Bioefficacy of tea catechins encapsulated in casein micelles tested on a normal mouse cell line (4D/WT) and its cancerous counterpart (D/v-src) before and after in vitro digestion
Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins. Much less work has been conducted to understand the metabolic conversions of tea-milk complexes during gastro-duodenal digestion. The objective of this study was to determine the significance...
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| Veröffentlicht in: | Food & function 2014-06, Vol.5 (6), p.116-1166 |
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| creator | Haratifar, Sanaz Meckling, Kelly A Corredig, Milena |
| description | Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins. Much less work has been conducted to understand the metabolic conversions of tea-milk complexes during gastro-duodenal digestion. The objective of this study was to determine the significance of this association on the digestibility of the milk proteins and on the bioaccessibility of the tea polyphenol epigallocatechin gallate (EGCG). An
in vitro
digestion model mimicking the gastric and duodenal phases of the human gastrointestinal tract was employed to follow the fate of the milk proteins during digestion and determine the bioefficacy of EGCG isolated or encapsulated with the caseins. The samples, before and after digestion, were tested using two parallel colonic epithelial cell lines, a normal line (4D/WT) and its cancerous transformed counterpart (D/v-src). EGCG caused a decrease in proliferation of cancer cells, while in normal cells, neither isolated nor encapsulated EGCG affected cell proliferation, at concentrations |
| doi_str_mv | 10.1039/c3fo60343a |
| format | Article |
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in vitro
digestion model mimicking the gastric and duodenal phases of the human gastrointestinal tract was employed to follow the fate of the milk proteins during digestion and determine the bioefficacy of EGCG isolated or encapsulated with the caseins. The samples, before and after digestion, were tested using two parallel colonic epithelial cell lines, a normal line (4D/WT) and its cancerous transformed counterpart (D/v-src). EGCG caused a decrease in proliferation of cancer cells, while in normal cells, neither isolated nor encapsulated EGCG affected cell proliferation, at concentrations <0.15 mg ml
−1
. At higher concentrations, both isolated and encapsulated produced similar decreases in proliferation. On the other hand, the bioefficacy on the cancer cell line showed some differences at lower concentrations. The results demonstrated that regardless of the extent of digestion of the nanoencapsulated EGCG, the bioefficacy of EGCG was not diminished, confirming that casein micelles are an appropriate delivery system for polyphenols.
Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins.</description><identifier>ISSN: 2042-6496</identifier><identifier>EISSN: 2042-650X</identifier><identifier>DOI: 10.1039/c3fo60343a</identifier><identifier>PMID: 24686838</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Caseins - chemistry ; Catechin - analogs & derivatives ; Catechin - chemistry ; Catechin - pharmacology ; Cell Line ; Cell Line, Tumor ; Cell Proliferation - drug effects ; Mice ; Micelles ; Polyphenols - chemistry ; Polyphenols - pharmacology ; Rats ; Tea - chemistry</subject><ispartof>Food & function, 2014-06, Vol.5 (6), p.116-1166</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c335t-a1086f6354207da83b30ec3dd636464c616229663f036ac35c340725845981de3</citedby><cites>FETCH-LOGICAL-c335t-a1086f6354207da83b30ec3dd636464c616229663f036ac35c340725845981de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24686838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haratifar, Sanaz</creatorcontrib><creatorcontrib>Meckling, Kelly A</creatorcontrib><creatorcontrib>Corredig, Milena</creatorcontrib><title>Bioefficacy of tea catechins encapsulated in casein micelles tested on a normal mouse cell line (4D/WT) and its cancerous counterpart (D/v-src) before and after in vitro digestion</title><title>Food & function</title><addtitle>Food Funct</addtitle><description>Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins. Much less work has been conducted to understand the metabolic conversions of tea-milk complexes during gastro-duodenal digestion. The objective of this study was to determine the significance of this association on the digestibility of the milk proteins and on the bioaccessibility of the tea polyphenol epigallocatechin gallate (EGCG). An
in vitro
digestion model mimicking the gastric and duodenal phases of the human gastrointestinal tract was employed to follow the fate of the milk proteins during digestion and determine the bioefficacy of EGCG isolated or encapsulated with the caseins. The samples, before and after digestion, were tested using two parallel colonic epithelial cell lines, a normal line (4D/WT) and its cancerous transformed counterpart (D/v-src). EGCG caused a decrease in proliferation of cancer cells, while in normal cells, neither isolated nor encapsulated EGCG affected cell proliferation, at concentrations <0.15 mg ml
−1
. At higher concentrations, both isolated and encapsulated produced similar decreases in proliferation. On the other hand, the bioefficacy on the cancer cell line showed some differences at lower concentrations. The results demonstrated that regardless of the extent of digestion of the nanoencapsulated EGCG, the bioefficacy of EGCG was not diminished, confirming that casein micelles are an appropriate delivery system for polyphenols.
Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins.</description><subject>Animals</subject><subject>Caseins - chemistry</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - chemistry</subject><subject>Catechin - pharmacology</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell Proliferation - drug effects</subject><subject>Mice</subject><subject>Micelles</subject><subject>Polyphenols - chemistry</subject><subject>Polyphenols - pharmacology</subject><subject>Rats</subject><subject>Tea - chemistry</subject><issn>2042-6496</issn><issn>2042-650X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtr3TAQhUVpSUKaTfYN6u6m4F7ZI0_kZZtHWwh0k9LsjK48ahVsyZXsQH5X_mDk3Dx21WbEnI9zGA5jh6X4XApo1gZsQAES9Bu2VwlZFViL67fPf9ngLjtI6UbkB02jGrXDdiuJChWoPXb_1QWy1hlt7niwfCLNjZ7I_HU-cfJGj2nu86LjzmclUR6DM9T3lDKdFiV4rrkPcdA9H8KciC86750nvpJn699Xx1z77DClbOENxQxxE2Y_URx1nPjqbH1bpGiO-YZsiPSIa5vlJfbWTTHwzv3JcS749-yd1X2ig6e5z35dnF-dfi8uf377cfrlsjAA9VToUii0CLWsxEmnFWxAkIGuQ0CJ0mCJVdUgghWA2kBtQIqTqlayblTZEeyz1dZ3jOHfnLPbwaXlMu0pH9CWNYimRqkwo5-2qIkhpUi2HaMbdLxrS9EuPbWvPWX46Ml33gzUvaDPrWTg4xaIybyorwbt2NnMfPgfAw9PnaN6</recordid><startdate>20140601</startdate><enddate>20140601</enddate><creator>Haratifar, Sanaz</creator><creator>Meckling, Kelly A</creator><creator>Corredig, Milena</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>20140601</creationdate><title>Bioefficacy of tea catechins encapsulated in casein micelles tested on a normal mouse cell line (4D/WT) and its cancerous counterpart (D/v-src) before and after in vitro digestion</title><author>Haratifar, Sanaz ; Meckling, Kelly A ; Corredig, Milena</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-a1086f6354207da83b30ec3dd636464c616229663f036ac35c340725845981de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Caseins - chemistry</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - chemistry</topic><topic>Catechin - pharmacology</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Cell Proliferation - drug effects</topic><topic>Mice</topic><topic>Micelles</topic><topic>Polyphenols - chemistry</topic><topic>Polyphenols - pharmacology</topic><topic>Rats</topic><topic>Tea - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haratifar, Sanaz</creatorcontrib><creatorcontrib>Meckling, Kelly A</creatorcontrib><creatorcontrib>Corredig, Milena</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>Food & function</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haratifar, Sanaz</au><au>Meckling, Kelly A</au><au>Corredig, Milena</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bioefficacy of tea catechins encapsulated in casein micelles tested on a normal mouse cell line (4D/WT) and its cancerous counterpart (D/v-src) before and after in vitro digestion</atitle><jtitle>Food & function</jtitle><addtitle>Food Funct</addtitle><date>2014-06-01</date><risdate>2014</risdate><volume>5</volume><issue>6</issue><spage>116</spage><epage>1166</epage><pages>116-1166</pages><issn>2042-6496</issn><eissn>2042-650X</eissn><abstract>Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins. Much less work has been conducted to understand the metabolic conversions of tea-milk complexes during gastro-duodenal digestion. The objective of this study was to determine the significance of this association on the digestibility of the milk proteins and on the bioaccessibility of the tea polyphenol epigallocatechin gallate (EGCG). An
in vitro
digestion model mimicking the gastric and duodenal phases of the human gastrointestinal tract was employed to follow the fate of the milk proteins during digestion and determine the bioefficacy of EGCG isolated or encapsulated with the caseins. The samples, before and after digestion, were tested using two parallel colonic epithelial cell lines, a normal line (4D/WT) and its cancerous transformed counterpart (D/v-src). EGCG caused a decrease in proliferation of cancer cells, while in normal cells, neither isolated nor encapsulated EGCG affected cell proliferation, at concentrations <0.15 mg ml
−1
. At higher concentrations, both isolated and encapsulated produced similar decreases in proliferation. On the other hand, the bioefficacy on the cancer cell line showed some differences at lower concentrations. The results demonstrated that regardless of the extent of digestion of the nanoencapsulated EGCG, the bioefficacy of EGCG was not diminished, confirming that casein micelles are an appropriate delivery system for polyphenols.
Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins.</abstract><cop>England</cop><pmid>24686838</pmid><doi>10.1039/c3fo60343a</doi><tpages>7</tpages></addata></record> |
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| ispartof | Food & function, 2014-06, Vol.5 (6), p.116-1166 |
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| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Animals Caseins - chemistry Catechin - analogs & derivatives Catechin - chemistry Catechin - pharmacology Cell Line Cell Line, Tumor Cell Proliferation - drug effects Mice Micelles Polyphenols - chemistry Polyphenols - pharmacology Rats Tea - chemistry |
| title | Bioefficacy of tea catechins encapsulated in casein micelles tested on a normal mouse cell line (4D/WT) and its cancerous counterpart (D/v-src) before and after in vitro digestion |
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