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Postprandial change in glucose metabolism at the molecular level in the adipose tissue of omnivorous GIFT Oreochromis niloticus
The study reported here is the first to systematically investigate the postprandial change in glucose metabolism in the adipose tissue (AT) of an omnivorous fish. Sub-adult Genetically Improved Farmed Tilapia (GIFT) Oreochromis niloticus were sampled at 0, 1, 3, 8 and 24 h after feeding (HAF), and t...
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Published in: | Fisheries science 2019-01, Vol.85 (1), p.33-41 |
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container_title | Fisheries science |
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creator | Feng, Jing-Yun Liu, Qin-Qin Xu, Hang-Zhong Chen, Rui-Hong Luo, Li Lin, Shi-Mei Chen, Yong-Jun Wang, De-Shou |
description | The study reported here is the first to systematically investigate the postprandial change in glucose metabolism in the adipose tissue (AT) of an omnivorous fish. Sub-adult Genetically Improved Farmed Tilapia (GIFT)
Oreochromis niloticus
were sampled at 0, 1, 3, 8 and 24 h after feeding (HAF), and the time course of changes in glucose transport and glycolipid metabolism at the transcript level were analyzed in the AT. The plasma glucose level increased between 1 and 8 HAF, and the expression of glucose transporter 1a (
glut1a
) and
glut4
in the AT were stimulated at the same time. Concomitantly, the mRNA levels of glycolytic genes, such as hexokinase 1a (
hk1a
),
hk1b
, glucokinase and liver type of phosphofructokinase, were upregulated. The expression of glycogen synthase 1 and glycogen level in the AT increased between 3 and 8 HAF, suggesting that AT has the capacity to store excess glucose in tilapia. The decreased glycogen level together with upregulated transcription of glucose-6-phosphatase catalytic subunit a2 (
g6pca2
) at 24 HAF suggests that glycogen breakdown and glucose release from AT might contribute to circular glucose in tilapia. The opposite expression patterns between
g6pca2
and phosphoenolpyruvate carboxykinase (
pck
) paralogs suggest that
pck
might participate in glyceroneogenesis rather than gluconeogenesis in the AT of tilapia. The mRNA levels of both cytosolic
pck1
and mitochondrial
pck2
increased during the period 1–8 HAF, and the expressions of lipogenic genes, such as acetyl-CoA carboxylase α and fatty acid synthase, were upregulated between 3 and 8 HAF, suggesting that glyceroneogenesis was probably stimulated as a source of glyceride–glycerol for triglyceride synthesis in the AT of tilapia. Taken together, our preliminary data suggest that AT plays an important role in the regulation of postprandial glucose homeostasis in the omnivorous tilapia, at least at the molecular level. |
doi_str_mv | 10.1007/s12562-018-1251-0 |
format | article |
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Oreochromis niloticus
were sampled at 0, 1, 3, 8 and 24 h after feeding (HAF), and the time course of changes in glucose transport and glycolipid metabolism at the transcript level were analyzed in the AT. The plasma glucose level increased between 1 and 8 HAF, and the expression of glucose transporter 1a (
glut1a
) and
glut4
in the AT were stimulated at the same time. Concomitantly, the mRNA levels of glycolytic genes, such as hexokinase 1a (
hk1a
),
hk1b
, glucokinase and liver type of phosphofructokinase, were upregulated. The expression of glycogen synthase 1 and glycogen level in the AT increased between 3 and 8 HAF, suggesting that AT has the capacity to store excess glucose in tilapia. The decreased glycogen level together with upregulated transcription of glucose-6-phosphatase catalytic subunit a2 (
