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The adequacy and efficacy of formulas containing 18∶3n−3 and\u002For fish oil in providing 22∶6n−3 for deposition was investigated in piglets fed formula from birth to 15 days. The test formulas contained high (HL) or low (LL) 18∶3n−3 (3.9 or 0.7% of the total formula fatty acids, respectively), or low 18∶3n−3 plus fish oil (LL+FO) to provide C20 and C22 n−3 polyunsaturated fatty acids (0.8% of total fatty acids). Fatty acid analyses of synaptic plasma membrane and retina ethanolamine phospholipids (EPL), which are especially enriched in 22∶6n−3, were compared to those of 15-day-old piglets fed sow milk (SM). Feeding LL resulted in lower 22∶6n−3 in synaptic plasma membrane. Fatty acid levels in HL and LL+FO piglets were equivalent to SM, with the exception of lower 22∶5n−3 in the synaptic plasma membrane of LL+FO and in the retina of HL and LL+FO-fed piglets. Levels of 22∶4n−6 were also lower in the retina of the LL+FO group. The results suggest formula 18∶3n−3 is at least 24% as effective as C20 and C22 n−3 fatty acids as a source of membrane 22∶6n−3. This study shows dietary 18∶3n−3, as the only n−3 fatty acid, can support deposition of comparable percentage of 22∶6n−3 to natural milk. Fish oil also supported tissue levels of 22∶6n−3 similar to natural milk; however, lower 22∶4n−6 may indicate possible inhibitory effects on n−6 metabolism.",{"EN":268},"Docosahexaenoic acid in developing brain and retina of piglets fed high or low α-linolenate formula with and without fish oil",{"VOID":270},"[]",{"VOID":272},"Bourre, J.M., Francois, M., Youyou, A., Dumont, O., Piciotti, M., Pascal, G., and Durand, G. (1989)J. Nutr. 119, 1880–1892.\nYamamoto, N., Sitoh, M., Moriuchi, A., and Nomura, M. (1987)J. Lipid Res. 28, 144–151.\nConnor, W.E., Neuringer, M., and Lin, D.S. (1990)J. Lipid Res. 31, 237–247.\nHrboticky, N., MacKinnon, M.J., Puterman, M.L., and Innis, S.M. (1989)J. Lipid Res. 30, 1173–1184.\nHrboticky, N., MacKinnon, M.J., and Innis, S.M. (1990)Am. J. Clin. Nutr. 51, 173–182.\nWainbright, P.E., Huang, Y.S., Bulman-Fleming, B., Mills, D.E., Redden, P., and McCutcheon, D. (1991)Lipids 26, 37–45.\nConnor, W.E., and Neuringer, M. (1988) inBiological Membranes: Aberrations in Membrane Structure and Function, pp. 275–294, Alan R. Liss, New York.\nHrboticky, N., MacKinnon, M.J., and Innis, S.M. (1991)Am. J. Clin. Nutr. 53, 483–490.\nBenolken, R.M., Anderson, R.E., and Wheeler, T.G. (1973)Science, 182, 1253–1254.\nCarlson, S., Cooke, R., Werkman, S., and Peeples, J. (1989)FASEB J. 4, A1056 (Abstract no. 4822).\nUauy, R., Birch, D.G., Birch, E.E., Tyson, J.E., and Hoffman, D.R. (1990)Pediatr. Res. 28, 485–492.\nCrawford, M.A., Hassam, A.G., and Williams, G. (1976)Lancet 28, 452–453.\nJensen, R.G. (1989) inTextbook of Gastroenterology and Nutrition in Infancy, 2nd edn. (Lebenthal, E., ed.), pp. 157–208, Raven Press, New York.\nPutnam, J.C., Carlson, S.E., and Devoe, P.W. (1982)Am. J. Clin. Nutr. 36, 106–114.\nCarlson, S.E., Rhodes, P.G., and Ferguson, M.G. (1986)Am. J. Clin. Nutr. 44, 798–804.\nClandinin, M.T., Chappell, J.E., Leong, S., Heim, T., Swyer, P.R., and Chance, G.W. (1980)Early Hum. Dev. 4, 131–138.\nClandinin, M.T., Chappell, J.E., and Van Aerde, J.E.E. (1989)Acta Paediatr. Scand. Suppl. 351, 63–71.\nUauy, R., Treen, M., and Hoffman, D.R. (1989)Seminars in Perinatology 13, 118–130.\nCarlson, S.E., Rhodes, P.G., Rao, V.S., and Goldgar, D.E. (1987)Pediatr. Res. 21, 507–510.\nFoote, K.D., Hrboticky, N., MacKinnon, M.J., and Innis, S.M. (1990)Am. J. Clin. Nutr. 51, 1001–1006.\nArbuckle, L.D., Rioux, F.M., MacKinnon, M.J., Hrboticky, N., and Innis, S.M. (1991)J. Nutr. 121, 1536–1547.\nBourre, J.M., Bonnell, M., Dumont, O., Piciotti, M., Nalbone, G., and Lafont, H. (1988)Biochim. Biophys. Acta 960, 458–461.\nPhilbrick, D.-J., Mahadevappa, V.G., Ackman, R.G., and Holub, B.J. (1987)J. Nutr. 117, 1663–1670.\nLiu, C.C.F., Carlson, S.E., Rhodes, P.G., Rao, V.S., and Meydrech, E.F. (1987)Pediatr. Res. 22, 292–296.\nWade, A.E. (1986)J. Environ. Pathol. Toxicol. Oncol. 6, 161–189.\nSmith, W.L. (1989)Biochem. J. 259, 315–324.\nGurr, M.I. (1983)Prog. Lipid Res. 22, 257–287.\nAnderson, G.J., Connor, W.E., and Corliss, J.D. (1990)Pediatr. Res. 27, 89–97.\nDobbing, J., and Sands, J. (1979)Early Hum. Dev. 3, 79–83.\nSastry, P.S. (1985)Prog. Lipid Res. 24, 69–176.\nAnderson, R.E. (1970)Exp. Eye Res. 10, 339–344.\nLepage, G., and Roy, C.C. (1986)J. Lipid Res. 27, 114–120.\nCruz, T.F., and Gurd, J.W. (1978)J. Biol. Chem. 253, 7314–7318.\nFolch, J., Lees, M., and Stanley, G.H.S. (1957)J. Biol. Chem. 226, 497–509.\nHolub, B.J., and Skeaff, C.M. (1987)Methods Enzymol. 141, 234–244.\nMontgomery, D.C. (1984)Design and Analysis of Experiments, 2nd edn., pp. 43–121, John Wiley & Sons, New York.\nAnding, R.H., and Hwang, D.H. (1986)Lipids 21, 697–701.\nLeyton, J., Drurry, P.J., and Crawford, M.A. (1987)Br. J. Nutr. 57, 383–393.\nClouet, P., Niot, I., and Bezard, J. (1989)Biochem. J. 263, 867–873.\nBarzanti, V., Maranesi, M., Solaini, G., and Turchetto, E. (1990)J. Nutr. Biochem. 1, 305–309.\nHagve, T.A., and Christophersen, B.O. (1986)Biochim. Biophys. Acta 875, 165–173.",{"VOID":274},"10.1007\u002FBF02535805","PUBLICATION","VERIFIED","2024-08-31T14:45:59.502+00:00","Auto Verify","https:\u002F\u002Faocs.onlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002FBF02535805",[281,297],{"id":282,"sortIndex":18,"researcher":17,"roles":283,"affiliations":285,"properties":294,"displayName":296,"givenName":17,"familyName":17},"b7ab5b50-bad5-4f8d-9b6a-24f88dd59ac8",[284],"AUTHOR",[286],{"id":287,"sortIndex":18,"affiliation":288,"properties":17},"eda18ae1-2078-4177-9a6a-90674a6880bb",{"id":287,"createTime":17,"updateTime":17,"relativeEntities":289,"slug":17,"properties":290,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":293,"statistic":17},[],{"title":291},{"VI":292},"Department of Human Nutrition, University of British Columbia, Vancouver, Canada",[],{"title":295},{"VI":296},"L. 