Phosphorylation of protein kinase B, the key enzyme in insulin-signaling cascade, is enhanced in linoleic and arachidonic acid–treated HT29 and HepG2 cells
•Levels of linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), eicosapentaenoic acid (EPA), and docoshexaenoic acid (DHA) as well as protein kinase B (AKT) phosphorylation were assessed in human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells treated with fatt...
Gespeichert in:
Veröffentlicht in: | Nutrition (Burbank, Los Angeles County, Calif.) Los Angeles County, Calif.), 2019-01, Vol.57, p.52-58 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 58 |
---|---|
container_issue | |
container_start_page | 52 |
container_title | Nutrition (Burbank, Los Angeles County, Calif.) |
container_volume | 57 |
creator | Mariniello, Katia Min, Yoeju Ghebremeskel, Kebreab |
description | •Levels of linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), eicosapentaenoic acid (EPA), and docoshexaenoic acid (DHA) as well as protein kinase B (AKT) phosphorylation were assessed in human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells treated with fatty acids.•LNA and ARA were more efficiently incorporated in HT29 than in HepG2 cells.•The phosphorylation of AKT increased significantly in HT29 cells that were treated with LNA and ARA, but not with ALA, EPA, or DHA.•A non-significant increase in AKT phosphorylation was observed in LNA- and ARA-treated HepG2 cells.
Defects in the insulin-signaling pathway have been implicated in the pathogenesis of impaired glucose uptake, insulin resistance, and type 2 diabetes. However, the specific defects that precipitate these abnormalities are yet to be fully elucidated. After binding to insulin, the plasma membrane–embedded insulin receptor transmembrane protein initiates a cascade of phosphorylation that leads to the activation of protein kinase B (AKT) and subsequently to the initiation of some metabolic actions of insulin. The activities of this receptor, insulin binding, and tyrosine kinase activation is dependent on its plasma lipid environment. Published data on the influence of omega-3 and -6 polyunsaturated fatty acids on insulin response are scarce. Moreover, the findings of the published investigations, most of which used omega-3 and -6, polyunsaturated fatty-acid blends, have been inconclusive. Hence, further, well thought out research is needed. The aim of the current study was to elucidate the effect of treatments with linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), docoshexaenoic acid (DHA), and eicosapentaenoic acid (EPA) on cell membrane composition and consequently on the insulin-signaling pathway and specifically AKT phosphorylation.
Human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells were treated with or without 40 µM of LNA, ARA, ALA, EPA, or DHA for 48 h, the fatty-acid composition of phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) from the treated cells by capillary gas liquid chromatograph. Cells were incubated for 30 min with or without human insulin (50 ng/mL), and the phosphorylation of AKT was assessed with the use of Western blotting.
The fatty acids were incorporated in the PtdCho and PtdEtn of both cell lines, but the level of incorporation was higher in HT29. Phosphorylation of |