g6pca2
) at 24 HAF suggests that glycogen breakdown and glucose release from AT might contribute to circular glucose in tilapia. The opposite expression patterns between
g6pca2
and phosphoenolpyruvate carboxykinase (
pck
) paralogs suggest that
pck
might participate in glyceroneogenesis rather than gluconeogenesis in the AT of tilapia. The mRNA levels of both cytosolic
pck1
and mitochondrial
pck2
increased during the period 1–8 HAF, and the expressions of lipogenic genes, such as acetyl-CoA carboxylase α and fatty acid synthase, were upregulated between 3 and 8 HAF, suggesting that glyceroneogenesis was probably stimulated as a source of glyceride–glycerol for triglyceride synthesis in the AT of tilapia. Taken together, our preliminary data suggest that AT plays an important role in the regulation of postprandial glucose homeostasis in the omnivorous tilapia, at least at the molecular level.</description><identifier>ISSN: 0919-9268</identifier><identifier>EISSN: 1444-2906</identifier><identifier>DOI: 10.1007/s12562-018-1251-0</identifier><language>eng</language><publisher>Tokyo: Springer Japan</publisher><subject>Acetyl-CoA carboxylase ; Adipose tissue ; Aquaculture ; Biomedical and Life Sciences ; blood glucose ; Body fat ; Capacity ; carboxy-lyases ; Catalysis ; Fatty acids ; Fatty-acid synthase ; Fish ; Fish & Wildlife Biology & Management ; Fish farms ; Food Science ; Freshwater & Marine Ecology ; Freshwater fishes ; Genes ; Glucokinase ; Gluconeogenesis ; Glucose ; Glucose metabolism ; Glucose transport ; Glucose transporter ; glucose transporters ; Glucose-6-phosphatase ; Glycerol ; glyceroneogenesis ; Glycogen ; glycogen (starch) synthase ; Glycogen synthase ; glycolipids ; Glycolysis ; Hexokinase ; Homeostasis ; Life Sciences ; Liver ; Metabolism ; Mitochondria ; omnivores ; Oreochromis niloticus ; Original Article ; Phosphatase ; Phosphofructokinase ; phosphofructokinases ; protein subunits ; Tilapia ; Tissue ; Transcription ; triacylglycerols</subject><ispartof>Fisheries science, 2019-01, Vol.85 (1), p.33-41</ispartof><rights>Japanese Society of Fisheries Science 2018</rights><rights>Fisheries Science is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-49aa3bfc04b7c2bbf32f14ea08450cf64f8d34c87f3282eaeaad42603fbb24c43</citedby><cites>FETCH-LOGICAL-c376t-49aa3bfc04b7c2bbf32f14ea08450cf64f8d34c87f3282eaeaad42603fbb24c43</cites><orcidid>0000-0002-0427-7555</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2093912683/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2093912683?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,776,780,11667,27901,27902,36037,36038,44339,74638</link.rule.ids></links><search><creatorcontrib>Feng, Jing-Yun</creatorcontrib><creatorcontrib>Liu, Qin-Qin</creatorcontrib><creatorcontrib>Xu, Hang-Zhong</creatorcontrib><creatorcontrib>Chen, Rui-Hong</creatorcontrib><creatorcontrib>Luo, Li</creatorcontrib><creatorcontrib>Lin, Shi-Mei</creatorcontrib><creatorcontrib>Chen, Yong-Jun</creatorcontrib><creatorcontrib>Wang, De-Shou</creatorcontrib><title>Postprandial change in glucose metabolism at the molecular level in the adipose tissue of omnivorous GIFT Oreochromis niloticus</title><title>Fisheries science</title><addtitle>Fish Sci</addtitle><description>The study reported here is the first to systematically investigate the postprandial change in glucose metabolism in the adipose tissue (AT) of an omnivorous fish. Sub-adult Genetically Improved Farmed Tilapia (GIFT)
Oreochromis niloticus
were sampled at 0, 1, 3, 8 and 24 h after feeding (HAF), and the time course of changes in glucose transport and glycolipid metabolism at the transcript level were analyzed in the AT. The plasma glucose level increased between 1 and 8 HAF, and the expression of glucose transporter 1a (
