In Human Entrocytes, GLN Transport and ASCT2 Surface Expression Induced by Short-Term EGF are MAPK, PI3K, and Rho-Dependent
Glutamine, a key nutrient for the enterocyte, is transported among other proteins by ASCT2. Epidermal growth factor (EGF) augments intestinal adaptation. We hypothesized that short-term treatment of human enterocytes with EGF enhances glutamine transport by increasing membranal ASCT2. To elucidate E...
Gespeichert in:
| Veröffentlicht in: | Digestive diseases and sciences 2008-08, Vol.53 (8), p.2113-2125 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2125 |
|---|---|
| container_issue | 8 |
| container_start_page | 2113 |
| container_title | Digestive diseases and sciences |
| container_volume | 53 |
| creator | Avissar, Nelly E. Sax, Harry C. Toia, Liana |
| description | Glutamine, a key nutrient for the enterocyte, is transported among other proteins by ASCT2. Epidermal growth factor (EGF) augments intestinal adaptation. We hypothesized that short-term treatment of human enterocytes with EGF enhances glutamine transport by increasing membranal ASCT2. To elucidate EGF-induced mechanisms, monolayers of C2
BBe
1 w/wo siRho transfection were treated w/wo EGF and w/wo tyrphostin AG1478 (AG1478), wortmanin, or PD98059. Total and system-specific
3
H-glutamine transports were determined w/wo 5 mmol/l amino acid inhibitors. Total and membranal ASCT2 proteins were measured by Westerns. EGF doubled glutamine transport by increasing B
0
/ASCT2 and B
0,+
activities. Despite the doubling of membranal ASCT2 protein with EGF treatment, total ASCT2 did not change. The increases in B
0
/ASCT2 activity and ASCT2 protein were eliminated by AG1478, PD98059, wortmanin, and siRho, while transport by B
0,+
was inhibited only by PD98059 and siRho. Thus, differential pathways are involved in EGF-induced increase in B
0
/ASCT2 glutamine transport and membranal ASCT2 compared to those involved in B
0,+
activity. |
| doi_str_mv | 10.1007/s10620-007-0120-y |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69279474</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1507562391</sourcerecordid><originalsourceid>FETCH-LOGICAL-c399t-c9e226d5fd5aead92a141dc09abfe187a3675460200a14faa3d647787fa189003</originalsourceid><addsrcrecordid>eNp1kVGLEzEUhYMobl39Ab5IEPRpR28yM8nksdRut1h1sfU5pMkdt0snM5vMgIN_3gwtLgi-JAfud08OOYS8ZvCBAciPkYHgkCWZAUtifEJmrJR5xktRPSUzYCJpxsQFeRHjPQAoycRzcsGqhAlVzsjvtac3Q2M8Xfo-tHbsMV7R1eYr3QXjY9eGnhrv6Hy72HG6HUJtLNLlry5gjIfW07V3g0VH9yPd3iU622Fo6HJ1TU1A-mV--_mK3q7zdE423-_a7BN26B36_iV5VptjxFfn-5L8uF7uFjfZ5ttqvZhvMpsr1WdWIefClbUrDRqnuGEFcxaU2dfIKmlyIctCAAdIk9qY3IlCykrWhlUKIL8k70--XWgfBoy9bg7R4vFoPLZD1EJxqQpZJPDtP-B9OwSfsmnOipxDrniC2AmyoY0xYK27cGhMGDUDPdWiT7XoSU616DHtvDkbD_sG3ePGuYcEvDsDJlpzrNPf20P8y3EoeSH5lJCfuJhG_ieGx4T_f_0Px-Sh_w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>214320392</pqid></control><display><type>article</type><title>In Human Entrocytes, GLN Transport and ASCT2 Surface Expression Induced by Short-Term EGF are MAPK, PI3K, and Rho-Dependent</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Avissar, Nelly E. ; Sax, Harry C. ; Toia, Liana</creator><creatorcontrib>Avissar, Nelly E. ; Sax, Harry C. ; Toia, Liana</creatorcontrib><description>Glutamine, a key nutrient for the enterocyte, is transported among other proteins by ASCT2. Epidermal growth factor (EGF) augments intestinal adaptation. We hypothesized that short-term treatment of human enterocytes with EGF enhances glutamine transport by increasing membranal ASCT2. To elucidate EGF-induced mechanisms, monolayers of C2
BBe
1 w/wo siRho transfection were treated w/wo EGF and w/wo tyrphostin AG1478 (AG1478), wortmanin, or PD98059. Total and system-specific
3
H-glutamine transports were determined w/wo 5 mmol/l amino acid inhibitors. Total and membranal ASCT2 proteins were measured by Westerns. EGF doubled glutamine transport by increasing B
0
/ASCT2 and B
0,+
activities. Despite the doubling of membranal ASCT2 protein with EGF treatment, total ASCT2 did not change. The increases in B
0
/ASCT2 activity and ASCT2 protein were eliminated by AG1478, PD98059, wortmanin, and siRho, while transport by B
0,+
was inhibited only by PD98059 and siRho. Thus, differential pathways are involved in EGF-induced increase in B
0
/ASCT2 glutamine transport and membranal ASCT2 compared to those involved in B
0,+
