Loading…

Water Adaptation Strategy in Anuran Amphibians: Molecular Diversity of Aquaporin

Most adult anuran amphibians except for the aquatic species absorb water across the ventral pelvic skin and reabsorb it from urine in the urinary bladder. Many terrestrial and arboreal species use a region in the posterior or pelvic region of the ventral skin that is specialized for rapid rehydratio...

Full description

Saved in:
Bibliographic Details
Published in:Endocrinology (Philadelphia) 2010-01, Vol.151 (1), p.165-173
Main Authors: Ogushi, Yuji, Akabane, Gen, Hasegawa, Takahiro, Mochida, Hiroshi, Matsuda, Manabu, Suzuki, Masakazu, Tanaka, Shigeyasu
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323
cites cdi_FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323
container_end_page 173
container_issue 1
container_start_page 165
container_title Endocrinology (Philadelphia)
container_volume 151
creator Ogushi, Yuji
Akabane, Gen
Hasegawa, Takahiro
Mochida, Hiroshi
Matsuda, Manabu
Suzuki, Masakazu
Tanaka, Shigeyasu
description Most adult anuran amphibians except for the aquatic species absorb water across the ventral pelvic skin and reabsorb it from urine in the urinary bladder. Many terrestrial and arboreal species use a region in the posterior or pelvic region of the ventral skin that is specialized for rapid rehydration from shallow water sources or moist substrates. Periods of terrestrial activity can be prolonged by reabsorption of dilute urine from the urinary bladder. Aquaporin (AQP), a water channel protein, plays a fundamental role in these water absorption/reabsorption processes, which are regulated by antidiuretic hormone. Characterization of AQPs from various anurans revealed that the unique water homeostasis is basically mediated by two types of anuran-specific AQPs, i.e. ventral pelvic skin and urinary bladder type, respectively. The bladder-type AQP is further expressed in the pelvic skin of terrestrial and arboreal species, together with the pelvic skin-type AQP. In contrast, the pelvic skin-type AQP (AQP-x3) of the aquatic Xenopus has lost the ability of efficient protein production. The extra C-terminal tail in AQP-x3 consisting of 33 nucleotides within the coding region appears to participate in the posttranscriptional regulation of AQP-x3 gene expression by attenuating protein expression. The positive transcriptional regulation of bladder-type AQP in the pelvic skin and negative posttranscriptional regulation of pelvic skin-type AQP provide flexibility in the water regulation mechanisms, which might have contributed to the evolutionary adaptation of anurans to a wide variety of water environments. Adaptation in different water environments of anuran amphibians is brought by molecular diversity of aquaporin, a water channel, expressed in the ventral pelvic skin.
doi_str_mv 10.1210/en.2009-0841
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_734205600</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1210/en.2009-0841</oup_id><sourcerecordid>3130608995</sourcerecordid><originalsourceid>FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323</originalsourceid><addsrcrecordid>eNp1kE2LFDEQhoMo7uzqzbM0iHix18rXJO1tWNcPWFFQ8Rhquqs1S0_Sm3QL8-_NMI0DoqdKioeqeh_GnnC45ILDKwqXAqCpwSp-j614o3RtuIH7bAXAZW2EMGfsPOfb8lVKyYfsjDdWK7s2K_b5O06Uqk2H44STj6H6MqXS-rGvfKg2YU5Yym786bceQ35dfYwDtfOAqXrjf1HKftpXsa82dzOOMfnwiD3occj0eKkX7Nvb669X7-ubT-8-XG1u6lYLO9WWo22RyEBvGsmNLI-1ajQaJCu3QFqrVqNEaW1vO-AdCBLUKwN220shL9iL49wxxbuZ8uR2Prc0DBgoztkZqQToNUAhn_1F3sY5hXKck1zCGmzT6EK9PFJtijkn6t2Y_A7T3nFwB9GOgjuIdgfRBX-6DJ23O-pO8GK2AM8XAHOLQ188tj7_4YSQsoTWpxxxHv-3sl5WyiNJoYttUU1jopxPaf556G_q76FO</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3130608995</pqid></control><display><type>article</type><title>Water Adaptation Strategy in Anuran Amphibians: Molecular Diversity of Aquaporin</title><source>Oxford Journals Online</source><creator>Ogushi, Yuji ; Akabane, Gen ; Hasegawa, Takahiro ; Mochida, Hiroshi ; Matsuda, Manabu ; Suzuki, Masakazu ; Tanaka, Shigeyasu</creator><creatorcontrib>Ogushi, Yuji ; Akabane, Gen ; Hasegawa, Takahiro ; Mochida, Hiroshi ; Matsuda, Manabu ; Suzuki, Masakazu ; Tanaka, Shigeyasu</creatorcontrib><description>Most adult anuran amphibians except for the aquatic species absorb water across the ventral pelvic skin and reabsorb it from urine in the urinary bladder. Many terrestrial and arboreal species use a region in the posterior or pelvic region of the ventral skin that is specialized for rapid rehydration from shallow water sources or moist substrates. Periods of terrestrial activity can be prolonged by reabsorption of dilute urine from the urinary bladder. Aquaporin (AQP), a water channel protein, plays a fundamental role in these water absorption/reabsorption processes, which are regulated by antidiuretic hormone. Characterization of AQPs from various anurans revealed that the unique water homeostasis is basically mediated by two types of anuran-specific AQPs, i.e. ventral pelvic skin and urinary bladder type, respectively. The bladder-type AQP is further expressed in the pelvic skin of terrestrial and arboreal species, together with the pelvic skin-type AQP. In contrast, the pelvic skin-type AQP (AQP-x3) of the aquatic Xenopus has lost the ability of efficient protein production. The extra C-terminal tail in AQP-x3 consisting of 33 nucleotides within the coding region appears to participate in the posttranscriptional regulation of AQP-x3 gene expression by attenuating protein expression. The positive transcriptional regulation of bladder-type AQP in the pelvic skin and negative posttranscriptional regulation of pelvic skin-type AQP provide flexibility in the water regulation mechanisms, which might have contributed to the evolutionary adaptation of anurans to a wide variety of water environments. Adaptation in different water environments of anuran amphibians is brought by molecular diversity of aquaporin, a water channel, expressed in the ventral pelvic skin.</description><identifier>ISSN: 0013-7227</identifier><identifier>EISSN: 1945-7170</identifier><identifier>DOI: 10.1210/en.2009-0841</identifier><identifier>PMID: 19854867</identifier><identifier>CODEN: ENDOAO</identifier><language>eng</language><publisher>Chevy Chase, MD: Endocrine Society</publisher><subject>Adaptation ; Adaptation, Biological - drug effects ; Adaptation, Biological - genetics ; Amino Acid Sequence ; Amphibians ; Animals ; Antidiuretics ; Anura - genetics ; Anura - metabolism ; Anura - physiology ; Aquaporins ; Aquaporins - genetics ; Aquaporins - metabolism ; Aquaporins - physiology ; Biological and medical sciences ; Bladder ; Ecological adaptation ; Ecosystem ; Environmental regulations ; Female ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation - drug effects ; Gene regulation ; Genetic Variation - physiology ; Homeostasis ; Male ; Molecular Sequence Data ; Nucleotides ; Post-transcription ; Protein structure ; Proteins ; Reabsorption ; Rehydration ; Sequence Homology, Amino Acid ; Shallow water ; Skin ; Species Specificity ; Urinary bladder ; Urinary Bladder - metabolism ; Urine ; Vertebrates: endocrinology ; Water - metabolism ; Water - pharmacology ; Water absorption ; Water-Electrolyte Balance - drug effects ; Water-Electrolyte Balance - genetics</subject><ispartof>Endocrinology (Philadelphia), 2010-01, Vol.151 (1), p.165-173</ispartof><rights>Copyright © 2010 by The Endocrine Society 2010</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 by The Endocrine Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323</citedby><cites>FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=22337375$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19854867$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogushi, Yuji</creatorcontrib><creatorcontrib>Akabane, Gen</creatorcontrib><creatorcontrib>Hasegawa, Takahiro</creatorcontrib><creatorcontrib>Mochida, Hiroshi</creatorcontrib><creatorcontrib>Matsuda, Manabu</creatorcontrib><creatorcontrib>Suzuki, Masakazu</creatorcontrib><creatorcontrib>Tanaka, Shigeyasu</creatorcontrib><title>Water