doi_str_mv | 10.1016/j.nut.2018.05.033 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2096553974</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0899900718306026</els_id><sourcerecordid>2096553974</sourcerecordid><originalsourceid>FETCH-LOGICAL-c381t-39d18cb8dad87d51cc2f9ec2f9b443e45b3276e122ce41284a8c87d96c36f22c3</originalsourceid><addsrcrecordid>eNp9kc1u1DAUhS0EokPhAdggS2xYNME_cWKLFVS0g1QJFmVteeybxtOMPdgJ0rDiHVjzcn0SHKawYMHG9vX97pF9DkLPKakpoe3rbR3mqWaEypqImnD-AK2o7HhFWdM8RCsilaoUId0JepLzlhBCVaseoxNOqOCiUyv089MQ836I6TCayceAY4_3KU7gA771wWTA787wNAC-hQOG8O2wA1x6PuR59KHK_iaYcrjB1mRrHJxhnws3mGDBLWRpxhG8xSY4bJKxg3cxLLX17u77jymBmQq6vmbqN7OG_SXDFsYxP0WPejNmeHa_n6LPF--vz9fV1cfLD-dvryrLJZ0qrhyVdiOdcbJzglrLegXLsmkaDo3YcNa1QBmz0FAmGyNtAVVreduXS36KXh11y9e_zJAnvfN5eYEJEOesGVGtEFx1TUFf_oNu45yKB4VqWtIJIaksFD1SNsWcE_R6n_zOpIOmRC_Z6a0u2eklO02ELtmVmRf3yvNmB-7vxJ-wCvDmCECx4quHpLP1sPjsE9hJu-j_I_8L4sirzA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2460755818</pqid></control><display><type>article</type><title>Phosphorylation of protein kinase B, the key enzyme in insulin-signaling cascade, is enhanced in linoleic and arachidonic acid–treated HT29 and HepG2 cells</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><source>ProQuest Central UK/Ireland</source><creator>Mariniello, Katia ; Min, Yoeju ; Ghebremeskel, Kebreab</creator><creatorcontrib>Mariniello, Katia ; Min, Yoeju ; Ghebremeskel, Kebreab</creatorcontrib><description>•Levels of linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), eicosapentaenoic acid (EPA), and docoshexaenoic acid (DHA) as well as protein kinase B (AKT) phosphorylation were assessed in human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells treated with fatty acids.•LNA and ARA were more efficiently incorporated in HT29 than in HepG2 cells.•The phosphorylation of AKT increased significantly in HT29 cells that were treated with LNA and ARA, but not with ALA, EPA, or DHA.•A non-significant increase in AKT phosphorylation was observed in LNA- and ARA-treated HepG2 cells.
Defects in the insulin-signaling pathway have been implicated in the pathogenesis of impaired glucose uptake, insulin resistance, and type 2 diabetes. However, the specific defects that precipitate these abnormalities are yet to be fully elucidated. After binding to insulin, the plasma membrane–embedded insulin receptor transmembrane protein initiates a cascade of phosphorylation that leads to the activation of protein kinase B (AKT) and subsequently to the initiation of some metabolic actions of insulin. The activities of this receptor, insulin binding, and tyrosine kinase activation is dependent on its plasma lipid environment. Published data on the influence of omega-3 and -6 polyunsaturated fatty acids on insulin response are scarce. Moreover, the findings of the published investigations, most of which used omega-3 and -6, polyunsaturated fatty-acid blends, have been inconclusive. Hence, further, well thought out research is needed. The aim of the current study was to elucidate the effect of treatments with linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), docoshexaenoic acid (DHA), and eicosapentaenoic acid (EPA) on cell membrane composition and consequently on the insulin-signaling pathway and specifically AKT phosphorylation.
Human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells were treated with or without 40 µM of LNA, ARA, ALA, EPA, or DHA for 48 h, the fatty-acid composition of phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) from the treated cells by capillary gas liquid chromatograph. Cells were incubated for 30 min with or without human insulin (50 ng/mL), and the phosphorylation of AKT was assessed with the use of Western blotting.
The fatty acids were incorporated in the PtdCho and PtdEtn of both cell lines, but the level of incorporation was higher in HT29. Phosphorylation of AKT increased when HT29 was treated with LNA (P < 0.05) and ARA (P < 0.01) but not with ALA, EPA, or DHA. A similar but non-significant increase in AKT phosphorylation was observed in LNA- and ARA- treated HepG2 cells.