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               Culex quinquefasciatus andCulex tritaeniorhynchus cells were grown in spinner culture medium. The cells were harvested at late logarithmic and stationary phases of growth. The total lipid, total neutral lipid, and total phospholipid contents of the cells were analyzed to determine changes that occurred in the fatty acid profiles of the lipids with aging and between species. There was an increase in the amount of total neutral lipids with a corresponding decrease in amount of total phospholipid from logarithmic to stationary phases of growth of theCulex quinquefasciatus cells. Chain elongation and\u002For desaturation of acids occurred with aging of cells. The fatty acids of the phospholipids had a longer average chain length than the neutral lipids.",{"EN":385},"Comparison of the lipid composition ofCulex quinquefasciatus andCulex tritaeniorhynchus cells obtained from the logarithmic and stationary phases of growth",{"VOID":387},"[\"12006814264308817186\"]",{"VOID":389},"Singh, K.R.P., Curr. Sci. 36:506 (1967).\nSingh, K.R.P., and S.D. Paul, Ibid. 37:65 (1968).\nSingh, K.R.P., and S.D. Paul, Ind. J. Med. Res. 56:815 (1968).\nBuckley, S.M., Proc. Soc. Exp. Biol. Med. 131:625 (1969).\nIgarashi, A., F. Sasao, S. Wungkobkiat, and K. Fukai, Biken J. 16:17 (1973).\nPeleg, J., Virology 35:617 (1968).\nIgarashi, A., T. Fukuoka, F. Sasao, S. Surimarut, and K. Fukai, Biken J. 16:67 (1973).\nFujita, N., Y. Yasui, S. Kitamuri, and S. Hotta, Kobe J. Med. Sci. 14:241 (1968).\nHsu, S.H., W.H. Mao, and J.H. Cross, J. Med. Entomol. 7:703 (1970).\nFast, P.G., Lipids 1:209 (1966).\nClayton, R.B., J. Lipid Res. 5:3 (1964).\nDadd, R.H., in “Annual Review Entomology,” Vol. 18, Edited by T.E. Mittler, C.N. Smith, R.F. Smith, Annual Review, Inc., Palo Alto, CA, 1973, p. 381.\nBarroso, C., A.M. Municio, and A. Ribera, Comp. Biochem. Physiol. 28:239 (1969).\nMadariaga, M.A., A.M. Municio, and A. Ribera, Ibid. 35:57 (1970).\nMcMeans, E., T.K. Yang, L.E. Anderson, and H.M. Jenkin, Lipids 10:99 (1975).\nAnderson, L.E., H. Kurzepa, and H.M. Jenkin, Abstracts Ann. Meeting, Am. Soc. Microbiol. p. 227 (1974).\nHsu, S.H., S.Y. Li, and J.H. Cross, J. Med. Entomol. 9:86 (1972).\nMitsuhashi, J., Jap. J. Appl. Entomol. Zool. 9:107 (1965).\nHanks, J.H., and R.E. Wallace, Proc. Soc. Exp. Biol. Med. 71:196 (1949).\nMakino, S., H.M. Jenkin, H.M. Yu, and D. Townsend, J. Bacterol. 103:62 (1970).\nTownsend, D., B. Livermore, and H. Jenkin, Microchem. J. 16:456 (1971).\nJenkin, H., D. Townsend, S. Makino, and T.K. Yang, in “Current Topics in Microbiology and Immunology,” Vol. 55, Edited by E. Weiss, Springer-Verlag, New York, NY, 1971, p. 97.\nFast, P.G., Mem. Entomol. Soc. Can. 37:1 (1964).\nFast, P.G., in “Progress in the Chemistry of Fats and Other Lipids,” Vol. 11, Edited by R.T. Holman, Pergamon Press, Oxford, England, 1970, p. 181.\nMunicio, A.M., J.M. Odriozola, and A. Pineiro, Comp. Biochem. Biophys. 37:387 (1970).\nMunicio, A.M., J.M. Odriozola, and A. Pineiro, and A. Ribera, Biochim. Biophys. Acta 280:248 (1972).",{"VOID":391},"10.1007\u002FBF02532581","2024-05-16T23:38:05.104+00:00","https:\u002F\u002Faocs.onlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002FBF02532581",[395,410,423,437,451],{"id":396,"sortIndex":18,"researcher":17,"roles":397,"affiliations":398,"properties":407,"displayName":409,"givenName":17,"familyName":17},"fa715702-7405-48b5-aa7d-752528e1d46d",[284],[399],{"id":400,"sortIndex":18,"affiliation":401,"properties":17},"09df6f8e-da0c-49b2-b139-f8c058533de6",{"id":400,"createTime":17,"updateTime":17,"relativeEntities":402,"slug":17,"properties":403,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":406,"statistic":17},[],{"title":404},{"VI":405},"The Hormel Institute, University of Minnesota, Austin",[],{"title":408},{"VI":409},"E. 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Yang",{"id":424,"sortIndex":425,"researcher":17,"roles":426,"affiliations":427,"properties":434,"displayName":436,"givenName":17,"familyName":17},"8ca34c36-1bb6-4a93-af89-af8300ffd7cf",2,[284],[428],{"id":400,"sortIndex":18,"affiliation":429,"properties":17},{"id":400,"createTime":17,"updateTime":17,"relativeEntities":430,"slug":17,"properties":431,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":433,"statistic":17},[],{"title":432},{"VI":405},[],{"title":435},{"VI":436},"L. E. 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the aim of obtaining a better understanding of lipids-lipases interactions in bacterioplankton communities in oceans, we used different methods for measuring lipase activities in pure cultures of the marine strain Alteromonas macleodii. The decay of tripalmitate added to cultures was followed chemically over time. In an enzymatic approach, lipase activities were measured using the fluorogenic lipid analogs MUF-palmitate and ELF-palmitate. When hydrolyzed by lipase, the non-fluorescent substrates release MUF and ELF Alcohol (ELFA) which are fluorescent. As shown by spectrofluorometry, ELF-palmitate was an efficient competitor for MUF-palmitate. However, the activities reached using these two fluorogenic substrates were different, but still much higher than the tripalmitate hydrolysis rate, measured chemically. MUF- and ELF-palmitate would not be hydrolyzed by lipase sensu stricto (defined as triacylglycerol acylesterase E.C. 3.1.1.3) but rather reflects lipolytic activities in a broad sense. ELFA is also water-insoluble and theoretically precipitates in the external membrane of bacteria causing its hydrolysis, which would allow microscopic identification of active cells. By epifluorescence microscopy, the accumulation of