l-Tryptophan Activates Mammalian Target of Rapamycin and Enhances Expression of Tight Junction Proteins in Intestinal Porcine Epithelial Cells
Besides serving as a substrate for protein synthesis, L-tryptophan (L-Trp) is used via serotonin-, kynurenine-, and niacin-synthetic pathways to produce bioactive compounds crucial for whole-body homeostasis. It is unknown whether L-Trp itself can regulate metabolic pathways in animal cells. This st...
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| Veröffentlicht in: | The Journal of nutrition 2015-06, Vol.145 (6), p.1156-1162 |
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| creator | Wang, Hao Ji, Yun Wu, Guoyao Sun, Kaiji Sun, Yuli Li, Wei Wang, Bin He, Beibei Zhang, Qing Dai, Zhaolai Wu, Zhenlong |
| description | Besides serving as a substrate for protein synthesis, L-tryptophan (L-Trp) is used via serotonin-, kynurenine-, and niacin-synthetic pathways to produce bioactive compounds crucial for whole-body homeostasis. It is unknown whether L-Trp itself can regulate metabolic pathways in animal cells.
This study tested the hypothesis that L-Trp may activate mammalian target of rapamycin (mTOR) complex 1 and enhance expression of tight junction (TJ) proteins in intestinal porcine epithelial cells.
Jejunal enterocytes, intestinal porcine epithelial cell line 1 (IPEC-1) isolated from newborn pigs, were cultured in customized Dulbecco's modified Eagle medium (DMEM) supplemented with or without L-Trp for the indicated time periods. Cell proliferation, L-Trp metabolism, protein turnover, mRNA abundance for L-Trp transporters [solute carrier family 3 member 1 (SLC3A1), solute carrier family 6 member 14 (SLC6A14), solute carrier family 6 member 19 (SLC6A19), and Na(+)/K(+) ATPase subunit-α1 (ATP1A1)], abundance of proteins involved in mTOR signaling, and TJ proteins were determined.
L-Trp was not degraded in IPEC-1 cells. Compared with basal medium containing 0.04 mmol/L L-Trp, 0.4 and 0.8 mmol/L L-Trp enhanced (P < 0.05) protein synthesis by 45-52% and cell growth by 17% and 25% on day 1 and 72% and 51% on day 2, respectively, while reducing (P < 0.05) protein degradation by 12% and 22%, respectively. These effects of L-Trp were associated with mTOR activation and increased (P < 0.05) mRNA abundance for L-Trp transporters (SLC6A19, SLC6A14, and SLC3A1) by 1.5-2.7 fold and ATP1A1 by 3 fold. L-Trp also upregulated (P < 0.05) the abundance of occludin, claudin-4, zonula occludens (ZO) 1 and 2 by 0.5-2 fold but did not affect expression of claudin-1 or ZO-3 in IPEC-1 cells.
L-Trp is not catabolized by pig small intestinal epithelial cells but can regulate intracellular protein turnover and expression of TJ proteins in these cells. |
| doi_str_mv | 10.3945/jn.114.209817 |
| format | Article |
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This study tested the hypothesis that L-Trp may activate mammalian target of rapamycin (mTOR) complex 1 and enhance expression of tight junction (TJ) proteins in intestinal porcine epithelial cells.
Jejunal enterocytes, intestinal porcine epithelial cell line 1 (IPEC-1) isolated from newborn pigs, were cultured in customized Dulbecco's modified Eagle medium (DMEM) supplemented with or without L-Trp for the indicated time periods. Cell proliferation, L-Trp metabolism, protein turnover, mRNA abundance for L-Trp transporters [solute carrier family 3 member 1 (SLC3A1), solute carrier family 6 member 14 (SLC6A14), solute carrier family 6 member 19 (SLC6A19), and Na(+)/K(+) ATPase subunit-α1 (ATP1A1)], abundance of proteins involved in mTOR signaling, and TJ proteins were determined.
L-Trp was not degraded in IPEC-1 cells. Compared with basal medium containing 0.04 mmol/L L-Trp, 0.4 and 0.8 mmol/L L-Trp enhanced (P < 0.05) protein synthesis by 45-52% and cell growth by 17% and 25% on day 1 and 72% and 51% on day 2, respectively, while reducing (P < 0.05) protein degradation by 12% and 22%, respectively. These effects of L-Trp were associated with mTOR activation and increased (P < 0.05) mRNA abundance for L-Trp transporters (SLC6A19, SLC6A14, and SLC3A1) by 1.5-2.7 fold and ATP1A1 by 3 fold. L-Trp also upregulated (P < 0.05) the abundance of occludin, claudin-4, zonula occludens (ZO) 1 and 2 by 0.5-2 fold but did not affect expression of claudin-1 or ZO-3 in IPEC-1 cells.