activity.</description><identifier>ISSN: 0163-2116</identifier><identifier>EISSN: 1573-2568</identifier><identifier>DOI: 10.1007/s10620-007-0120-y</identifier><identifier>PMID: 18157695</identifier><identifier>CODEN: DDSCDJ</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Amino Acid Transport System ASC - metabolism ; Androstadienes - pharmacology ; Biochemistry ; Biological and medical sciences ; Blotting, Western ; Caco-2 Cells ; Cell Membrane - metabolism ; Enterocytes - drug effects ; Enterocytes - enzymology ; Enterocytes - metabolism ; Epidermal Growth Factor - metabolism ; Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Feeding. Feeding behavior ; Flavonoids - pharmacology ; Fundamental and applied biological sciences. Psychology ; Gastroenterology ; Glutamine - metabolism ; Hepatology ; Humans ; Medicine ; Medicine & Public Health ; Minor Histocompatibility Antigens ; Oncology ; Original Paper ; Phosphatidylinositol 3-Kinases - antagonists & inhibitors ; Phosphatidylinositol 3-Kinases - metabolism ; Protein Kinase Inhibitors - pharmacology ; Protein Transport ; Protein Tyrosine Phosphatases - antagonists & inhibitors ; Protein Tyrosine Phosphatases - metabolism ; Quinazolines ; Receptor, Epidermal Growth Factor - antagonists & inhibitors ; Receptor, Epidermal Growth Factor - metabolism ; rho GTP-Binding Proteins - genetics ; rho GTP-Binding Proteins - metabolism ; RNA Interference ; Signal Transduction - drug effects ; Sodium - metabolism ; Time Factors ; Transplant Surgery ; Tyrphostins - pharmacology ; Up-Regulation ; Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><ispartof>Digestive diseases and sciences, 2008-08, Vol.53 (8), p.2113-2125</ispartof><rights>Springer Science+Business Media, LLC 2007</rights><rights>2008 INIST-CNRS</rights><rights>Springer Science+Business Media, LLC 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-c9e226d5fd5aead92a141dc09abfe187a3675460200a14faa3d647787fa189003</citedby><cites>FETCH-LOGICAL-c399t-c9e226d5fd5aead92a141dc09abfe187a3675460200a14faa3d647787fa189003</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10620-007-0120-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10620-007-0120-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20524724$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18157695$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Avissar, Nelly E.</creatorcontrib><creatorcontrib>Sax, Harry C.</creatorcontrib><creatorcontrib>Toia, Liana</creatorcontrib><title>In Human Entrocytes, GLN Transport and ASCT2 Surface Expression Induced by Short-Term EGF are MAPK, PI3K, and Rho-Dependent</title><title>Digestive diseases and sciences</title><addtitle>Dig Dis Sci</addtitle><addtitle>Dig Dis Sci</addtitle><description>Glutamine, a key nutrient for the enterocyte, is transported among other proteins by ASCT2. Epidermal growth factor (EGF) augments intestinal adaptation. We hypothesized that short-term treatment of human enterocytes with EGF enhances glutamine transport by increasing membranal ASCT2. To elucidate EGF-induced mechanisms, monolayers of C2
BBe
1 w/wo siRho transfection were treated w/wo EGF and w/wo tyrphostin AG1478 (AG1478), wortmanin, or PD98059. Total and system-specific
3
H-glutamine transports were determined w/wo 5 mmol/l amino acid inhibitors. Total and membranal ASCT2 proteins were measured by Westerns. EGF doubled glutamine transport by increasing B
0
/ASCT2 and B
0,+
activities. Despite the doubling of membranal ASCT2 protein with EGF treatment, total ASCT2 did not change. The increases in B
0
/ASCT2 activity and ASCT2 protein were eliminated by AG1478, PD98059, wortmanin, and siRho, while transport by B
0,+
was inhibited only by PD98059 and siRho. Thus, differential pathways are involved in EGF-induced increase in B
0
/ASCT2 glutamine transport and membranal ASCT2 compared to those involved in B
0,+