ELFA fluorescence over time was detected (as large, diffuse halos), but no precipitates were clearly associated with bacteria on slide preparations, neither for pure cultures of Alteromonas macleodii nor for natural samples from the Bay of Marseille, France. Among possible biases, those related to the hydrophobic\u002Fhydrophilic conditions required for precipitation are discussed.",{"EN":537},"Determination of Lipid Degradation by Marine Lipase-Producing Bacteria: Critical Evaluation of Lipase Activity Assays",{"VOID":539},"[\"6127077973321589031\"]",{"VOID":541},"citation_journal_title=Estuar Coast Mar Sci; citation_title=Concentration and microbial utilization of small organic molecules in the Scheldt estuary, the Belgian coastal zone of the North Sea and the English Channel; citation_author=G Billen, C Joiris, J Wijnant, G Gillain; citation_volume=11; citation_publication_date=1980; citation_pages=279-294; citation_doi=10.1016\u002FS0302-3524(80)80084-3; citation_id=CR1\ncitation_journal_title=Science; citation_title=Bacterioplankton: a sink for a carbon in a coastal marine plankton community; citation_author=HW Ducklow, DA Purdie, PJL Williams, JM Davies; citation_volume=232; citation_publication_date=1986; citation_pages=865-867; citation_doi=10.1126\u002Fscience.232.4752.865; citation_id=CR2\ncitation_journal_title=Oceanogr Mar Biol A Rev; citation_title=The role of bacteria in the turnover of organic matter en the sea; citation_author=IR Joint, RJ Morris; citation_volume=20; citation_publication_date=1982; citation_pages=65-118; citation_id=CR3\ncitation_journal_title=Hydrobiologia; citation_title=Energetics of microbial food webs; citation_author=L Pomeroy, W Wiebe; citation_volume=159; citation_publication_date=1988; citation_pages=7-18; citation_id=CR4\ncitation_title=Analysis of composition and function by a molecular–biochemical approach; citation_inbook_title=Microbial ecology of lake Plußsee; citation_publication_date=1994; citation_id=CR5; citation_author=U Münster; citation_author=D Albrecht; citation_publisher=Springer\ncitation_journal_title=Ann Limnol; citation_title=Nouvelles approches d’étude des réseaux microbiens; citation_author=M Bianchi; citation_volume=34; citation_issue=4; citation_publication_date=1998; citation_pages=465-473; citation_doi=10.1051\u002Flimn\u002F1998037; citation_id=CR6\ncitation_journal_title=J Am Oil Chem Soc; citation_title=Lipids in sea water; citation_author=LM Jeffrey; citation_volume=43; citation_publication_date=1966; citation_pages=211-214; citation_doi=10.1007\u002FBF02641089; citation_id=CR7\ncitation_journal_title=Jpn J Limnol; citation_title=Chemical composition of organic compounds present in water of the Tamagawa River; citation_author=N Ogura, Y Ambe, K Ogura, R Ishiwatari, T Mizutani, Y Satoh, H Matsushima, T Katase, M Ochiai, K Tadokoro, T Takada, K Sughihara, G Matsumoto, N Nakamoto, M Funakoshi, T Hanya; citation_volume=36; citation_publication_date=1975; citation_pages=23-30; citation_id=CR8\nBourguet N, Goutx M, Ghiglione JF, Pujo-Pay M, Mével G, Momzikoff A, Mousseau L, Guigue C, Garcia N, Raimbault P, Pete R, Oriol L, Lefèvre D (2009) Lipid biomarkers and bacterial lipase activities as indicators of organic matter and bacterial dynamics in contrasted regimes at the dyfamed site, NW Mediterranean. 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(HMG)-CoA reductase, the rate-limiting enzyme in cholesterol biosynthesis, catalyzes the formation of mevalonate which is also required for cell proliferation. Changes in HMG-CoA reductase may mediate the differential effects of n-3 and n-6 polyunsaturated fatty acids (PUFA) on experimental mammary tumorigenesis, but the mechanisms by which these fatty acids regulate HMG-CoA reductase are unclear. To determine whether the low density lipoprotein receptor (LDL-R) is required for this regulation, groups of female LDL-R knockout (−\u002F−) and wild-type (+\u002F+) mice were fed 7% fat diets rich in either n-3 (menhaden oil) or n-6 (safflower oil) PUFA for 1 wk. Dietary PUFA and deletion of the LDL-R had independent effects on HMG-CoA reductase and serum lipids, and a significant diet-gene interaction was observed. The effects of PUFA on HMG-CoA reductase in the mammary gland, but not the liver, were mediated by the LDL-R. We also observed that differences in HMG-CoA reductase and serum LDL-cholesterol, high density lipoprotein cholesterol, and triglycerides between −\u002F− and +\u002F+ mice were dependent on whether the mice were fed n-3 or n-6 PUFA. Differences between −\u002F− and +\u002F+ mice were much greater when animals were fed n-6 PUFA rather than n-3 PUFA. These results show that the LDL-R mediates the effects of PUFA on HMG-CoA reductase in the mammary gland but not the liver. Furthermore, the composition of dietary PUFA profoundly influences the effects of deleting the LDL-R on HMG-CoA reductase and serum lipids and suggests that diet may influence the phenotype of other knockout or transgenic animals.",{"EN":660},"Regulation of mevalonate synthesis in low density lipoprotein receptor knockout mice fed n-3 or n-6 polyunsaturated fatty acids",{"VOID":662},"[\"7509693497163692518\"]",{"VOID":664},"10.1007\u002Fs11745-999-0455-8","2024-05-03T08:37:42.392+00:00","https:\u002F\u002Faocs.onlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002Fs11745-999-0455-8",[668,685],{"id":669,"sortIndex":18,"researcher":17,"roles":670,"affiliations":671,"properties":680,"displayName":682,"givenName":17,"familyName":17},"f5590825-7b16-4541-9e34-0b105741dde7",[284],[672],{"id":673,"sortIndex":18,"affiliation":674,"properties":17},"42268854-46fb-4ec0-a4dc-6059ef7b8fee",{"id":673,"createTime":17,"updateTime":17,"relativeEntities":675,"slug":17,"properties":676,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":679,"statistic":17},[],{"title":677},{"VI":678},"Department of Nutritional Sciences, Faculty of Medicine, University of Toronto, Toronto, Canada",[],{"title":681,"gsAuthor":683},{"VI":682},"Ahmed El-Sohemy",{"VOID":684},"[\"p5ZwiGcAAAAJ\"]",{"id":686,"sortIndex":299,"researcher":17,"roles":687,"affiliations":688,"properties":695,"displayName":697,"givenName":17,"familyName":17},"7255766c-446b-45f6-b656-6312629dd58b",[284],[689],{"id":673,"sortIndex":18,"affiliation":690,"properties":17},{"id":673,"createTime":17,"updateTime":17,"relativeEntities":691,"slug":17,"properties":692,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":694,"statistic":17},[],{"title":693},{"VI":678},[],{"title":696},{"VI":697},"Michael C. 