Adaptation Strategy in Anuran Amphibians: Molecular Diversity of Aquaporin</title><title>Endocrinology (Philadelphia)</title><addtitle>Endocrinology</addtitle><description>Most adult anuran amphibians except for the aquatic species absorb water across the ventral pelvic skin and reabsorb it from urine in the urinary bladder. Many terrestrial and arboreal species use a region in the posterior or pelvic region of the ventral skin that is specialized for rapid rehydration from shallow water sources or moist substrates. Periods of terrestrial activity can be prolonged by reabsorption of dilute urine from the urinary bladder. Aquaporin (AQP), a water channel protein, plays a fundamental role in these water absorption/reabsorption processes, which are regulated by antidiuretic hormone. Characterization of AQPs from various anurans revealed that the unique water homeostasis is basically mediated by two types of anuran-specific AQPs, i.e. ventral pelvic skin and urinary bladder type, respectively. The bladder-type AQP is further expressed in the pelvic skin of terrestrial and arboreal species, together with the pelvic skin-type AQP. In contrast, the pelvic skin-type AQP (AQP-x3) of the aquatic Xenopus has lost the ability of efficient protein production. The extra C-terminal tail in AQP-x3 consisting of 33 nucleotides within the coding region appears to participate in the posttranscriptional regulation of AQP-x3 gene expression by attenuating protein expression. The positive transcriptional regulation of bladder-type AQP in the pelvic skin and negative posttranscriptional regulation of pelvic skin-type AQP provide flexibility in the water regulation mechanisms, which might have contributed to the evolutionary adaptation of anurans to a wide variety of water environments. Adaptation in different water environments of anuran amphibians is brought by molecular diversity of aquaporin, a water channel, expressed in the ventral pelvic skin.</description><subject>Adaptation</subject><subject>Adaptation, Biological - drug effects</subject><subject>Adaptation, Biological - genetics</subject><subject>Amino Acid Sequence</subject><subject>Amphibians</subject><subject>Animals</subject><subject>Antidiuretics</subject><subject>Anura - genetics</subject><subject>Anura - metabolism</subject><subject>Anura - physiology</subject><subject>Aquaporins</subject><subject>Aquaporins - genetics</subject><subject>Aquaporins - metabolism</subject><subject>Aquaporins - physiology</subject><subject>Biological and medical sciences</subject><subject>Bladder</subject><subject>Ecological adaptation</subject><subject>Ecosystem</subject><subject>Environmental regulations</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation - drug effects</subject><subject>Gene regulation</subject><subject>Genetic Variation - physiology</subject><subject>Homeostasis</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Nucleotides</subject><subject>Post-transcription</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Reabsorption</subject><subject>Rehydration</subject><subject>Sequence Homology, Amino Acid</subject><subject>Shallow water</subject><subject>Skin</subject><subject>Species Specificity</subject><subject>Urinary bladder</subject><subject>Urinary Bladder - metabolism</subject><subject>Urine</subject><subject>Vertebrates: endocrinology</subject><subject>Water - metabolism</subject><subject>Water - pharmacology</subject><subject>Water absorption</subject><subject>Water-Electrolyte Balance - drug effects</subject><subject>Water-Electrolyte Balance - genetics</subject><issn>0013-7227</issn><issn>1945-7170</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp1kE2LFDEQhoMo7uzqzbM0iHix18rXJO1tWNcPWFFQ8Rhquqs1S0_Sm3QL8-_NMI0DoqdKioeqeh_GnnC45ILDKwqXAqCpwSp-j614o3RtuIH7bAXAZW2EMGfsPOfb8lVKyYfsjDdWK7s2K_b5O06Uqk2H44STj6H6MqXS-rGvfKg2YU5Yym786bceQ35dfYwDtfOAqXrjf1HKftpXsa82dzOOMfnwiD3occj0eKkX7Nvb669X7-ubT-8-XG1u6lYLO9WWo22RyEBvGsmNLI-1ajQaJCu3QFqrVqNEaW1vO-AdCBLUKwN220shL9iL49wxxbuZ8uR2Prc0DBgoztkZqQToNUAhn_1F3sY5hXKck1zCGmzT6EK9PFJtijkn6t2Y_A7T3nFwB9GOgjuIdgfRBX-6DJ23O-pO8GK2AM8XAHOLQ188tj7_4YSQsoTWpxxxHv-3sl5WyiNJoYttUU1jopxPaf556G_q76FO</recordid><startdate>201001</startdate><enddate>201001</enddate><creator>Ogushi, Yuji</creator><creator>Akabane, Gen</creator><creator>Hasegawa, Takahiro</creator><creator>Mochida, Hiroshi</creator><creator>Matsuda, Manabu</creator><creator>Suzuki, Masakazu</creator><creator>Tanaka, Shigeyasu</creator><general>Endocrine Society</general><general>Oxford University Press</general><scope>IQODW</scope><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>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>201001</creationdate><title>Water Adaptation Strategy in Anuran Amphibians: Molecular Diversity of Aquaporin</title><author>Ogushi, Yuji ; Akabane, Gen ; Hasegawa, Takahiro ; Mochida, Hiroshi ; Matsuda, Manabu ; Suzuki, Masakazu ; Tanaka, Shigeyasu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Adaptation</topic><topic>Adaptation, Biological - drug effects</topic><topic>Adaptation, Biological - genetics</topic><topic>Amino Acid Sequence</topic><topic>Amphibians</topic><topic>Animals</topic><topic>Antidiuretics</topic><topic>Anura - genetics</topic><topic>Anura - metabolism</topic><topic>Anura - physiology</topic><topic>Aquaporins</topic><topic>Aquaporins - genetics</topic><topic>Aquaporins - metabolism</topic><topic>Aquaporins - physiology</topic><topic>Biological and medical sciences</topic><topic>Bladder</topic><topic>Ecological adaptation</topic><topic>Ecosystem</topic><topic>Environmental regulations</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Gene Expression Regulation - drug effects</topic><topic>Gene regulation</topic><topic>Genetic Variation - physiology</topic><topic>Homeostasis</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Nucleotides</topic><topic>Post-transcription</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Reabsorption</topic><topic>Rehydration</topic><topic>Sequence Homology, Amino Acid</topic><topic>Shallow water</topic><topic>Skin</topic><topic>Species Specificity</topic><topic>Urinary bladder</topic><topic>Urinary Bladder - metabolism</topic><topic>Urine</topic><topic>Vertebrates: endocrinology</topic><topic>Water - metabolism</topic><topic>Water - pharmacology</topic><topic>Water absorption</topic><topic>Water-Electrolyte Balance - drug effects</topic><topic>Water-Electrolyte Balance - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogushi, Yuji</creatorcontrib><creatorcontrib>Akabane, Gen</creatorcontrib><creatorcontrib>Hasegawa, Takahiro</creatorcontrib><creatorcontrib>Mochida, Hiroshi</creatorcontrib><creatorcontrib>Matsuda, Manabu</creatorcontrib><creatorcontrib>Suzuki, Masakazu</creatorcontrib><creatorcontrib>Tanaka, Shigeyasu</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Endocrinology (Philadelphia)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogushi, Yuji</au><au>Akabane, Gen</au><au>Hasegawa, Takahiro</au><au>Mochida, Hiroshi</au><au>Matsuda, Manabu</au><au>Suzuki, Masakazu</au><au>Tanaka, Shigeyasu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Water Adaptation Strategy in Anuran Amphibians: Molecular Diversity of Aquaporin</atitle><jtitle>Endocrinology (Philadelphia)</jtitle><addtitle>Endocrinology</addtitle><date>2010-01</date><risdate>2010</risdate><volume>151</volume><issue>1</issue><spage>165</spage><epage>173</epage><pages>165-173</pages><issn>0013-7227</issn><eissn>1945-7170</eissn><coden>ENDOAO</coden><abstract>Most adult anuran amphibians except