The finding of this investigation demonstrates that plasma membrane lipid bilayer enrichment with LNA or ARA treatment enhances insulin action by AKT activation.</description><identifier>ISSN: 0899-9007</identifier><identifier>EISSN: 1873-1244</identifier><identifier>DOI: 10.1016/j.nut.2018.05.033</identifier><identifier>PMID: 30153579</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Abnormalities ; Adenocarcinoma ; AKT phosphorylation ; AKT protein ; Arachidonic acid ; Arachidonic Acid - pharmacology ; Binding ; Cell membranes ; Cells, Cultured ; Chromatography ; Colon ; Composition ; Defects ; Diabetes ; Diabetes mellitus (non-insulin dependent) ; Eicosapentaenoic acid ; Fatty acids ; Glucose ; Hep G2 Cells ; Hepatocytes ; HT29 Cells ; Humans ; Hydrochloric acid ; In Vitro Techniques ; Insulin ; Insulin - metabolism ; Insulin resistance ; Investigations ; Kinases ; Lecithin ; Linoleic acid ; Linoleic Acid - pharmacology ; Linolenic acid ; Lipid bilayers ; Lipids ; Membrane composition ; Membrane phospholipids ; Nitrogen ; Omega 3 fatty acids ; Omega 6 fatty acids ; Pathogenesis ; Phosphatidylcholine ; Phosphatidylethanolamine ; Phosphorylation ; Plasma ; Polyunsaturated fatty acids ; Protein-tyrosine kinase ; Proteins ; Proto-Oncogene Proteins c-akt - drug effects ; Proto-Oncogene Proteins c-akt - metabolism ; Receptors ; Signal transduction ; Signal Transduction - drug effects ; Signaling ; Tyrosine ; Western blotting</subject><ispartof>Nutrition (Burbank, Los Angeles County, Calif.), 2019-01, Vol.57, p.52-58</ispartof><rights>2018 Elsevier Ltd</rights><rights>Copyright © 2018 Elsevier Ltd. All rights reserved.</rights><rights>2018. Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-39d18cb8dad87d51cc2f9ec2f9b443e45b3276e122ce41284a8c87d96c36f22c3</citedby><cites>FETCH-LOGICAL-c381t-39d18cb8dad87d51cc2f9ec2f9b443e45b3276e122ce41284a8c87d96c36f22c3</cites><orcidid>0000-0002-6264-1044</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/2460755818?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995,64385,64387,64389,72469</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30153579$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mariniello, Katia</creatorcontrib><creatorcontrib>Min, Yoeju</creatorcontrib><creatorcontrib>Ghebremeskel, Kebreab</creatorcontrib><title>Phosphorylation of protein kinase B, the key enzyme in insulin-signaling cascade, is enhanced in linoleic and arachidonic acid–treated HT29 and HepG2 cells</title><title>Nutrition (Burbank, Los Angeles County, Calif.)</title><addtitle>Nutrition</addtitle><description>•Levels of linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), eicosapentaenoic acid (EPA), and docoshexaenoic acid (DHA) as well as protein kinase B (AKT) phosphorylation were assessed in human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells treated with fatty acids.•LNA and ARA were more efficiently incorporated in HT29 than in HepG2 cells.•The phosphorylation of AKT increased significantly in HT29 cells that were treated with LNA and ARA, but not with ALA, EPA, or DHA.•A non-significant increase in AKT phosphorylation was observed in LNA- and ARA-treated HepG2 cells.
Defects in the insulin-signaling pathway have been implicated in the pathogenesis of impaired glucose uptake, insulin resistance, and type 2 diabetes. However, the specific defects that precipitate these abnormalities are yet to be fully elucidated. After binding to insulin, the plasma membrane–embedded insulin receptor transmembrane protein initiates a cascade of phosphorylation that leads to the activation of protein kinase B (AKT) and subsequently to the initiation of some metabolic actions of insulin. The activities of this receptor, insulin binding, and tyrosine kinase activation is dependent on its plasma lipid environment. Published data on the influence of omega-3 and -6 polyunsaturated fatty acids on insulin response are scarce. Moreover, the findings of the published investigations, most of which used omega-3 and -6, polyunsaturated fatty-acid blends, have been inconclusive. Hence, further, well thought out research is needed. The aim of the current study was to elucidate the effect of treatments with linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), docoshexaenoic acid (DHA), and eicosapentaenoic acid (EPA) on cell membrane composition and consequently on the insulin-signaling pathway and specifically AKT phosphorylation.
Human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells were treated with or without 40 µM of LNA, ARA, ALA, EPA, or DHA for 48 h, the fatty-acid composition of phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) from the treated cells by capillary gas liquid chromatograph. Cells were incubated for 30 min with or without human insulin (50 ng/mL), and the phosphorylation of AKT was assessed with the use of Western blotting.
The fatty acids were incorporated in the PtdCho and PtdEtn of both cell lines, but the level of incorporation was higher in HT29. Phosphorylation of AKT increased when HT29 was treated with LNA (P < 0.05) and ARA (P < 0.01) but not with ALA, EPA, or DHA. A similar but non-significant increase in AKT phosphorylation was observed in LNA- and ARA- treated HepG2 cells.