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Fat content and FA composition of liver, plasma, and feces were analyzed. Key enzymes involved in FA synthesis and catabolism in liver, TG, cholesterol, and FFA content of plasma were also determined. Dietary CLA increased TG, total cholesterol, and HDL cholesterol levels in plasma. The increased plasma TG level could be caused by increased FA synthesis in the liver after CLA feeding, because the activity of FA synthase in the liver increased after dietary CLA treatment. Dietary CLA changed the FA composition of feces but had no effect on fat content. Compared to the amounts of linoleic and linolenic acids present in the control diet, the amounts excreted into the feces of CLA‐treated birds were significantly higher. Liver weights of broilers significantly increased after CLA feeding, but there was no difference in liver fat content among the different CLA treatments. CLA treatment did not influence total FFA content in plasma; however, there was a significant difference in the composition of FFA. Dietary CLA reduced the content of linoleic and arachidonic acids in both plasma and liver.\u003C\u002Fjats:p>",{"EN":1079},"Dietary CLA affects lipid metabolism in broiler chicks",{"VOID":1081},"12880105",{"VOID":1083},"10.1007\u002Fs11745-003-1091-z","2024-06-24T09:38:37.320+00:00",[1086],"EN","https:\u002F\u002Faocs.onlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002Fs11745-003-1091-z",[1089,1110],{"id":1090,"sortIndex":18,"researcher":17,"roles":1091,"affiliations":1092,"properties":1101,"displayName":1105,"givenName":17,"familyName":17},"3f2b9777-f5f0-402d-8424-111b38523161",[],[1093],{"id":1094,"sortIndex":18,"affiliation":1095,"properties":17},"15a1941a-3ba9-488d-835e-093df3dabdc3",{"id":1094,"createTime":17,"updateTime":17,"relativeEntities":1096,"slug":17,"properties":1097,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":1100,"statistic":17},[],{"title":1098},{"EN":1099},"Department of Animal Science, Iowa State University, 2276 Kildee Hall, Ames, IA, 50011",[],{"orcid":1102,"title":1104,"gsAuthor":1106,"openalex":1108},{"VOID":1103},"https:\u002F\u002Forcid.org\u002F0000-0002-7232-072X",{"EN":1105},"Min Du",{"VOID":1107},"[\"gzjcTFUAAAAJ\"]",{"VOID":1109},"A5074270918",{"id":1111,"sortIndex":299,"researcher":17,"roles":1112,"affiliations":1113,"properties":1120,"displayName":1124,"givenName":17,"familyName":17},"5e6276e2-31b2-44a6-85c1-f607c21976fb",[],[1114],{"id":1094,"sortIndex":18,"affiliation":1115,"properties":17},{"id":1094,"createTime":17,"updateTime":17,"relativeEntities":1116,"slug":17,"properties":1117,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":1119,"statistic":17},[],{"title":1118},{"EN":1099},[],{"orcid":1121,"title":1123,"gsAuthor":1125,"openalex":1127},{"VOID":1122},"https:\u002F\u002Forcid.org\u002F0000-0001-9523-7630",{"EN":1124},"Dong U. 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It is apparent that long-chain polyunsaturated n−3 fatty acids, either as free acids or as part of triglycerides, are readily absorbed in the gut and transported by the circulatory system. Indeed, it would appear that long-chain polyunsaturated n−3 fatty acids are digested, absorbed and transported similarly to other long-chain fatty acids with only minor variations, although there is much that is still not understood about these processes. The main unresolved issues in the area of the absorption and transport of long-chain polyunsaturated n−3 fatty acids appear to be: 1) If they, when located in the 2-position of triglycerides, have unique metabolic pathways; and 2) whether the unnatural forms, i.e., methyl or ethyl ester derivatives, are suitable vehicles for administration as dietary supplements. The effect in man of dietary, long-chain polyunsaturated n−3 fatty acids on blood serum lipid and lipoprotein levels, particularly the low density lipoproteins, remains controversial, except for the well-documented reduction in serum triglyceride levels. Also, there is uncertainty regarding their distribution and metabolism in tissues. Finally, if the consumption of long-chain polyunsaturated n−3 fatty acids has beneficial health consequences, what is the appropriate therapeutic dose? In view of these important, unresolved issues and uncertainties, it would seem prudent to direct additional research toward a better understanding of the overall process by which fat is digested, absorbed and transported.",{"EN":1288},"Absorption and transport of fat in mammals with emphasis on n−3 polyunsaturated fatty acids",{"VOID":1290},"[\"10804238314589812329\"]",{"VOID":1292},"citation_journal_title=Prog. Lipid Res.; citation_author=J. 