activity.</description><subject>Amino Acid Transport System ASC - metabolism</subject><subject>Androstadienes - pharmacology</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Caco-2 Cells</subject><subject>Cell Membrane - metabolism</subject><subject>Enterocytes - drug effects</subject><subject>Enterocytes - enzymology</subject><subject>Enterocytes - metabolism</subject><subject>Epidermal Growth Factor - metabolism</subject><subject>Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Feeding. Feeding behavior</subject><subject>Flavonoids - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gastroenterology</subject><subject>Glutamine - metabolism</subject><subject>Hepatology</subject><subject>Humans</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Minor Histocompatibility Antigens</subject><subject>Oncology</subject><subject>Original Paper</subject><subject>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>Protein Transport</subject><subject>Protein Tyrosine Phosphatases - antagonists & inhibitors</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Quinazolines</subject><subject>Receptor, Epidermal Growth Factor - antagonists & inhibitors</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>rho GTP-Binding Proteins - genetics</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>RNA Interference</subject><subject>Signal Transduction - drug effects</subject><subject>Sodium - metabolism</subject><subject>Time Factors</subject><subject>Transplant Surgery</subject><subject>Tyrphostins - pharmacology</subject><subject>Up-Regulation</subject><subject>Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><issn>0163-2116</issn><issn>1573-2568</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNp1kVGLEzEUhYMobl39Ab5IEPRpR28yM8nksdRut1h1sfU5pMkdt0snM5vMgIN_3gwtLgi-JAfud08OOYS8ZvCBAciPkYHgkCWZAUtifEJmrJR5xktRPSUzYCJpxsQFeRHjPQAoycRzcsGqhAlVzsjvtac3Q2M8Xfo-tHbsMV7R1eYr3QXjY9eGnhrv6Hy72HG6HUJtLNLlry5gjIfW07V3g0VH9yPd3iU622Fo6HJ1TU1A-mV--_mK3q7zdE423-_a7BN26B36_iV5VptjxFfn-5L8uF7uFjfZ5ttqvZhvMpsr1WdWIefClbUrDRqnuGEFcxaU2dfIKmlyIctCAAdIk9qY3IlCykrWhlUKIL8k70--XWgfBoy9bg7R4vFoPLZD1EJxqQpZJPDtP-B9OwSfsmnOipxDrniC2AmyoY0xYK27cGhMGDUDPdWiT7XoSU616DHtvDkbD_sG3ePGuYcEvDsDJlpzrNPf20P8y3EoeSH5lJCfuJhG_ieGx4T_f_0Px-Sh_w</recordid><startdate>20080801</startdate><enddate>20080801</enddate><creator>Avissar, Nelly E.</creator><creator>Sax, Harry C.</creator><creator>Toia, Liana</creator><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9-</scope><scope>K9.</scope><scope>KB0</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope></search><sort><creationdate>20080801</creationdate><title>In Human Entrocytes, GLN Transport and ASCT2 Surface Expression Induced by Short-Term EGF are MAPK, PI3K, and Rho-Dependent</title><author>Avissar, Nelly E. ; Sax, Harry C. ; Toia, Liana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-c9e226d5fd5aead92a141dc09abfe187a3675460200a14faa3d647787fa189003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Transport System ASC - metabolism</topic><topic>Androstadienes - pharmacology</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Caco-2 Cells</topic><topic>Cell Membrane - metabolism</topic><topic>Enterocytes - drug effects</topic><topic>Enterocytes - enzymology</topic><topic>Enterocytes - metabolism</topic><topic>Epidermal Growth Factor - metabolism</topic><topic>Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Feeding. Feeding behavior</topic><topic>Flavonoids - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gastroenterology</topic><topic>Glutamine - metabolism</topic><topic>Hepatology</topic><topic>Humans</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Minor Histocompatibility Antigens</topic><topic>Oncology</topic><topic>Original Paper</topic><topic>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Protein Kinase Inhibitors - pharmacology</topic><topic>Protein Transport</topic><topic>Protein Tyrosine Phosphatases - antagonists & inhibitors</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Quinazolines</topic><topic>Receptor, Epidermal Growth Factor - antagonists & inhibitors</topic><topic>Receptor, Epidermal Growth Factor - metabolism</topic><topic>rho GTP-Binding Proteins - genetics</topic><topic>rho GTP-Binding Proteins - metabolism</topic><topic>RNA Interference</topic><topic>Signal Transduction - drug effects</topic><topic>Sodium - metabolism</topic><topic>Time Factors</topic><topic>Transplant Surgery</topic><topic>Tyrphostins - pharmacology</topic><topic>Up-Regulation</topic><topic>Vertebrates: anatomy and physiology, studies on body, several organs or systems</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Avissar, Nelly E.</creatorcontrib><creatorcontrib>Sax, Harry C.</creatorcontrib><creatorcontrib>Toia, Liana</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>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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>MEDLINE - Academic</collection><jtitle>Digestive diseases and sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Avissar, Nelly E.