biological Transport","mj":false,"ui":"D001692"},{"d":"Cell Membrane Permeability","mj":false,"ui":"D002463"},{"d":"Desiccation","mj":false,"ui":"D003890"},{"d":"Gene Expression Profiling","mj":false,"ui":"D020869"},{"d":"Gene Expression Regulation","mj":false,"ui":"D005786"},{"d":"Gene Knockdown Techniques","mj":false,"ui":"D055785"},{"d":"Insect Proteins","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D019476"},{"d":"Oocytes","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D009865"},{"d":"Organ Specificity","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"}],"ui":"D009928"},{"d":"RNA Interference","mj":false,"ui":"D034622"},{"d":"Water","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D014867"},{"d":"Xenopus","mj":false,"ui":"D014981"},{"d":"Yellow Fever","mj":false,"qs":[{"q":"parasitology","mj":true,"ui":"Q000469"}],"ui":"D015004"}],"chemicals":[{"n":"Aquaglyceroporins","ui":"D051397","reg":"0"},{"n":"Aquaporins","ui":"D020346","reg":"0"},{"n":"Insect Proteins","ui":"D019476","reg":"0"},{"n":"Water","ui":"D014867","reg":"059QF0KO0R"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":"https://www.nature.com/articles/srep07795.pdf","s2_open_access_landing_url":"https://www.semanticscholar.org/paper/b1ceca9db01e931a292f2b12b7c5b5e487497c8e","s2_open_access_license":"CCBYNCND","s2_open_access_status":"GOLD","pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"After taking vertebrate blood, female mosquitoes quickly shed excess water and ions while retaining and concentrating the mostly proteinaceous nutrients. Aquaporins (AQPs) are an evolutionary conserved family of membrane transporter proteins that regulate the flow of water and in some cases glycerol and other small molecules across cellular membranes. In a previous study, we found six putative AQP genes in the genome of the yellow fever mosquito, Ae. aegypti and demonstrated the involvement of three of them in the blood meal-induced diuresis. Here we characterized AQP expression in different tissues before and after a blood meal, explored the substrate specificity of AQPs expressed in the Malpighian tubules and performed RNAi-mediated knockdown and tested for changes in mosquito desiccation resistance. We found that AQPs are generally down-regulated 24 hrs after a blood meal. Ae. aegypti AQP 1 strictly transports water, AQP 2 and 5 demonstrate limited solute transport, but primarily function as water transporters. AQP 4 is an aquaglyceroporin with multiple substrates. Knockdown of AQPs expressed in the MTs increased survival of Ae. aegypti under dry conditions. We conclude that Malpighian tubules of adult female yellow fever mosquitoes utilize three distinct AQPs and one aquaglyceroporin in their osmoregulatory functions.","claims":[{"public_id":"cl_010f36383bb3431ef5f083d030b98201","status":"active","text":"AQP 4 functions as an aquaglyceroporin with multiple substrates.","confidence":0.93,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_010f36383bb3431ef5f083d030b98201"},{"public_id":"cl_9854457492f7a54d56cf3bdf6a57511f","status":"active","text":"Aedes aegypti AQP 1 strictly transports water, while AQP 2 and AQP 5 have limited solute transport but mainly function as water transporters.","confidence":0.95,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous 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