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Harris, D.R. Illingworth; citation_volume=312; citation_publication_date=1985; citation_pages=1210-1219; citation_doi=10.1056\u002FNEJM198505093121902; citation_id=CR199\ncitation_title=n−3 News I; citation_publication_date=1986; citation_id=CR200; citation_author=A.P. Bimbo; citation_publisher=Department of Preventive Medicine Harvard Medical School\ncitation_journal_title=Ann. Rev. Nutr.; citation_author=D.A. Sweetser, R.O. Heuckeroth, J.I. Gordon; citation_volume=7; citation_publication_date=1987; citation_pages=337-359; citation_doi=10.1146\u002Fannurev.nu.07.070187.002005; citation_id=CR201\ncitation_journal_title=Rev. Franc. Corps Gras; citation_author=F. Driss, Ph. Darcet; citation_volume=35; citation_publication_date=1988; citation_pages=7-11; citation_id=CR202",{"VOID":1294},"10.1007\u002FBF02535644","2024-06-24T23:41:40.924+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02535644","https:\u002F\u002Flink.springer.com\u002Fcontent\u002Fpdf\u002F10.1007\u002FBF02535644.pdf",[1299,1314],{"id":1300,"sortIndex":18,"researcher":17,"roles":1301,"affiliations":1302,"properties":1311,"displayName":1313,"givenName":17,"familyName":17},"dde24c51-cf81-4eb3-9cce-bd2a085f1718",[284],[1303],{"id":1304,"sortIndex":18,"affiliation":1305,"properties":17},"981a1554-c14b-4d04-ad6e-2fc2f5c1920c",{"id":1304,"createTime":17,"updateTime":17,"relativeEntities":1306,"slug":17,"properties":1307,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":1310,"statistic":17},[],{"title":1308},{"VI":1309},"Biochemistry Research Unit, Western Human Nutrition Research Center, ARS, U.S. Dept. of Agriculture, San Francisco",[],{"title":1312},{"VI":1313},"Nelson, Gary J.",{"id":1315,"sortIndex":299,"researcher":17,"roles":1316,"affiliations":1317,"properties":1326,"displayName":1328,"givenName":17,"familyName":17},"74b9b960-31de-46df-a7ee-903a96995ea4",[284],[1318],{"id":1319,"sortIndex":18,"affiliation":1320,"properties":17},"04d95ff6-7976-4fff-84cf-9b8b9bfa0b25",{"id":1319,"createTime":17,"updateTime":17,"relativeEntities":1321,"slug":17,"properties":1322,"entityType":17,"verifyStatus":17,"verifyTime":17,"verifyNote":17,"languages":17,"translateLanguages":17,"viewCount":17,"url":17,"parentIds":1325,"statistic":17},[],{"title":1323},{"VI":1324},"Canadian Institute of Fisheries Technology, Technical University of Nova Scotia, Halifax, Canada",[],{"title":1327},{"VI":1328},"Ackman, Robert 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s":17,"references":17,"isForceReanalyzing":374},"8552ae54-c7f1-43a1-815a-ba7709c0a757","2024-01-28T16:23:36.771+00:00","2026-07-23T11:33:02.022+00:00",[],"Purification-molecular-cloning-and-expression-of-the-gene-encoding-fatty-acid-13-hydroperoxide-lyase-from-guava-fruit-Psidium-guajava-",{"abstract":1398,"title":1400,"gsPaper":1402,"references":1404,"doi":1406},{"EN":1399},"Guava fruit was identified as a particularly rich source of 13-hydroperoxide lyase activity. The enzyme proved stable to chromatographic procedures and was purified to homogeneity. Based on gel filtration and gel electrophoresis, the native enzyme appears to be a homotetramer with subunits of 55 kD. Starting with primers based on the peptide sequence, the enzyme was cloned by polymerase chain reaction with 3′ and 5′ rapid amplification of cDNA ends. The sequence shows approximately 60–70% identity to known 13-hydroperoxide lyases and is classified in cytochrome P450 74B subfamily as CYP74B5. The cDNA was expressed in Escherichia coli (BL21 cells), with optimal enzyme activity obtained in the absence of isopropyl-β-d-thiogalactopyranoside and σ-aminolevulinic acid. The expressed enzyme metabolized 13(S)-hydroperoxylinolenic acid over 10-fold faster than 13(S)-hydroperoxylinoleic acid and the 9-hydroperoxides of linoleic and linolenic acids. 13(S)-Hydroperoxylinolenic acid was converted to 12-oxododec-9(Z)-enoic acid and 3(Z)-hexenal, as identified by gas chromatography-mass spectrometry. The turnover number with this substrate, with enzyme concentration estimated from the Soret absorbance, was≈2000\u002Fs, comparable to values reported for the related allene oxide synthases. Distinctive features of the guava 13-hydroperoxide lyase and related cytochrome P450 are discussed.",{"EN":1401},"Purification, molecular cloning, and expression of the gene encoding fatty acid 13-hydroperoxide lyase from guava fruit (Psidium guajava)",{"VOID":1403},"[\"11494245001542964184\"]",{"VOID":1405},"Kim, I.S., and Grosch, W. (1981) Partial-Purification and Properties of a Hydroperoxide Lyase from Fruits of Pear, J. Agric. Food. Chem. 29, 1220–1225.\nHatanaka, A., Kajiwara, T., and Sekija, J. (1987) Biosynthetic Pathway for C6-Aldehydes Formation from Linolenic Acid in Green Leaves, Chem. Phys. Lipids 44, 341–361.\nCroft, K.P.C., Jüttner, F., and Slusarenko, A.J. (1993) Volatile Products of the Lipoxygenase Pathway Evolved from Phaseolus vulgaris (L.) Leaves Inoculated with Pseudomonas syringae pv. phaseolicola, Plant Physiol. 101, 13–24.\nDickens, J.C., Billings, R.F., and Payne, T.L. (1992) Green Leaf Volatiles Interrupt Aggregation Pheromone Response in Bark Beetles Infesting Southern Pines, Experientia 48, 523–524.\nHatanaka, A. (1993) The Biogeneration of Green Odor by Green Leaves, Phytochemistry 34, 1201–1218.\nTressl, R., and Drawert, F. (1973) Biogenesis of Banana Volatiles, J. Agric. Food Chem. 21, 560–565.\nVick, B.A., and Zimmerman, D.C. (1976) Lipoxygenase and Hydroperoxide Lyase in Germinating Watermelon Seedlings, Plant Physiol. 57, 780–788.\nSchreier, P., and Lorenz, G. (1982) Separation, Partial Purification and Characterisation of a Fatty Acid Hydroperoxide Cleaving Enzyme from Apple and Tomato Fruits, Z. Naturforsch. C 37, 165–173.\nMatsui, K., Shibata, Y., Kajiwara, T., and Hatanaka, A. (1989) Separation of 13-Hydroperoxide and 9-Hydroperoxide Lyase Activities in Cotyledons of Cucumber Seedlings, Z. Natur forsch. C 44, 883–885.\nOlias, J.M., Rios, J.J., Valle, M., Zamora, R., Sanz, L.C., and Axelrod, B. (1990) Fatty Acid Hydroperoxide Lyase in Germinating Soybean Seedlings, J. Agric. Food Chem. 38, 624–630.\nMatsui, K., Toyota, H., Kajiwara, T., Kakuno, T., and Hatanaka, A. (1991) Fatty Acid Hydroperoxide Cleaving Enzyme, Hydroperoxide Lyase, from Tea Leaves, Phytochemistry 30, 2109–2113.