glut1a
) and
glut4
in the AT were stimulated at the same time. Concomitantly, the mRNA levels of glycolytic genes, such as hexokinase 1a (
hk1a
),
hk1b
, glucokinase and liver type of phosphofructokinase, were upregulated. The expression of glycogen synthase 1 and glycogen level in the AT increased between 3 and 8 HAF, suggesting that AT has the capacity to store excess glucose in tilapia. The decreased glycogen level together with upregulated transcription of glucose-6-phosphatase catalytic subunit a2 (
g6pca2
) at 24 HAF suggests that glycogen breakdown and glucose release from AT might contribute to circular glucose in tilapia. The opposite expression patterns between
g6pca2
and phosphoenolpyruvate carboxykinase (
pck
) paralogs suggest that
pck
might participate in glyceroneogenesis rather than gluconeogenesis in the AT of tilapia. The mRNA levels of both cytosolic
pck1
and mitochondrial
pck2
increased during the period 1–8 HAF, and the expressions of lipogenic genes, such as acetyl-CoA carboxylase α and fatty acid synthase, were upregulated between 3 and 8 HAF, suggesting that glyceroneogenesis was probably stimulated as a source of glyceride–glycerol for triglyceride synthesis in the AT of tilapia. Taken together, our preliminary data suggest that AT plays an important role in the regulation of postprandial glucose homeostasis in the omnivorous tilapia, at least at the molecular level.</description><subject>Acetyl-CoA carboxylase</subject><subject>Adipose tissue</subject><subject>Aquaculture</subject><subject>Biomedical and Life Sciences</subject><subject>blood glucose</subject><subject>Body fat</subject><subject>Capacity</subject><subject>carboxy-lyases</subject><subject>Catalysis</subject><subject>Fatty acids</subject><subject>Fatty-acid synthase</subject><subject>Fish</subject><subject>Fish & Wildlife Biology & Management</subject><subject>Fish farms</subject><subject>Food Science</subject><subject>Freshwater & Marine Ecology</subject><subject>Freshwater fishes</subject><subject>Genes</subject><subject>Glucokinase</subject><subject>Gluconeogenesis</subject><subject>Glucose</subject><subject>Glucose metabolism</subject><subject>Glucose transport</subject><subject>Glucose transporter</subject><subject>glucose transporters</subject><subject>Glucose-6-phosphatase</subject><subject>Glycerol</subject><subject>glyceroneogenesis</subject><subject>Glycogen</subject><subject>glycogen (starch) synthase</subject><subject>Glycogen synthase</subject><subject>glycolipids</subject><subject>Glycolysis</subject><subject>Hexokinase</subject><subject>Homeostasis</subject><subject>Life Sciences</subject><subject>Liver</subject><subject>Metabolism</subject><subject>Mitochondria</subject><subject>omnivores</subject><subject>Oreochromis niloticus</subject><subject>Original Article</subject><subject>Phosphatase</subject><subject>Phosphofructokinase</subject><subject>phosphofructokinases</subject><subject>protein subunits</subject><subject>Tilapia</subject><subject>Tissue</subject><subject>Transcription</subject><subject>triacylglycerols</subject><issn>0919-9268</issn><issn>1444-2906</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>M0C</sourceid><recordid>eNp1kc1KAzEUhYMoWKsP4C7gxs3oTSadn6UUrYVCXdR1yGSSNiUzGZOZgitf3QwjCIKrhHu_czjcg9AtgQcCkD8GQhcZTYAUSfyRBM7QjDDGElpCdo5mUJIyKWlWXKKrEI4AkC2gmKGvNxf6zou2NsJieRDtXmHT4r0dpAsKN6oXlbMmNFj0uD_EibNKDlZ4bNVJ2REex6I23SjoTQiDwk5j17Tm5LwbAl6tX3Z465WTB-8aE3BrrOuNHMI1utDCBnXz887R-8vzbvmabLar9fJpk8g0z_qElUKklZbAqlzSqtIp1YQpAQVbgNQZ00WdMlnkcVFQJZQQNaMZpLqqKJMsnaP7ybfz7mNQoecxhlTWilbFhJxSSiCDPErm6O4PenSDb2M6TqFMSxKvmEaKTJT0LgSvNO-8aYT_5AT4WAmfKuGxEj5WwkdnOmlCZOOh_a_z_6Jv-miQtw</recordid><startdate>20190101</startdate><enddate>20190101</enddate><creator>Feng, Jing-Yun</creator><creator>Liu, Qin-Qin</creator><creator>Xu, Hang-Zhong</creator><creator>Chen, Rui-Hong</creator><creator>Luo, Li</creator><creator>Lin, Shi-Mei</creator><creator>Chen, Yong-Jun</creator><creator>Wang, De-Shou</creator><general>Springer