The finding of this investigation demonstrates that plasma membrane lipid bilayer enrichment with LNA or ARA treatment enhances insulin action by AKT activation.</description><subject>Abnormalities</subject><subject>Adenocarcinoma</subject><subject>AKT phosphorylation</subject><subject>AKT protein</subject><subject>Arachidonic acid</subject><subject>Arachidonic Acid - pharmacology</subject><subject>Binding</subject><subject>Cell membranes</subject><subject>Cells, Cultured</subject><subject>Chromatography</subject><subject>Colon</subject><subject>Composition</subject><subject>Defects</subject><subject>Diabetes</subject><subject>Diabetes mellitus (non-insulin dependent)</subject><subject>Eicosapentaenoic acid</subject><subject>Fatty acids</subject><subject>Glucose</subject><subject>Hep G2 Cells</subject><subject>Hepatocytes</subject><subject>HT29 Cells</subject><subject>Humans</subject><subject>Hydrochloric acid</subject><subject>In Vitro Techniques</subject><subject>Insulin</subject><subject>Insulin - metabolism</subject><subject>Insulin resistance</subject><subject>Investigations</subject><subject>Kinases</subject><subject>Lecithin</subject><subject>Linoleic acid</subject><subject>Linoleic Acid - pharmacology</subject><subject>Linolenic acid</subject><subject>Lipid bilayers</subject><subject>Lipids</subject><subject>Membrane composition</subject><subject>Membrane phospholipids</subject><subject>Nitrogen</subject><subject>Omega 3 fatty acids</subject><subject>Omega 6 fatty acids</subject><subject>Pathogenesis</subject><subject>Phosphatidylcholine</subject><subject>Phosphatidylethanolamine</subject><subject>Phosphorylation</subject><subject>Plasma</subject><subject>Polyunsaturated fatty acids</subject><subject>Protein-tyrosine kinase</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-akt - drug effects</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Receptors</subject><subject>Signal transduction</subject><subject>Signal Transduction - drug effects</subject><subject>Signaling</subject><subject>Tyrosine</subject><subject>Western blotting</subject><issn>0899-9007</issn><issn>1873-1244</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kc1u1DAUhS0EokPhAdggS2xYNME_cWKLFVS0g1QJFmVteeybxtOMPdgJ0rDiHVjzcn0SHKawYMHG9vX97pF9DkLPKakpoe3rbR3mqWaEypqImnD-AK2o7HhFWdM8RCsilaoUId0JepLzlhBCVaseoxNOqOCiUyv089MQ836I6TCayceAY4_3KU7gA771wWTA787wNAC-hQOG8O2wA1x6PuR59KHK_iaYcrjB1mRrHJxhnws3mGDBLWRpxhG8xSY4bJKxg3cxLLX17u77jymBmQq6vmbqN7OG_SXDFsYxP0WPejNmeHa_n6LPF--vz9fV1cfLD-dvryrLJZ0qrhyVdiOdcbJzglrLegXLsmkaDo3YcNa1QBmz0FAmGyNtAVVreduXS36KXh11y9e_zJAnvfN5eYEJEOesGVGtEFx1TUFf_oNu45yKB4VqWtIJIaksFD1SNsWcE_R6n_zOpIOmRC_Z6a0u2eklO02ELtmVmRf3yvNmB-7vxJ-wCvDmCECx4quHpLP1sPjsE9hJu-j_I_8L4sirzA</recordid><startdate>201901</startdate><enddate>201901</enddate><creator>Mariniello, Katia</creator><creator>Min, Yoeju</creator><creator>Ghebremeskel, Kebreab</creator><general>Elsevier Inc</general><general>Elsevier Limited</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>3V.</scope><scope>7RQ</scope><scope>7RV</scope><scope>7TS</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88C</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AN0</scope><scope>ASE</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FPQ</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K6X</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M0T</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-6264-1044</orcidid></search><sort><creationdate>201901</creationdate><title>Phosphorylation of protein kinase B, the key enzyme in insulin-signaling cascade, is enhanced in linoleic and arachidonic acid–treated HT29 and HepG2 cells</title><author>Mariniello, Katia ; Min, Yoeju ; Ghebremeskel, Kebreab</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-39d18cb8dad87d51cc2f9ec2f9b443e45b3276e122ce41284a8c87d96c36f22c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Abnormalities</topic><topic>Adenocarcinoma</topic><topic>AKT