\nShibata, Y., Matsui, K., Kajiwara, T., and Hatanaka, A. (1995) Purification and Properties of Fatty Acid Hydroperoxide Lyase from Green Bell Pepper Fruits, Plant Cell Physiol. 36, 147–156.\nItoh, A., and Vick, B.A. (1999) The Purification and Characterization of Fatty Acid Hydroperoxide Lyase in Sunflower, Biochim. Biophys. Acta 1436, 531–540.\nMatsui, K., Shibutani, M., Hase, T., and Kajiwara, T. (1996) Bell Pepper Fruit Fatty Acid Hydroperoxide Lyase Is a Cytochrome P450 (CYP74B), FEBS Lett. 394, 21–24.\nBate, N., Sivasankar, S., Moxon, C., Riley, J.M., Thompson, J.E., and Rothstein, S.J. (1998) Molecular Characterization of an Arabidopsis Gene Encoding Hydroperoxide Lyase, a Cytochrome P-450 That Is Wound Inducible, Plant Physiol. 117, 1393–1400.\nWan, C.Y., and Wilkins, T.A. (1994) A Modified Hot Borate Method Significantly Enhances the Yield of High-Quality RNA from Cotton (Gossypium hirsutum L.), Anal. Biochem. 223, 7–12.\nBrash, A.R., Boeglin, W.E., Chang, M.S., and Shieh, B.-H. (1996) Purification and Molecular Cloning of an 8R-Lipoxygenase from the Coral Plexaura homomalla Reveal the Related Primary Structures of R- and S-Lipoxygenases, J. Biol. Chem. 271, 20949–20957.\nHoffman, B.J., Broadwater, J.A., Johnson, P., Harper, J., Fox, B.G., and Kenealy, W.R. (1995) Lactose Fed-Batch Overexpression of Recombinant Metalloproteins in Escherichia coli BL21 (DE3): Process Control Yielding High Levels of Metal-Incorporated Soluble Protein, Prot. Express. Purific. 6, 646–654.\nImai, T., Globerman, H., Gertner, J.M., Kagawa, N., and Waterman, M.R. (1993) Expression and Purification of Functional Human 17 Alpha-Hydroxylase\u002F17,20-lyase (P450c17) in Escherichia coli. Use of This System for Study of a Novel Form of Combined 17 Alpha-Hydroxylase\u002F17,20-Lyase Deficiency, J. Biol. Chem. 26, 19681–19689.\nVick, B.A. (1991) A Spectrophotometric Assay for Hydroperoxide Lyase, Lipids 26, 315–320.\nBrash, A.R., and Song, W.-C. (1996) Detection, Assay, and Isolation of Allene Oxide Synthase, Methods Enzymol. 272, 250–259.\nSong, W.-C., Funk, C.D., and Brash, A.R. (1993) Molecular Cloning of an Allene Oxide Synthase: A Cytochrome P450 Specialized for the Metabolism of Fatty Acid Hydroperoxides, Proc. Natl. Acad. Sci. USA 90, 8519–8523.\nPan, Z.Q., Durst, F., Werk-Reichhart, D., Gardner, H.W., Camara, B., Cornish, K., and Backhaus, R.A. (1995) The Major Protein of Guayule Rubber Particles Is a Cytochrome P450, J. Biol. Chem. 270, 8487–8494.\nZimmerman, D.C., and Coudron, C.A. (1979) Identification of Traumatin, a Wound Hormone, as 12-Oxo-trans-10-dodecenoic Acid, Plant Physiol. 63, 536–541.\nHatanaka, A., Kajiwara, T., Sekiya, J., and Fukumoto, T. (1982) Oxygen-Isotope Effect in Enzymatic Cleavage Reaction of 13-l-Hydroperoxyliholeic acid to Hexanal and 11-Formyl-cis-9-undecenoic Acid, Z. Naturforsch. 37C, 752–757.\nBrash, A.R., and Song, W.-C. (1995) Structure-Function Features of Flaxseed Allene Oxide Synthase, J. Lipid Mediat. Cell Signal. 12, 275–282.\nLaudert, D., Pfannschmidt, U., Lottspeich F., Hollander Czytko, H., and Weiler, E.W. (1996) Cloning, Molecular and Functional Characterization of Arabidopsis thaliana Allene Oxide Synthase (CYP74), the First Enzyme of the Octadecanoid Pathway to Jasmonates, Plant Mol. Biol. 31, 323–335.\nGuo, Z., Gillam, E.M.J., Ohmori, S., Tukey, R.H., and Guengerich, F.P. (1994) Expression of Modified Human Cytochrome P450 1A1 in Escherichia coli: Effects of 5′ Substitution, Stabilization, Purification, Spectral Characterization, and Catalytic Properties, Arch. Biochem. Biophys. 312, 436–446.\nGillam, E.M.J., Guo, Z., Ueng, Y.-F., Yamasaki, H., Cock, I., Reilly, P.E.B., Hooper, W.D., and Guengerich, F.P. (1995) Expression of Cytochrome P450 3A5 in Escherichia coli: Effects of 5′ Modification, Purification, Spectral Characterization, Reconstitution Conditions, and Catalytic Activities, Arch. Biochem. Biophys. 317, 374–384.\nCapdevila, J.H., Wei, S., Helvig, C., Falck, J.R., Belosludtsev, Y., Truan, G., Graham-Lorence, S.E., and Peterson, J.A. (1996) The Highly Stereoselective Oxidation of Polyunsaturated Fatty Acids by Cytochrome P450BM-3, J. Biol. Chem. 271, 22663–22671.\nNoordermeer, M.A., van Dijken, A.J.H., Smeekens, S.C.M., Veldink, G.A., and Vliegenthart, J.F.G. (2000) Characterization of Three Cloned and Expressed 13-Hydroperoxide Lyase Isoenzymes from Alfalfa with Unusual N-Terminal Sequences and Different Enzyme Kinetics, Eur. J. 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muscle phospholipid fatty acid (PLFA) composition is associated with insulin sensitivity in animal models and in man. However, it is not clear whether changes in insulin sensitivity cause a change in PLFA composition or vice versa. The present studies have examined the effects of agents known to increase or decrease insulin sensitivity on PLFA composition of the major phospholipids, phosphatidylcholine (PC) and phosphatidylethanolamine (PE), in soleus and extensor digitorum longus muscle. Four groups of Sprague-Dawley rats— control, 0.2% troglitazone (Tgz), 60% fructose fed, and fructose + Tgz—were treated for 3 wk. Fructose feeding was associated with a decrease in muscle membrane polyunsaturated fatty acids (PUFA) and n-3 fatty acids in both PC and PE. Administration of Igz alone resulted in an increase in liver (3.75±0.93 to 6.93±1.00 μmol\u002Fmin\u002Fmg tissue, P\u003C0.05) and soleus muscle (0.34±0.03 to 0.67±0.09 μmol\u002Fmin\u002Fmg, P\u003C0.01) elongase activity, which would be expected to increase membrane PUFA. However, Tgz decreased PLFA associated with greater insulin sensitivity (e.g., PUFA and n-3 fatty acids) and increased PLFA associated with decreased insulin sensitivity (16∶0 and n-6 fatty acids) in both PC and PE. Co-administration of fructose and Tgz did not reverse the decrease in PUFA observed with fructose alone. We conclude that the improvement in insulin sensitivity reported with Tgz is associated with an apparently paradoxical effect to decrease PUFA and n-3 PLFA composition in rat skeletal muscle. These studies suggest that Tgz-mediated increases in insulin sensitivity do not result in improved PLFA composition.",{"EN":1607},"Effects of fructose and troglitazone on phospholipid fatty acid composition in rat skeletal muscle",{"VOID":270},{"VOID":1610},"Clore, J.N., Li, J., Gill, R., Gupta, S., Spencer, R., Azzam, A., Zuelzer, W., Rizzo, W.B., and Blackard, W.G. (1998) Skeletal Muscle Phosphatidylcholine Fatty Acids and Insulin Sensitivity in Normal Humans, Am. J. Physiol. 