Japan</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TN</scope><scope>7U7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7XB</scope><scope>87Z</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FRNLG</scope><scope>F~G</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H95</scope><scope>H98</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>L.-</scope><scope>L.G</scope><scope>LK8</scope><scope>M0C</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PCBAR</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-0427-7555</orcidid></search><sort><creationdate>20190101</creationdate><title>Postprandial change in glucose metabolism at the molecular level in the adipose tissue of omnivorous GIFT Oreochromis niloticus</title><author>Feng, Jing-Yun ; Liu, Qin-Qin ; Xu, Hang-Zhong ; Chen, Rui-Hong ; Luo, Li ; Lin, Shi-Mei ; Chen, Yong-Jun ; Wang, De-Shou</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-49aa3bfc04b7c2bbf32f14ea08450cf64f8d34c87f3282eaeaad42603fbb24c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Acetyl-CoA carboxylase</topic><topic>Adipose tissue</topic><topic>Aquaculture</topic><topic>Biomedical and Life Sciences</topic><topic>blood glucose</topic><topic>Body fat</topic><topic>Capacity</topic><topic>carboxy-lyases</topic><topic>Catalysis</topic><topic>Fatty acids</topic><topic>Fatty-acid synthase</topic><topic>Fish</topic><topic>Fish & Wildlife Biology & Management</topic><topic>Fish farms</topic><topic>Food Science</topic><topic>Freshwater & Marine Ecology</topic><topic>Freshwater fishes</topic><topic>Genes</topic><topic>Glucokinase</topic><topic>Gluconeogenesis</topic><topic>Glucose</topic><topic>Glucose metabolism</topic><topic>Glucose transport</topic><topic>Glucose transporter</topic><topic>glucose transporters</topic><topic>Glucose-6-phosphatase</topic><topic>Glycerol</topic><topic>glyceroneogenesis</topic><topic>Glycogen</topic><topic>glycogen (starch) synthase</topic><topic>Glycogen synthase</topic><topic>glycolipids</topic><topic>Glycolysis</topic><topic>Hexokinase</topic><topic>Homeostasis</topic><topic>Life Sciences</topic><topic>Liver</topic><topic>Metabolism</topic><topic>Mitochondria</topic><topic>omnivores</topic><topic>Oreochromis niloticus</topic><topic>Original Article</topic><topic>Phosphatase</topic><topic>Phosphofructokinase</topic><topic>phosphofructokinases</topic><topic>protein subunits</topic><topic>Tilapia</topic><topic>Tissue</topic><topic>Transcription</topic><topic>triacylglycerols</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, Jing-Yun</creatorcontrib><creatorcontrib>Liu, Qin-Qin</creatorcontrib><creatorcontrib>Xu, Hang-Zhong</creatorcontrib><creatorcontrib>Chen, Rui-Hong</creatorcontrib><creatorcontrib>Luo, Li</creatorcontrib><creatorcontrib>Lin, Shi-Mei</creatorcontrib><creatorcontrib>Chen, Yong-Jun</creatorcontrib><creatorcontrib>Wang, De-Shou</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Oceanic Abstracts</collection><collection>Toxicology Abstracts</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection</collection><collection>ProQuest SciTech 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(Corporate)</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Fisheries