Identification of a novel hypocholesterolemic protein, major royal jelly protein 1, derived from royal jelly
Royal jelly (RJ) intake lowers serum cholesterol levels in animals and humans, but the active component in RJ that lowers serum cholesterol level and its molecular mechanism are unclear. In this study, we set out to identify the bile acid-binding protein contained in RJ, because dietary bile acid-bi...
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| Veröffentlicht in: | PloS one 2014-08, Vol.9 (8), p.e105073-e105073 |
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| creator | Kashima, Yuri Kanematsu, Satoshi Asai, Saori Kusada, Mio Watanabe, Suzuyo Kawashima, Takuji Nakamura, Tadashi Shimada, Masaya Goto, Tsuyoshi Nagaoka, Satoshi |
| description | Royal jelly (RJ) intake lowers serum cholesterol levels in animals and humans, but the active component in RJ that lowers serum cholesterol level and its molecular mechanism are unclear. In this study, we set out to identify the bile acid-binding protein contained in RJ, because dietary bile acid-binding proteins including soybean protein and its peptide are effective in ameliorating hypercholesterolemia. Using a cholic acid-conjugated column, we separated some bile acid-binding proteins from RJ and identified the major RJ protein 1 (MRJP1), MRJP2, and MRJP3 as novel bile acid-binding proteins from RJ, based on matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Purified MRJP1, which is the most abundant protein of the bile acid-binding proteins in RJ, exhibited taurocholate-binding activity in vitro. The micellar solubility of cholesterol was significantly decreased in the presence of MRJP1 compared with casein in vitro. Liver bile acids levels were significantly increased, and cholesterol 7α-hydroxylase (CYP7A1) mRNA and protein tended to increase by MRJP1 feeding compared with the control. CYP7A1 mRNA and protein levels were significantly increased by MRJP1 tryptic hydrolysate treatment compared with that of casein tryptic hydrolysate in hepatocytes. MRJP1 hypocholesterolemic effect has been investigated in rats. The cholesterol-lowering action induced by MRJP1 occurs because MRJP1 interacts with bile acids induces a significant increase in fecal bile acids excretion and a tendency to increase in fecal cholesterol excretion and also enhances the hepatic cholesterol catabolism. We have identified, for the first time, a novel hypocholesterolemic protein, MRJP1, in RJ. Interestingly, MRJP1 exhibits greater hypocholesterolemic activity than the medicine β-sitosterol in rats. |
| doi_str_mv | 10.1371/journal.pone.0105073 |
| format | Article |
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In this study, we set out to identify the bile acid-binding protein contained in RJ, because dietary bile acid-binding proteins including soybean protein and its peptide are effective in ameliorating hypercholesterolemia. Using a cholic acid-conjugated column, we separated some bile acid-binding proteins from RJ and identified the major RJ protein 1 (MRJP1), MRJP2, and MRJP3 as novel bile acid-binding proteins from RJ, based on matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Purified MRJP1, which is the most abundant protein of the bile acid-binding proteins in RJ, exhibited taurocholate-binding activity in vitro. The micellar solubility of cholesterol was significantly decreased in the presence of MRJP1 compared with casein in vitro. Liver bile acids levels were significantly increased, and cholesterol 7α-hydroxylase (CYP7A1) mRNA and protein tended to increase by MRJP1 feeding compared with the control. CYP7A1 mRNA and protein levels were significantly increased by MRJP1 tryptic hydrolysate treatment compared with that of casein tryptic hydrolysate in hepatocytes. MRJP1 hypocholesterolemic effect has been investigated in rats. The cholesterol-lowering action induced by MRJP1 occurs because MRJP1 interacts with bile acids induces a significant increase in fecal bile acids excretion and a tendency to increase in fecal cholesterol excretion and also enhances the hepatic cholesterol catabolism. We have identified, for the first time, a novel hypocholesterolemic protein, MRJP1, in RJ. Interestingly, MRJP1 exhibits greater hypocholesterolemic activity than the medicine β-sitosterol in rats.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0105073</identifier><identifier>PMID: 25144734</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Animals ; Anticholesteremic agents ; Bile ; Bile acids ; Binding proteins ; Biology and Life Sciences ; Blood cholesterol ; Blotting, Western ; Caco-2 Cells ; Cardiovascular disease ; Casein ; Caseins - pharmacology ; Catabolism ; Cholesterol ; Cholesterol - blood ; Cholic acid ; Chromatography, Gel ; Cytochrome P-450 ; Deoxycholic acid ; Diet ; Electrophoresis, Polyacrylamide Gel ; Excretion ; Fatty Acids - chemistry ; Glycoproteins - chemistry ; Glycoproteins - pharmacology ; Hep G2 Cells ; Hepatocytes ; Humans ; Hydroxylase ; Hypercholesterolemia ; Insect Proteins - chemistry ; Insect Proteins - pharmacology ; Ionization ; Lipids ; Liver ; Liver - drug effects ; Liver - metabolism ; Low density lipoprotein ; Mass spectrometry ; Mass spectroscopy ; mRNA ; Phytosterols ; Protein binding ; Proteins ; Rats ; RNA ; Rodents ; Royal jelly ; Sitosterols - pharmacology ; Solubility ; Soybeans ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><ispartof>PloS one, 2014-08, Vol.9 (8), p.e105073-e105073</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Kashima et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Kashima et al 2014 Kashima et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-bc7ede4019bc53b277ed3581582dccdc4de3fa1885f483b0b0946a33c8ec8a443</citedby><cites>FETCH-LOGICAL-c692t-bc7ede4019bc53b277ed3581582dccdc4de3fa1885f483b0b0946a33c8ec8a443</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4140749/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4140749/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2095,2914,23846,27903,27904,53769,53771,79346,79347</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25144734$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Moschetta, Antonio</contributor><creatorcontrib>Kashima, Yuri</creatorcontrib><creatorcontrib>Kanematsu, Satoshi</creatorcontrib><creatorcontrib>Asai, Saori</creatorcontrib><creatorcontrib>Kusada, Mio</creatorcontrib><creatorcontrib>Watanabe, Suzuyo</creatorcontrib><creatorcontrib>Kawashima, Takuji</creatorcontrib><creatorcontrib>Nakamura, Tadashi</creatorcontrib><creatorcontrib>Shimada, Masaya</creatorcontrib><creatorcontrib>Goto, Tsuyoshi</creatorcontrib><creatorcontrib>Nagaoka, Satoshi</creatorcontrib><title>Identification of a novel hypocholesterolemic protein, major royal jelly protein 1, derived from royal jelly</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Royal jelly (RJ) intake lowers serum cholesterol levels in animals and humans, but the active component in RJ that lowers serum cholesterol level and its molecular mechanism are unclear. In this study, we set out to identify the bile acid-binding protein contained in RJ, because dietary bile acid-binding proteins including soybean protein and its peptide are effective in ameliorating hypercholesterolemia. Using a cholic acid-conjugated column, we separated some bile acid-binding proteins from RJ and identified the major RJ protein 1 (MRJP1), MRJP2, and MRJP3 as novel bile acid-binding proteins from RJ, based on matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Purified MRJP1, which is the most abundant protein of the bile acid-binding proteins in RJ, exhibited taurocholate-binding activity in vitro. The micellar solubility of cholesterol was significantly decreased in the presence of MRJP1 compared with casein in vitro. Liver bile acids levels were significantly increased, and cholesterol 7α-hydroxylase (CYP7A1) mRNA and protein tended to increase by MRJP1 feeding compared with the control. CYP7A1 mRNA and protein levels were significantly increased by MRJP1 tryptic hydrolysate treatment compared with that of casein tryptic hydrolysate in hepatocytes. MRJP1 hypocholesterolemic effect has been investigated in rats. The cholesterol-lowering action induced by MRJP1 occurs because MRJP1 interacts with bile acids induces a significant increase in fecal bile acids excretion and a tendency to increase in fecal cholesterol excretion and also enhances the hepatic cholesterol catabolism. We have identified, for the first time, a novel hypocholesterolemic protein, MRJP1, in RJ. Interestingly, MRJP1 exhibits greater hypocholesterolemic activity than the medicine β-sitosterol in rats.</description><subject>Acids</subject><subject>Animals</subject><subject>Anticholesteremic agents</subject><subject>Bile</subject><subject>Bile acids</subject><subject>Binding proteins</subject><subject>Biology and Life Sciences</subject><subject>Blood cholesterol</subject><subject>Blotting, Western</subject><subject>Caco-2 Cells</subject><subject>Cardiovascular disease</subject><subject>Casein</subject><subject>Caseins - pharmacology</subject><subject>Catabolism</subject><subject>Cholesterol</subject><subject>Cholesterol - blood</subject><subject>Cholic acid</subject><subject>Chromatography, Gel</subject><subject>Cytochrome P-450</subject><subject>Deoxycholic acid</subject><subject>Diet</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Excretion</subject><subject>Fatty Acids - chemistry</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - pharmacology</subject><subject>Hep G2 Cells</subject><subject>Hepatocytes</subject><subject>Humans</subject><subject>Hydroxylase</subject><subject>Hypercholesterolemia</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - pharmacology</subject><subject>Ionization</subject><subject>Lipids</subject><subject>Liver</subject><subject>Liver - drug effects</subject><subject>Liver - metabolism</subject><subject>Low density lipoprotein</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>mRNA</subject><subject>Phytosterols</subject><subject>Protein binding</subject><subject>Proteins</subject><subject>Rats</subject><subject>RNA</subject><subject>Rodents</subject><subject>Royal jelly</subject><subject>Sitosterols - pharmacology</subject><subject>Solubility</subject><subject>Soybeans</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser 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of a novel hypocholesterolemic protein, major royal jelly protein 1, derived from royal jelly</title><author>Kashima, Yuri ; Kanematsu, Satoshi ; Asai, Saori ; Kusada, Mio ; Watanabe, Suzuyo ; Kawashima, Takuji ; Nakamura, Tadashi ; Shimada, Masaya ; Goto, Tsuyoshi ; Nagaoka, Satoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-bc7ede4019bc53b277ed3581582dccdc4de3fa1885f483b0b0946a33c8ec8a443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Acids</topic><topic>Animals</topic><topic>Anticholesteremic agents</topic><topic>Bile</topic><topic>Bile acids</topic><topic>Binding proteins</topic><topic>Biology and Life Sciences</topic><topic>Blood cholesterol</topic><topic>Blotting, Western</topic><topic>Caco-2 Cells</topic><topic>Cardiovascular disease</topic><topic>Casein</topic><topic>Caseins - pharmacology</topic><topic>Catabolism</topic><topic>Cholesterol</topic><topic>Cholesterol - blood</topic><topic>Cholic acid</topic><topic>Chromatography, Gel</topic><topic>Cytochrome P-450</topic><topic>Deoxycholic acid</topic><topic>Diet</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Excretion</topic><topic>Fatty Acids - chemistry</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - pharmacology</topic><topic>Hep G2 Cells</topic><topic>Hepatocytes</topic><topic>Humans</topic><topic>Hydroxylase</topic><topic>Hypercholesterolemia</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - pharmacology</topic><topic>Ionization</topic><topic>Lipids</topic><topic>Liver</topic><topic>Liver - drug effects</topic><topic>Liver - metabolism</topic><topic>Low density lipoprotein</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>mRNA</topic><topic>Phytosterols</topic><topic>Protein 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Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kashima, Yuri</au><au>Kanematsu, Satoshi</au><au>Asai, Saori</au><au>Kusada, Mio</au><au>Watanabe, Suzuyo</au><au>Kawashima, Takuji</au><au>Nakamura, Tadashi</au><au>Shimada, Masaya</au><au>Goto, Tsuyoshi</au><au>Nagaoka, Satoshi</au><au>Moschetta, Antonio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a novel hypocholesterolemic protein, major royal jelly protein 1, derived from royal jelly</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-08-21</date><risdate>2014</risdate><volume>9</volume><issue>8</issue><spage>e105073</spage><epage>e105073</epage><pages>e105073-e105073</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Royal jelly (RJ) intake lowers serum cholesterol levels in animals and humans, but the active component in RJ that lowers serum cholesterol level and its molecular mechanism are unclear. In this study, we set out to identify the bile acid-binding protein contained in RJ, because dietary bile acid-binding proteins including soybean protein and its peptide are effective in ameliorating hypercholesterolemia. Using a cholic acid-conjugated column, we separated some bile acid-binding proteins from RJ and identified the major RJ protein 1 (MRJP1), MRJP2, and MRJP3 as novel bile acid-binding proteins from RJ, based on matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Purified MRJP1, which is the most abundant protein of the bile acid-binding proteins in RJ, exhibited taurocholate-binding activity in vitro. The micellar solubility of cholesterol was significantly decreased in the presence of MRJP1 compared with casein in vitro. Liver bile acids levels were significantly increased, and cholesterol 7α-hydroxylase (CYP7A1) mRNA and protein tended to increase by MRJP1 feeding compared with the control. CYP7A1 mRNA and protein levels were significantly increased by MRJP1 tryptic hydrolysate treatment compared with that of casein tryptic hydrolysate in hepatocytes. MRJP1 hypocholesterolemic effect has been investigated in rats. The cholesterol-lowering action induced by MRJP1 occurs because MRJP1 interacts with bile acids induces a significant increase in fecal bile acids excretion and a tendency to increase in fecal cholesterol excretion and also enhances the hepatic cholesterol catabolism. We have identified, for the first time, a novel hypocholesterolemic protein, MRJP1, in RJ. Interestingly, MRJP1 exhibits greater hypocholesterolemic activity than the medicine β-sitosterol in rats.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25144734</pmid><doi>10.1371/journal.pone.0105073</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2014-08, Vol.9 (8), p.e105073-e105073 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1555283585 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Acids Animals Anticholesteremic agents Bile Bile acids Binding proteins Biology and Life Sciences Blood cholesterol Blotting, Western Caco-2 Cells Cardiovascular disease Casein Caseins - pharmacology Catabolism Cholesterol Cholesterol - blood Cholic acid Chromatography, Gel Cytochrome P-450 Deoxycholic acid Diet Electrophoresis, Polyacrylamide Gel Excretion Fatty Acids - chemistry Glycoproteins - chemistry Glycoproteins - pharmacology Hep G2 Cells Hepatocytes Humans Hydroxylase Hypercholesterolemia Insect Proteins - chemistry Insect Proteins - pharmacology Ionization Lipids Liver Liver - drug effects Liver - metabolism Low density lipoprotein Mass spectrometry Mass spectroscopy mRNA Phytosterols Protein binding Proteins Rats RNA Rodents Royal jelly Sitosterols - pharmacology Solubility Soybeans Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| title | Identification of a novel hypocholesterolemic protein, major royal jelly protein 1, derived from royal jelly |
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