L-Trp is not catabolized by pig small intestinal epithelial cells but can regulate intracellular protein turnover and expression of TJ proteins in these cells.</description><identifier>ISSN: 0022-3166</identifier><identifier>EISSN: 1541-6100</identifier><identifier>DOI: 10.3945/jn.114.209817</identifier><identifier>PMID: 25878205</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Cell Proliferation - drug effects ; Cells, Cultured ; Claudin-1 - genetics ; Claudin-1 - metabolism ; Claudin-4 - genetics ; Claudin-4 - metabolism ; Enterocytes - drug effects ; Enterocytes - metabolism ; Intestinal Mucosa - metabolism ; Intestine, Small - drug effects ; Intestine, Small - metabolism ; Intestines - cytology ; Intestines - drug effects ; Mechanistic Target of Rapamycin Complex 1 ; Multiprotein Complexes - genetics ; Multiprotein Complexes - metabolism ; Occludin - genetics ; Occludin - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Signal Transduction ; Swine ; Tight Junction Proteins - genetics ; Tight Junction Proteins - metabolism ; Tight Junctions - drug effects ; Tight Junctions - metabolism ; TOR Serine-Threonine Kinases - genetics ; TOR Serine-Threonine Kinases - metabolism ; Tryptophan - pharmacology ; Up-Regulation</subject><ispartof>The Journal of nutrition, 2015-06, Vol.145 (6), p.1156-1162</ispartof><rights>2015 American Society for Nutrition.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-37746c15681f5879ecd8200015562687c982da701555a7036b2c792e87a1174b3</citedby><cites>FETCH-LOGICAL-c398t-37746c15681f5879ecd8200015562687c982da701555a7036b2c792e87a1174b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25878205$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Hao</creatorcontrib><creatorcontrib>Ji, Yun</creatorcontrib><creatorcontrib>Wu, Guoyao</creatorcontrib><creatorcontrib>Sun, Kaiji</creatorcontrib><creatorcontrib>Sun, Yuli</creatorcontrib><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Wang, Bin</creatorcontrib><creatorcontrib>He, Beibei</creatorcontrib><creatorcontrib>Zhang, Qing</creatorcontrib><creatorcontrib>Dai, Zhaolai</creatorcontrib><creatorcontrib>Wu, Zhenlong</creatorcontrib><title>l-Tryptophan Activates Mammalian Target of Rapamycin and Enhances Expression of Tight Junction Proteins in Intestinal Porcine Epithelial Cells</title><title>The Journal of nutrition</title><addtitle>J Nutr</addtitle><description>Besides serving as a substrate for protein synthesis, L-tryptophan (L-Trp) is used via serotonin-, kynurenine-, and niacin-synthetic pathways to produce bioactive compounds crucial for whole-body homeostasis. It is unknown whether L-Trp itself can regulate metabolic pathways in animal cells.
This study tested the hypothesis that L-Trp may activate mammalian target of rapamycin (mTOR) complex 1 and enhance expression of tight junction (TJ) proteins in intestinal porcine epithelial cells.
Jejunal enterocytes, intestinal porcine epithelial cell line 1 (IPEC-1) isolated from newborn pigs, were cultured in customized Dulbecco's modified Eagle medium (DMEM) supplemented with or without L-Trp for the indicated time periods. Cell proliferation, L-Trp metabolism, protein turnover, mRNA abundance for L-Trp transporters [solute carrier family 3 member 1 (SLC3A1), solute carrier family 6 member 14 (SLC6A14), solute carrier family 6 member 19 (SLC6A19), and Na(+)/K(+) ATPase subunit-α1 (ATP1A1)], abundance of proteins involved in mTOR signaling, and TJ proteins were determined.
L-Trp was not degraded in IPEC-1 cells. Compared with basal medium containing 0.04 mmol/L L-Trp, 0.4 and 0.8 mmol/L L-Trp enhanced (P < 0.05) protein synthesis by 45-52% and cell growth by 17% and 25% on day 1 and 72% and 51% on day 2, respectively, while reducing (P < 0.05) protein degradation by 12% and 22%, respectively. These effects of L-Trp were associated with mTOR activation and increased (P < 0.05) mRNA abundance for L-Trp transporters (SLC6A19, SLC6A14, and SLC3A1) by 1.5-2.7 fold and ATP1A1 by 3 fold. L-Trp also upregulated (P < 0.05) the abundance of occludin, claudin-4, zonula occludens (ZO) 1 and 2 by 0.5-2 fold but did not affect expression of claudin-1 or ZO-3 in IPEC-1 cells.