275, E665-E670.\nKriketos, A.D., Pan, D.A., Lillioja, S., Cooney, G.J., Baur, L.A., Milner, M.R., Sutton, J.R., Jenkins, A.B., Bogardus, C., and Storlien, L.H. (1996) Interrelationships Between Muscle Morphology, Insulin Action, and Adiposity, Am. J. Physiol. 270, R1332-R1339.\nPan, D.A., Hulbert, A.J., and Storlien, L.H. (1994) Dietary Fats, Membrane Phospholipids and Obesity, J. Nutr. 124, 1555–1565.\nVessby, B., Tengblad, S., and Lithell, H. (1994) Insulin Sensitivity Is Related to the Fatty Acid Composition of Serum Lipids and Skeletal Muscle Phospholipids in 70-year-old Men, Diabetologia 37, 1044–1050.\nKriketos, A.D., Pan, D.A., Sutton, J.R., Hoh, J.F., Baur, L.A., Cooney, G.J., Jenkins, A.B., and Storlien, L.H. (1995) Relationships Between Muscle Membrane Lipids, Fiber Type, and Enzyme Activities in Sedentary and Exercised Rats, Am. J. Physiol. 269, R1154-R1162.\nTakagi, A. (1971) Lipid Composition of Sarcoplasmic Reticulum of Human Skeletal Muscle, Biochim. Biophys. Acta 248, 12–20.\nBlackard, W.G., Li, J., Clore, J.N., and Rizzo, W.B. (1997) Phospholipid Fatty Acid Composition in Type I and Type II Rat Muscle, Lipids 32, 193–198.\nStorlien, L.H., Jenkins, A.B., Chisholm, D.J., Pascoe, W.S., Khouri, S., and Kraegen, E.W. (1991) Influence of Dietary Fat Composition on Development of Insulin Resistance in Rats. Relationship to Muscle Triglyceride and Omega-3 Fatty Acids in Muscle Phospholipid, Diabetes 40, 280–289.\nClandinin, M.T., Cheema, S., Field, C.J., and Baracos, V.E. (1993) Dietary Lipids Influence Insulin Action, Ann. NY Acad. Sci. 683, 151–163.\nLiu, S., Baracos, V.E., Quinney, H.A., and Clandinin, M.T. (1994) Dietary Omega-3 and Polyunsaturated Fatty Acids Modify Fatty Acyl Composition and Insulin Binding in Skeletal-Muscle Sarcolemma, Biochem. J. 299, 831–837.\nAndersson, A., Sjodin, A., Olsson, R., and Vessby, B. (1998) Effects of Physical Exercise on Phospholipid Fatty Acid Composition in Skeletal Muscle, Am. J. Physiol. 274, E432-E438.\nClore, J.N., Harris, P.A., Li, J., Azzam, A., Gill, R., Zuelzer, W., Rizzo, W.B., and Blackard, W.G. (2000) Changes in Phosphatidylcholine Fatty Acid Composition Are Associated with Altered Skeletal Muscle Insulin Responsiveness in Normal Man, Metabolism 49, 232–238.\nTobey, T.A., Mondon, C.E., Zavaroni, I., and Reaven, G.M. (1982) Mechanism of Insulin Resistance in Fructose-Fed Rats, Metabolism 31, 608–612.\nCiaraldi, T.P., Gilmore, A., Olefsky, J.M., Goldberg, M., and Heidenreich, K.A. (1990) In vitro Studies on the Action of CS-045, a New Antidiabetic Agent, Metabolism 39, 1056–1062.\nLee, M.K., Miles, P.D., Khoursheed, M., Gao, K.M., Moossa, A.R., and Olefsky, J.M. (1994) Metabolic Effects of Troglitazone on Fructose-Induced Insulin Resistance in the Rat, Diabetes 43, 1435–1439.\nBorkman, M., Storlien, L.H., Pan, D.A., Jenkins, A.B., Chisholm, D.J., and Campbell, L.V. (1993) The Relation Between Insulin Sensitivity and the Fatty-Acid Composition of Skeletal-Muscle Phospholipids, N. Engl. J. Med. 328, 238–244.\nFolch, J., Lees, M., and Sloane Stanley, G.H. (1957) A Simple Method for the Isolation and Purification of Total Lipids from Animal Tissues, J. Biol. Chem. 226, 497–509.\nAlegret, M., Cerqueda, E., Ferrando, R., Vazquez, M., Sanchez, R.M., Adzet, T., Merlos, M., and Laguna, J.C. (1995) Selective Modification of Rat Hepatic Microsomal Fatty Acid Chain Elongation and Desaturation by Fibrates: Relationship with Peroxisome Proliferation, Br. J. Pharmacol. 114 1351–1358.\nMorgan, C.R., and Lazarow, A. (1963) Immunoassay of Insulin: Two Antibody System: Plasma Insulin Levels of Normal, Subdiabetic and Diabetic Rats, Diabetes 12, 115–126.\nMcGarry, J.D., Stark, M.J., and Foster, D.W. (1978) Hepatic Malonyl-CoA Levels of Fed, Fasted and Diabetic Rats as Measured Using a Simple Radioisotopic Assay, J. Biol. Chem. 253, 8291–8293.\nLinn, T.C. (1981) Purification and Crystallization of Rat Liver Fatty Acid Synthetase, Arch. Biochem. Biophys. 209, 613–619.\nAyre, K.J., and Hulbert, A.J. (1996) Dietary Fatty Acid Profile Influences the Composition of Skeletal Muscle Phospholipids in Rats, J. Nutr. 126, 653–662.\nKraegen, E.W., Clark, P.W., Jenkins, A.B., Daley, E.A., Chisholm, D.J., and Storlien, L.H. (1991) Development of Muscle Insulin Resistance After Liver Insulin Resistance in High-Fat-Fed Rats, Diabetes 40, 1397–1403.\nPan, D.A., Lillioja, S., Milner, M.R., Kriketos, A.D., Baur, L.A., Bogardus, C., and Storlien, L.H. (1995) Skeletal Muscle Membrane Lipid Composition Is Related to Adiposity and Insulin Action, J. Clin. Invest. 96, 2802–2808.\nThorburn, A.W., Storlien, L.H., Jenkins, A.B., Khouri, S., and Kraegen, E.W. (1989) Fructose-Induced in vivo Insulin Resistance and Elevated Plasma Triglyceride Levels in Rats, Am. J. Clin. Nutr. 49, 1155–1163.\nStorlien, L.H., Oakes, N.D., Pan, D.A., Kusunoki, M., and Jenkins, A.B. (1993) Syndromes of Insulin Resistance in the Rat. Inducement by Diet and Amelioration with Benfluorex, Diabetes 42, 457–462.\nSreenan, S., Keck, S., Fuller, T., Cockburn, B., and Burant, C.F. (1999) Effects of Troglitazone on Substrate Storage and Utilization in Insulin-Resistant Rats, Am J. Physiol. 