phosphorylation</topic><topic>AKT protein</topic><topic>Arachidonic acid</topic><topic>Arachidonic Acid - pharmacology</topic><topic>Binding</topic><topic>Cell membranes</topic><topic>Cells, Cultured</topic><topic>Chromatography</topic><topic>Colon</topic><topic>Composition</topic><topic>Defects</topic><topic>Diabetes</topic><topic>Diabetes mellitus (non-insulin dependent)</topic><topic>Eicosapentaenoic acid</topic><topic>Fatty acids</topic><topic>Glucose</topic><topic>Hep G2 Cells</topic><topic>Hepatocytes</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>Hydrochloric acid</topic><topic>In Vitro Techniques</topic><topic>Insulin</topic><topic>Insulin - metabolism</topic><topic>Insulin resistance</topic><topic>Investigations</topic><topic>Kinases</topic><topic>Lecithin</topic><topic>Linoleic acid</topic><topic>Linoleic Acid - pharmacology</topic><topic>Linolenic acid</topic><topic>Lipid bilayers</topic><topic>Lipids</topic><topic>Membrane composition</topic><topic>Membrane phospholipids</topic><topic>Nitrogen</topic><topic>Omega 3 fatty acids</topic><topic>Omega 6 fatty acids</topic><topic>Pathogenesis</topic><topic>Phosphatidylcholine</topic><topic>Phosphatidylethanolamine</topic><topic>Phosphorylation</topic><topic>Plasma</topic><topic>Polyunsaturated fatty acids</topic><topic>Protein-tyrosine kinase</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-akt - drug effects</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Receptors</topic><topic>Signal transduction</topic><topic>Signal Transduction - drug effects</topic><topic>Signaling</topic><topic>Tyrosine</topic><topic>Western blotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mariniello, Katia</creatorcontrib><creatorcontrib>Min, Yoeju</creatorcontrib><creatorcontrib>Ghebremeskel, Kebreab</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Career & Technical Education Database</collection><collection>Nursing & Allied Health Database</collection><collection>Physical Education Index</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Healthcare Administration Database (Alumni)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>British Nursing Database</collection><collection>British Nursing Index</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>British Nursing Index (BNI) (1985 to Present)</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>British Nursing Index</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Healthcare Administration Database</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</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 China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Nutrition (Burbank, Los Angeles County, Calif.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mariniello, Katia</au><au>Min, Yoeju</au><au>Ghebremeskel, Kebreab</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of protein kinase B, the key enzyme in insulin-signaling cascade, is enhanced in linoleic and arachidonic acid–treated HT29 and HepG2 cells</atitle><jtitle>Nutrition (Burbank, Los Angeles County, Calif.)</jtitle><addtitle>Nutrition</addtitle><date>2019-01</date><risdate>2019</risdate><volume>57</volume><spage>52</spage><epage>58</epage><pages>52-58</pages><issn>0899-9007</issn><eissn>1873-1244</eissn><abstract>•Levels of linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), eicosapentaenoic acid (EPA), and docoshexaenoic acid (DHA) as well as protein kinase B (AKT) phosphorylation were assessed in human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells treated with fatty acids.•LNA and ARA were more efficiently incorporated in HT29 than in HepG2 cells.•The phosphorylation of AKT increased significantly in HT29 cells that were treated with LNA and ARA, but not with ALA, EPA, or DHA.•A non-significant increase in AKT phosphorylation was observed in LNA- and ARA-treated HepG2 cells.