for the aquatic species absorb water across the ventral pelvic skin and reabsorb it from urine in the urinary bladder. Many terrestrial and arboreal species use a region in the posterior or pelvic region of the ventral skin that is specialized for rapid rehydration from shallow water sources or moist substrates. Periods of terrestrial activity can be prolonged by reabsorption of dilute urine from the urinary bladder. Aquaporin (AQP), a water channel protein, plays a fundamental role in these water absorption/reabsorption processes, which are regulated by antidiuretic hormone. Characterization of AQPs from various anurans revealed that the unique water homeostasis is basically mediated by two types of anuran-specific AQPs, i.e. ventral pelvic skin and urinary bladder type, respectively. The bladder-type AQP is further expressed in the pelvic skin of terrestrial and arboreal species, together with the pelvic skin-type AQP. In contrast, the pelvic skin-type AQP (AQP-x3) of the aquatic Xenopus has lost the ability of efficient protein production. The extra C-terminal tail in AQP-x3 consisting of 33 nucleotides within the coding region appears to participate in the posttranscriptional regulation of AQP-x3 gene expression by attenuating protein expression. The positive transcriptional regulation of bladder-type AQP in the pelvic skin and negative posttranscriptional regulation of pelvic skin-type AQP provide flexibility in the water regulation mechanisms, which might have contributed to the evolutionary adaptation of anurans to a wide variety of water environments. Adaptation in different water environments of anuran amphibians is brought by molecular diversity of aquaporin, a water channel, expressed in the ventral pelvic skin.</abstract><cop>Chevy Chase, MD</cop><pub>Endocrine Society</pub><pmid>19854867</pmid><doi>10.1210/en.2009-0841</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0013-7227
ispartof Endocrinology (Philadelphia), 2010-01, Vol.151 (1), p.165-173
issn 0013-7227
1945-7170
language eng
recordid cdi_proquest_miscellaneous_734205600
source Oxford Journals Online
subjects Adaptation
Adaptation, Biological - drug effects
Adaptation, Biological - genetics
Amino Acid Sequence
Amphibians
Animals
Antidiuretics
Anura - genetics
Anura - metabolism
Anura - physiology
Aquaporins
Aquaporins - genetics
Aquaporins - metabolism
Aquaporins - physiology
Biological and medical sciences
Bladder
Ecological adaptation
Ecosystem
Environmental regulations
Female
Fundamental and applied biological sciences. Psychology
Gene expression
Gene Expression Regulation - drug effects
Gene regulation
Genetic Variation - physiology
Homeostasis
Male
Molecular Sequence Data
Nucleotides
Post-transcription
Protein structure
Proteins
Reabsorption
Rehydration
Sequence Homology, Amino Acid
Shallow water
Skin
Species Specificity
Urinary bladder
Urinary Bladder - metabolism
Urine
Vertebrates: endocrinology
Water - metabolism
Water - pharmacology
Water absorption
Water-Electrolyte Balance - drug effects
Water-Electrolyte Balance - genetics
title Water Adaptation Strategy in Anuran Amphibians: Molecular Diversity of Aquaporin
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T19%3A20%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=Water%20Adaptation%20Strategy%20in%20Anuran%20Amphibians:%20Molecular%20Diversity%20of%20Aquaporin&rft.jtitle=Endocrinology%20(Philadelphia)&rft.au=Ogushi,%20Yuji&rft.date=2010-01&rft.volume=151&rft.issue=1&rft.spage=165&rft.epage=173&rft.pages=165-173&rft.issn=0013-7227&rft.eissn=1945-7170&rft.coden=ENDOAO&rft_id=info:doi/10.1210/en.2009-0841&rft_dat=%3Cproquest_cross%3E3130608995%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c528t-81a8caee70f79317370f6495a7ae83b0e554c5a3a388f8d01d02e2ef4708bf323%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=3130608995&rft_id=info:pmid/19854867&rft_oup_id=10.1210/en.2009-0841&rfr_iscdi=true