</au><au>Sax, Harry C.</au><au>Toia, Liana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In Human Entrocytes, GLN Transport and ASCT2 Surface Expression Induced by Short-Term EGF are MAPK, PI3K, and Rho-Dependent</atitle><jtitle>Digestive diseases and sciences</jtitle><stitle>Dig Dis Sci</stitle><addtitle>Dig Dis Sci</addtitle><date>2008-08-01</date><risdate>2008</risdate><volume>53</volume><issue>8</issue><spage>2113</spage><epage>2125</epage><pages>2113-2125</pages><issn>0163-2116</issn><eissn>1573-2568</eissn><coden>DDSCDJ</coden><abstract>Glutamine, a key nutrient for the enterocyte, is transported among other proteins by ASCT2. Epidermal growth factor (EGF) augments intestinal adaptation. We hypothesized that short-term treatment of human enterocytes with EGF enhances glutamine transport by increasing membranal ASCT2. To elucidate EGF-induced mechanisms, monolayers of C2
BBe
1 w/wo siRho transfection were treated w/wo EGF and w/wo tyrphostin AG1478 (AG1478), wortmanin, or PD98059. Total and system-specific
3
H-glutamine transports were determined w/wo 5 mmol/l amino acid inhibitors. Total and membranal ASCT2 proteins were measured by Westerns. EGF doubled glutamine transport by increasing B
0
/ASCT2 and B
0,+
activities. Despite the doubling of membranal ASCT2 protein with EGF treatment, total ASCT2 did not change. The increases in B
0
/ASCT2 activity and ASCT2 protein were eliminated by AG1478, PD98059, wortmanin, and siRho, while transport by B
0,+
was inhibited only by PD98059 and siRho. Thus, differential pathways are involved in EGF-induced increase in B
0
/ASCT2 glutamine transport and membranal ASCT2 compared to those involved in B
0,+
activity.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>18157695</pmid><doi>10.1007/s10620-007-0120-y</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0163-2116 |
| ispartof | Digestive diseases and sciences, 2008-08, Vol.53 (8), p.2113-2125 |
| issn | 0163-2116 1573-2568 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69279474 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino Acid Transport System ASC - metabolism Androstadienes - pharmacology Biochemistry Biological and medical sciences Blotting, Western Caco-2 Cells Cell Membrane - metabolism Enterocytes - drug effects Enterocytes - enzymology Enterocytes - metabolism Epidermal Growth Factor - metabolism Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors Extracellular Signal-Regulated MAP Kinases - metabolism Feeding. Feeding behavior Flavonoids - pharmacology Fundamental and applied biological sciences. Psychology Gastroenterology Glutamine - metabolism Hepatology Humans Medicine Medicine & Public Health Minor Histocompatibility Antigens Oncology Original Paper Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - metabolism Protein Kinase Inhibitors - pharmacology Protein Transport Protein Tyrosine Phosphatases - antagonists & inhibitors Protein Tyrosine Phosphatases - metabolism Quinazolines Receptor, Epidermal Growth Factor - antagonists & inhibitors Receptor, Epidermal Growth Factor - metabolism rho GTP-Binding Proteins - genetics rho GTP-Binding Proteins - metabolism RNA Interference Signal Transduction - drug effects Sodium - metabolism Time Factors Transplant Surgery Tyrphostins - pharmacology Up-Regulation Vertebrates: anatomy and physiology, studies on body, several organs or systems |
| title | In Human Entrocytes, GLN Transport and ASCT2 Surface Expression Induced by Short-Term EGF are MAPK, PI3K, and Rho-Dependent |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T05%3A08%3A33IST&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=In%20Human%20Entrocytes,%20GLN%20Transport%20and%20ASCT2%20Surface%20Expression%20Induced%20by%20Short-Term%20EGF%20are%20MAPK,%20PI3K,%20and%20Rho-Dependent&rft.jtitle=Digestive%20diseases%20and%20sciences&rft.au=Avissar,%20Nelly%20E.&rft.date=2008-08-01&rft.volume=53&rft.issue=8&rft.spage=2113&rft.epage=2125&rft.pages=2113-2125&rft.issn=0163-2116&rft.eissn=1573-2568&rft.coden=DDSCDJ&rft_id=info:doi/10.1007/s10620-007-0120-y&rft_dat=%3Cproquest_cross%3E1507562391%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=214320392&rft_id=info:pmid/18157695&rfr_iscdi=true |