L-Trp is not catabolized by pig small intestinal epithelial cells but can regulate intracellular protein turnover and expression of TJ proteins in these cells.</description><subject>Animals</subject><subject>Cell Proliferation - drug effects</subject><subject>Cells, Cultured</subject><subject>Claudin-1 - genetics</subject><subject>Claudin-1 - metabolism</subject><subject>Claudin-4 - genetics</subject><subject>Claudin-4 - metabolism</subject><subject>Enterocytes - drug effects</subject><subject>Enterocytes - metabolism</subject><subject>Intestinal Mucosa - metabolism</subject><subject>Intestine, Small - drug effects</subject><subject>Intestine, Small - metabolism</subject><subject>Intestines - cytology</subject><subject>Intestines - drug effects</subject><subject>Mechanistic Target of Rapamycin Complex 1</subject><subject>Multiprotein Complexes - genetics</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Occludin - genetics</subject><subject>Occludin - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Signal Transduction</subject><subject>Swine</subject><subject>Tight Junction Proteins - genetics</subject><subject>Tight Junction Proteins - metabolism</subject><subject>Tight Junctions - drug effects</subject><subject>Tight Junctions - metabolism</subject><subject>TOR Serine-Threonine Kinases - genetics</subject><subject>TOR Serine-Threonine Kinases - metabolism</subject><subject>Tryptophan - pharmacology</subject><subject>Up-Regulation</subject><issn>0022-3166</issn><issn>1541-6100</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kUlPwzAQhS0EgrIcuSIfuaR4iZccUVU2gahQOUeu67auEifYLqJ_gt_MVAVOI4--eZ43D6FLSoa8KsXNOgwpLYeMVJqqAzSgoqSFpIQcogEhjBWcSnmCTlNaE0JoWeljdMKEVpoRMUDfTTGN2z53_coEfGuz_zTZJfxi2tY0HnpTE5cu426B30xv2q31AZswx-MAExbQ8VcfXUq-Czto6perjJ82AaSgM4lddj4kDFOPAZSzD6bBky6CjsPj3ueVg38aPHJNk87R0cI0yV381jP0fjeejh6K59f7x9Htc2F5pXPBlSqlpUJqugArlbNzsAP2hJBMamUrzeZG7d4CCpczZlXFnFaGUlXO-Bm63uv2sfvYwFZ165OFDUxw3SbVVGqhBJWcA1rsURu7lKJb1H30rYnbmpJ6F0G9DjVEUO8jAP7qV3oza938n_67Of8BRfWCEA</recordid><startdate>20150601</startdate><enddate>20150601</enddate><creator>Wang, Hao</creator><creator>Ji, Yun</creator><creator>Wu, Guoyao</creator><creator>Sun, Kaiji</creator><creator>Sun, Yuli</creator><creator>Li, Wei</creator><creator>Wang, Bin</creator><creator>He, Beibei</creator><creator>Zhang, Qing</creator><creator>Dai, Zhaolai</creator><creator>Wu, Zhenlong</creator><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>7X8</scope></search><sort><creationdate>20150601</creationdate><title>l-Tryptophan Activates Mammalian Target of Rapamycin and Enhances Expression of Tight Junction Proteins in Intestinal Porcine Epithelial Cells</title><author>Wang, Hao ; Ji, Yun ; Wu, Guoyao ; Sun, Kaiji ; Sun, Yuli ; Li, Wei ; Wang, Bin ; He, Beibei ; Zhang, Qing ; Dai, Zhaolai ; Wu, Zhenlong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-37746c15681f5879ecd8200015562687c982da701555a7036b2c792e87a1174b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Animals</topic><topic>Cell Proliferation - drug effects</topic><topic>Cells, Cultured</topic><topic>Claudin-1 - genetics</topic><topic>Claudin-1 - metabolism</topic><topic>Claudin-4 - genetics</topic><topic>Claudin-4 - metabolism</topic><topic>Enterocytes - drug effects</topic><topic>Enterocytes - metabolism</topic><topic>Intestinal Mucosa - metabolism</topic><topic>Intestine, Small - drug effects</topic><topic>Intestine, Small - metabolism</topic><topic>Intestines - cytology</topic><topic>Intestines - drug effects</topic><topic>Mechanistic Target of Rapamycin Complex 1</topic><topic>Multiprotein Complexes - genetics</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Occludin - genetics</topic><topic>Occludin - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Signal Transduction</topic><topic>Swine</topic><topic>Tight Junction Proteins - genetics</topic><topic>Tight Junction Proteins - metabolism</topic><topic>Tight Junctions - drug effects</topic><topic>Tight Junctions - metabolism</topic><topic>TOR Serine-Threonine Kinases - genetics</topic><topic>TOR Serine-Threonine Kinases - metabolism</topic><topic>Tryptophan - pharmacology</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Hao</creatorcontrib><creatorcontrib>Ji, Yun</creatorcontrib><creatorcontrib>Wu, Guoyao</creatorcontrib><creatorcontrib>Sun, Kaiji</creatorcontrib><creatorcontrib>Sun, Yuli</creatorcontrib><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Wang, Bin</creatorcontrib><creatorcontrib>He, Beibei</creatorcontrib><creatorcontrib>Zhang, Qing</creatorcontrib><creatorcontrib>Dai, Zhaolai</creatorcontrib><creatorcontrib>Wu, Zhenlong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Hao</au><au>Ji, Yun</au><au>Wu, Guoyao</au><au>Sun, Kaiji</au><au>Sun, Yuli</au><au>Li, Wei</au><au>Wang, Bin</au><au>He, Beibei</au><au>Zhang, Qing</au><au>Dai, Zhaolai</au><au>Wu, Zhenlong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>l-Tryptophan Activates Mammalian Target of Rapamycin and Enhances Expression of Tight Junction Proteins in Intestinal Porcine Epithelial Cells</atitle><jtitle>The Journal of nutrition</jtitle><addtitle>J Nutr</addtitle><date>2015-06-01</date><risdate>2015</risdate><volume>145</volume><issue>6</issue><spage>1156</spage><epage>1162</epage><pages>1156-1162</pages><issn>0022-3166</issn><eissn>1541-6100</eissn><abstract>Besides serving as a substrate for protein synthesis, L-tryptophan (L-Trp) is used via serotonin-, kynurenine-, and niacin-synthetic pathways to produce bioactive compounds crucial for whole-body homeostasis. It is unknown whether L-Trp itself can regulate metabolic pathways in animal cells.
This study tested the hypothesis that L-Trp may activate mammalian target of rapamycin (mTOR) complex 1 and enhance expression of tight junction (TJ) proteins in intestinal porcine epithelial cells.
Jejunal enterocytes, intestinal porcine epithelial cell line 1 (IPEC-1) isolated from newborn pigs, were cultured in customized Dulbecco's modified Eagle medium (DMEM) supplemented with or without L-Trp for the indicated time periods. Cell proliferation, L-Trp metabolism, protein turnover, mRNA abundance for L-Trp transporters [solute carrier family 3 member 1 (SLC3A1), solute carrier family 6 member 14 (SLC6A14), solute carrier family 6 member 19 (SLC6A19), and Na(+)/K(+) ATPase subunit-α1 (ATP1A1)], abundance of proteins involved in mTOR signaling, and TJ proteins were determined.
L-Trp was not degraded in IPEC-1 cells. Compared with basal medium containing 0.04 mmol/L L-Trp, 0.4 and 0.8 mmol/L L-Trp enhanced (P < 0.05) protein synthesis by 45-52% and cell growth by 17% and 25% on day 1 and 72% and 51% on day 2, respectively, while reducing (P < 0.05) protein degradation by 12% and 22%, respectively. These effects of L-Trp were associated with mTOR activation and increased (P < 0.05) mRNA abundance for L-Trp transporters (SLC6A19, SLC6A14, and SLC3A1) by 1.5-2.7 fold and ATP1A1 by 3 fold. L-Trp also upregulated (P < 0.05) the abundance of occludin, claudin-4, zonula occludens (ZO) 1 and 2 by 0.5-2 fold but did not affect expression of claudin-1 or ZO-3 in IPEC-1 cells.
L-Trp is not catabolized by pig small intestinal epithelial cells but can regulate intracellular protein turnover and expression of TJ proteins in these cells.</abstract><cop>United States</cop><pmid>25878205</pmid><doi>10.3945/jn.114.209817</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Cell Proliferation - drug effects Cells, Cultured Claudin-1 - genetics Claudin-1 - metabolism Claudin-4 - genetics Claudin-4 - metabolism Enterocytes - drug effects Enterocytes - metabolism Intestinal Mucosa - metabolism Intestine, Small - drug effects Intestine, Small - metabolism Intestines - cytology Intestines - drug effects Mechanistic Target of Rapamycin Complex 1 Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Occludin - genetics Occludin - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism Signal Transduction Swine Tight Junction Proteins - genetics Tight Junction Proteins - metabolism Tight Junctions - drug effects Tight Junctions - metabolism TOR Serine-Threonine Kinases - genetics TOR Serine-Threonine Kinases - metabolism Tryptophan - pharmacology Up-Regulation |
| title | l-Tryptophan Activates Mammalian Target of Rapamycin and Enhances Expression of Tight Junction Proteins in Intestinal Porcine Epithelial Cells |
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