276, E1119-E1129.\nHiga, M., Zhou, Y.T., Ravazzola, M., Baetens, D., Orci, L., and Unger, R.H. (1999) Troglitazone Prevents Mitochondrial Alterations Beta Cell Destruction, and Diabetes in Obese Prediabetic Rats, Proc. Natl. Acad. Sci. USA 96, 11513–11518.\nOakes, N.D., Kennedy, C.J., Jenkins, A.B., Laybutt, D.R., Chisholm, D.J., and Kraegen, E.W. (1994) A New Antidiabetic Agent, BRL 49653, Reduces Lipid Availability and Improves Insulin Action and Glucoregulation in the Rat, Diabetes 43, 1203–1210.\nKraegen, E.W., James, D.E., Jenkins, A.B., Chisholm, D.J., and Storlien, L.H. (1989) A Potent in vivo Effect of Ciglitazone on Muscle Insulin Resistance Induced by High Fat Feeding of Rats, Metabolism 38, 1089–1093.\nPrasad, M.R., Nagi, M.N., Ghesquier, D., Cook, L., and Cinti, D.L. (1986) Evidence for Multiple Condensing Enzymes in Rat Hepatic Microsomes Catalyzing the Condensation of Saturated, Monounsaturated, and Polyunsaturated Acyl Coenzyme A, J. Biol. 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of phospholipase D-like (PLD) activity in the intestinal mitochondria was identified using endogenous phospholipids as substrate. The enzyme had a pH optimum of 6.5, did not show trans-phosphatidylation activity in the presence of ethanol or butanol, and the product formed was phosphatidic acid (PA). This was confirmed by separation of reaction products by high-performance liquid chromatography and analysis of composition of the PA formed which gave phosphate\u002Ffatty acid ratio of 1∶2. PLD-like activity was further confirmed by the formation of ethanolamine and choline as products of enzyme action. This activity was stimulated by various metal ions; when stimulated by Mg2+ and Ba2+, it hydrolyzed both phosphatidylcholine and phosphatidylethanolamine, and when stimulated by Ca2+, it preferentially hydrolyzed phosphatidylethanolamine. There was no requirement for sodium oleate for the PLD-like activity in mitochondria. These results suggest that intestinal mitochondria have an active PLD-like enzyme which differs in certain properties from phospholipase D from other tissues.",{"EN":1724},"Metal ion stimulation of phospholipase D-like activity of isolated rat intestinal mitochondria",{"VOID":1726},"[\"8639236104804081558\"]",{"VOID":1728},"Shukla, S.D., and Halenda, S.P. (1991) Life Sciences 48, 851–866.\nLiscovitch, M., Ben-Ar, P., Damin, M., Faimar, G., Eldar, H., and Livnch, E. (1993) J. Lipid Mediators 8, 177–182.\nBalboa, M.A., Firestein, B.L., Godon, C., Bell, K.S., and Insell, P.A. (1994) J. Biol. Chem. 269, 10511–10516.\nConricode, K.M., Smith, J.L., Burn, G.J., and Exton, J.H. (1994) FEBS Lett. 342, 149–153.\nGuillemain, I., and Rossignol, B. (1994) Am. J. Physiol. 266, C692-C699.\nGustavsson, L., Mehren, G., Marquez, M.E., Benstant, C., Rubin, R., and Hoek, J. (1994) J. Biol. Chem. 269, 849–859.\nNatarajan, V., and Iwamoto, G.K. (1994) Biochim. Biophys. Acta. 1213, 14–20.\nKiss, Z., and Anderson, W.H. (1994) Arch. Biochem. Biophys. 311, 430–436.\nNatarajan, V., Taher, M.M., Roehm, B., Parinandi, N.L., Schmid, H.H.O., Kiss, Z., and Garcia, J.G.N. (1993) J. Biol. Chem. 268, 930–937.\nKanfer, J.N., and McCartney, D. (1994) FEBS Lett. 337, 251–254.\nChalifa, V., Mohn, H., and Liscovitch, M. (1990) J. Biol. Chem. 265, 17512–17519.\nGunter, T.E., Gunter, K.K., Sheu, S., and Gavin, C.E. (1994) Am. J. Physiol. 267, C313-C339.\nRichter, C. (1993) FEBS Lett. 325, 104–107.\nRichter, C., and Kass, G.E.N. (1991) Chem. Biol. Interactions 77, 1–23.\nTyson, C.A., Zarde, H.V., and Greh, D.E. (1976) J. Biol. Chem. 251, 1326–1332.\nDutney, J.W., Weiss, S.J., Van De Walle, C.M., and Haddas, R.A. (1980) Nature 284, 345–347.\nKobayshi, M., and Kanfer, J.N. (1987) J. Neurochem. 48, 1597–1603.\nRakhimov, M.M., Gorbataia, O.N., and Almatou, K.T. (1989) Biokhimica 54, 1066–1074.\nChalifour, R.J., and Kanfer, J.N. (1980) Biochem. Biophys. Res. Commun 96, 742–747.\nChristie, W.W. (1982) in Lipid Analysis, 2nd edn., Pergamon Press, Oxford, pp. 165–166.\nMasola, B., and Evered, D.F. (1984) Biochem. J. 218, 411–447.\nLowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951) J. Biol. Chem. 193, 265–275.\nBligh, E.G., and Dyer, W.J. (1959) Can. J. Biochem. Physiol. 37, 911–917.\nCohen, P., and Derksen, A. (1969) Br. J. Hematol. 17, 359–371.\nBartlett, G.R. (1959) J. Biol. Chem. 234, 466–468.\nGeny, B., and Cockcroft, S. (1992) Biochem. J. 284, 531–538.\nMizunuma, M., Tanaka, S., Kudo, R., and Kano, H. (1993) Biochim. Biophys. Acta 1168, 213–219.\nBursten, S.L., and Harris, W.E. (1991) Biochemistry 30, 6195–6203.\nVance, D.E., Pelech, S.D., and Choy, P. (1981) Methods Enzymol. 71, 576–581.\nZlatkis, A., Zak, B., and boyle, A.J.J. (1953) J. Lab. Clin. Med. 41, 486–492.\nSnyder, F., and Stephens, N. (1959) Biochim. Biophys. Acta 34, 244–245.\nShipski, V.P., Peterson, R.F., and Barclay, M. (1964) Biochem. J. 90, 374–378.\nSchmid, P.C., Pfeiffer, D.R., and Schmid, H.H.O. (1981) J. Lipid Res. 22, 882–886.\nTaki, T., and Kanfer, J.N. (1979) J. Biol. Chem. 254, 9761–9765.\nInamori, K., Sagawa, N., Hasegawa, M., Itoh, H., Veda, H., Kobayashi, F., Ihara, Y., and Mori, T. (1993) Biochem. Biophys. Res. Commun. 191, 1270–1277.\nNishida, A., Shimizu, M., Kanabo, Y., Nozawa, Y., and Yamowaki, S. (1992) Brain Res. 595, 12–16.\nChattopadhyay, J., Natarajan, V., and Schmid, H.D. (1991) J. Neurochem. 57, 1429–1436.\nRider, M.H., and Baquet, A. (1988) Biochem. J. 255, 923–928.\nKanoh, H., and Akesson, B. (1978) Eur. J. Biochem. 85, 225–232.\nNalini, S., and Balasubramanian, K.A. (1991) Chem. Biol. Interactions 80, 135–144.\nAhamed Ibrahim, S., and Balasubramanian, K.A. (1993) Ind. J. Biochem. Biophys. 30, 285–288.\nHermes-Lima, M., Castillo, R.F., Valle, V.G.R., Bechare, E.J.H., and Vercesi, A.E. (1992) Biochim. Biophys. 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