science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, Jing-Yun</au><au>Liu, Qin-Qin</au><au>Xu, Hang-Zhong</au><au>Chen, Rui-Hong</au><au>Luo, Li</au><au>Lin, Shi-Mei</au><au>Chen, Yong-Jun</au><au>Wang, De-Shou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Postprandial change in glucose metabolism at the molecular level in the adipose tissue of omnivorous GIFT Oreochromis niloticus</atitle><jtitle>Fisheries science</jtitle><stitle>Fish Sci</stitle><date>2019-01-01</date><risdate>2019</risdate><volume>85</volume><issue>1</issue><spage>33</spage><epage>41</epage><pages>33-41</pages><issn>0919-9268</issn><eissn>1444-2906</eissn><abstract>The study reported here is the first to systematically investigate the postprandial change in glucose metabolism in the adipose tissue (AT) of an omnivorous fish. Sub-adult Genetically Improved Farmed Tilapia (GIFT)
Oreochromis niloticus
were sampled at 0, 1, 3, 8 and 24 h after feeding (HAF), and the time course of changes in glucose transport and glycolipid metabolism at the transcript level were analyzed in the AT. The plasma glucose level increased between 1 and 8 HAF, and the expression of glucose transporter 1a (
glut1a
) and
glut4
in the AT were stimulated at the same time. Concomitantly, the mRNA levels of glycolytic genes, such as hexokinase 1a (
hk1a
),
hk1b
, glucokinase and liver type of phosphofructokinase, were upregulated. The expression of glycogen synthase 1 and glycogen level in the AT increased between 3 and 8 HAF, suggesting that AT has the capacity to store excess glucose in tilapia. The decreased glycogen level together with upregulated transcription of glucose-6-phosphatase catalytic subunit a2 (
g6pca2
) at 24 HAF suggests that glycogen breakdown and glucose release from AT might contribute to circular glucose in tilapia. The opposite expression patterns between
g6pca2
and phosphoenolpyruvate carboxykinase (
pck
) paralogs suggest that
pck
might participate in glyceroneogenesis rather than gluconeogenesis in the AT of tilapia. The mRNA levels of both cytosolic
pck1
and mitochondrial
pck2
increased during the period 1–8 HAF, and the expressions of lipogenic genes, such as acetyl-CoA carboxylase α and fatty acid synthase, were upregulated between 3 and 8 HAF, suggesting that glyceroneogenesis was probably stimulated as a source of glyceride–glycerol for triglyceride synthesis in the AT of tilapia. Taken together, our preliminary data suggest that AT plays an important role in the regulation of postprandial glucose homeostasis in the omnivorous tilapia, at least at the molecular level.</abstract><cop>Tokyo</cop><pub>Springer Japan</pub><doi>10.1007/s12562-018-1251-0</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-0427-7555</orcidid></addata></record> |
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subjects | Acetyl-CoA carboxylase Adipose tissue Aquaculture Biomedical and Life Sciences blood glucose Body fat Capacity carboxy-lyases Catalysis Fatty acids Fatty-acid synthase Fish Fish & Wildlife Biology & Management Fish farms Food Science Freshwater & Marine Ecology Freshwater fishes Genes Glucokinase Gluconeogenesis Glucose Glucose metabolism Glucose transport Glucose transporter glucose transporters Glucose-6-phosphatase Glycerol glyceroneogenesis Glycogen glycogen (starch) synthase Glycogen synthase glycolipids Glycolysis Hexokinase Homeostasis Life Sciences Liver Metabolism Mitochondria omnivores Oreochromis niloticus Original Article Phosphatase Phosphofructokinase phosphofructokinases protein subunits Tilapia Tissue Transcription triacylglycerols |
title | Postprandial change in glucose metabolism at the molecular level in the adipose tissue of omnivorous GIFT Oreochromis niloticus |
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