Defects in the insulin-signaling pathway have been implicated in the pathogenesis of impaired glucose uptake, insulin resistance, and type 2 diabetes. However, the specific defects that precipitate these abnormalities are yet to be fully elucidated. After binding to insulin, the plasma membrane–embedded insulin receptor transmembrane protein initiates a cascade of phosphorylation that leads to the activation of protein kinase B (AKT) and subsequently to the initiation of some metabolic actions of insulin. The activities of this receptor, insulin binding, and tyrosine kinase activation is dependent on its plasma lipid environment. Published data on the influence of omega-3 and -6 polyunsaturated fatty acids on insulin response are scarce. Moreover, the findings of the published investigations, most of which used omega-3 and -6, polyunsaturated fatty-acid blends, have been inconclusive. Hence, further, well thought out research is needed. The aim of the current study was to elucidate the effect of treatments with linoleic acid (LNA), arachidonic acid (ARA), alpha-linolenic acid (ALA), docoshexaenoic acid (DHA), and eicosapentaenoic acid (EPA) on cell membrane composition and consequently on the insulin-signaling pathway and specifically AKT phosphorylation.
Human colon adenocarcinoma (HT29) and liver hepatocellular (HepG2) cells were treated with or without 40 µM of LNA, ARA, ALA, EPA, or DHA for 48 h, the fatty-acid composition of phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) from the treated cells by capillary gas liquid chromatograph. Cells were incubated for 30 min with or without human insulin (50 ng/mL), and the phosphorylation of AKT was assessed with the use of Western blotting.
The fatty acids were incorporated in the PtdCho and PtdEtn of both cell lines, but the level of incorporation was higher in HT29. Phosphorylation of AKT increased when HT29 was treated with LNA (P < 0.05) and ARA (P < 0.01) but not with ALA, EPA, or DHA. A similar but non-significant increase in AKT phosphorylation was observed in LNA- and ARA- treated HepG2 cells.
The finding of this investigation demonstrates that plasma membrane lipid bilayer enrichment with LNA or ARA treatment enhances insulin action by AKT activation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>30153579</pmid><doi>10.1016/j.nut.2018.05.033</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-6264-1044</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0899-9007 |
ispartof | Nutrition (Burbank, Los Angeles County, Calif.), 2019-01, Vol.57, p.52-58 |
issn | 0899-9007 1873-1244 |
language | eng |
recordid | cdi_proquest_miscellaneous_2096553974 |
source | MEDLINE; Access via ScienceDirect (Elsevier); ProQuest Central UK/Ireland |
subjects | Abnormalities Adenocarcinoma AKT phosphorylation AKT protein Arachidonic acid Arachidonic Acid - pharmacology Binding Cell membranes Cells, Cultured Chromatography Colon Composition Defects Diabetes Diabetes mellitus (non-insulin dependent) Eicosapentaenoic acid Fatty acids Glucose Hep G2 Cells Hepatocytes HT29 Cells Humans Hydrochloric acid In Vitro Techniques Insulin Insulin - metabolism Insulin resistance Investigations Kinases Lecithin Linoleic acid Linoleic Acid - pharmacology Linolenic acid Lipid bilayers Lipids Membrane composition Membrane phospholipids Nitrogen Omega 3 fatty acids Omega 6 fatty acids Pathogenesis Phosphatidylcholine Phosphatidylethanolamine Phosphorylation Plasma Polyunsaturated fatty acids Protein-tyrosine kinase Proteins Proto-Oncogene Proteins c-akt - drug effects Proto-Oncogene Proteins c-akt - metabolism Receptors Signal transduction Signal Transduction - drug effects Signaling Tyrosine Western blotting |
title | Phosphorylation of protein kinase B, the key enzyme in insulin-signaling cascade, is enhanced in linoleic and arachidonic acid–treated HT29 and HepG2 cells |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T16%3A28%3A05IST&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=Phosphorylation%20of%20protein%20kinase%20B,%20the%20key%20enzyme%20in%20insulin-signaling%20cascade,%20is%20enhanced%20in%20linoleic%20and%20arachidonic%20acid%E2%80%93treated%20HT29%20and%20HepG2%20cells&rft.jtitle=Nutrition%20(Burbank,%20Los%20Angeles%20County,%20Calif.)&rft.au=Mariniello,%20Katia&rft.date=2019-01&rft.volume=57&rft.spage=52&rft.epage=58&rft.pages=52-58&rft.issn=0899-9007&rft.eissn=1873-1244&rft_id=info:doi/10.1016/j.nut.2018.05.033&rft_dat=%3Cproquest_cross%3E2096553974%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=2460755818&rft_id=info:pmid/30153579&rft_els_id=S0899900718306026&rfr_iscdi=true |