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Original Articles

Effects of Dietary Oyster Extract on Lipid Metabolism, Blood Pressure, and Blood Glucose in SD Rats, Hypertensive Rats, and Diabetic Rats

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Pages 462-470 | Received 23 Aug 2005, Accepted 01 Nov 2005, Published online: 22 May 2014

  • 1) Arai, S., Osawa, T., Ohigashi, H., Yoshikawa, M., Kaminogawa, S., Watanabe, M., Ogawa, T., Okubo, K., Watanabe, S., Nishino, H., Shinohara, K., Esashi, T., and Hirahara, T., A mainstay of functional food science in Japan—history, present status, and future outlook. Biosci. Biotechnol. Biochem., 65, 1–13 (2001).
  • 2) Dziuba, J., Minkiewicz, P., Nalecz, D., and Iwaniak, A., Database of biologically active peptide sequences. Nahrung, 43, 190–195 (1999).
  • 3) Carroll, K. K., and Hamilton, R. M. G., Effects of dietary protein and carbohydrate on plasma cholesterol in relation to atherosclerosis. J. Food Sci., 40, 18–23 (1975).
  • 4) Nagata, Y., Tanaka, K., and Sugano, M., Further studies on the hypocholesterolaemic effect of soya-bean protein in rats. Br. J. Nutr., 45, 233–241 (1981).
  • 5) Martin, D. S., Breitkopf, N. P., Eyster, K. M., and Williams, J. L., Dietary soy exerts an antihypertensive effect in spontaneously hypertensive female rats. Am. J. Physiol. Regul. Integr. Comp. Physiol., 281, R553–560 (2000).
  • 6) Wu, J., and Ding, X., Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats. J. Agric. Food Chem., 49, 501–506 (2001).
  • 7) Kops, S. K., West, A. B., Leach, J., and Miller, R. H., Partially purified soy hydrolysates retard proliferation and inhibit bacterial translocation in cultured C2Bbe cells. J. Nutr., 127, 1744–1751 (1997).
  • 8) Niiho, Y., Yamazaki, T., Hosono, T., Ishizaki, M., and Kurashige, T., Pharmacological studies on small peptide fraction derived from soybean: the effects of small peptide fraction derived from soybean on fatigue, obesity and glycemia in mice. Yakugaku Zasshi, 113, 334–342 (1993).
  • 9) FitzGerald, R. J., Murray, B. A., and Walsh, D. J., Hypotensive peptides from milk proteins. J. Nutr., 34, 980S–988S (2004).
  • 10) Crombie, I. K., McLoone, P., Smith, W. C., Thompson, M., and Pedoe, J. T., International differences in coronary heart disease mortality and consumption of fish and other food-stuffs. Eur. Heart J., 8, 560–563 (1987).
  • 11) Daviglus, M. L., Stamlaer, J., Orencia, A. J., Dyer, A. R., Liu, K., Greenland, P., Walsh, M. K., Morris, D., and Shekelle, R. B., Fish consumption and the 30-year risk of fatal myocardial infarction. N. Engl. J. Med., 336, 1046–1053 (1997).
  • 12) Harris, W. S., Fish oils and plasma lipid and lipoprotein metabolism in humans: a critical review. J. Lipid Res., 30, 785–807 (1989).
  • 13) Harris, W. S., N-3 fatty acids and lipoproteins: comparison of results from human and animal studies. Lipids, 31, 243–252 (1996).
  • 14) Vanschoonbeek, K., de Maat, M. P., and Heemskerk, J. W., Fish oil consumption and reduction of arterial disease. J. Nutr., 133, 657–660 (2003).
  • 15) Tanaka, K., Fukuda, M., Ikeda, I., and Sugano, M., Effects of dietary short-necked clam, Tapes japonica, on serum and liver cholesterol levels in mice. J. Nutr. Sci. Vitaminol., 40, 325–333 (1994).
  • 16) Tanaka, K., Sakai, T., Ikeda, I., Imaizumi, K., and Sugano, M., Effects of dietary shrimp, squid and octopus on serum and liver lipid levels in mice. Biosci. Biotechnol. Biochem., 62, 1369–1375 (1998).
  • 17) Tanaka, K., Ikeda, I., Yoshida, H., and Imaizumi, K., Effects of dietary defatted squid on cholesterol metabolism and hepatic lipogenesis in rats. Lipids, 36, 461–466 (2001).
  • 18) Bergeron, N., and Jacques, H., Influence of fish protein as compared to casein and soy protein on serum and liver lipids, and serum lipoprotein cholesterol levels. Atherosclerosis, 78, 113–121 (1989).
  • 19) Zhang, X., and Beynen, A. C., Influence of dietary fish proteins on plasma and liver cholesterol concentrations in rats. Br. J. Nutr., 69, 767–777 (1993).
  • 20) Ait-Yahia, D., Mahani, S., Savelli, J.-L., Prost, J., Bouchenak, M., and Belleville, J., Dietary fish protein lowers blood pressure and alters tissue polyunsaturated fatty acid composition in spontaneously hypertensive rats. Nutrition, 19, 342–346 (2003).
  • 21) Mollsten, A. V., Dahlquist, G. G., Stattin, E. L., and Rudberg, S., Higher intakes of fish protein are related to a lower risk of microalbuminuria in young Swedish type 1 diabetic patients. Diabetes Care, 24, 805–810 (2001).
  • 22) Boukortt, F. O., Grard, A., Prost, J. L., Ait-Yahia, D., Bouchenak, M., and Belleville, J., Fish protein improves the total antioxidant status of streptozotocin-induced diabetes in spontaneously hypertensive rat. Med. Sci. Monit., 26, BR397–404 (2004).
  • 23) Wergedahl, H., Liaset, B., Gudbrandsen, O. A., Lied, E., Espe, M., Muna, Z., Mork, S., and Berge, R. K., Fish protein hydrolysate reduces plasma total cholesterol, increases the proportion of HDL cholesterol, and lowers acyl-CoA:cholesterol acyltransferase activity in liver of Zucker rats. J. Nutr., 134, 1320–1327 (2004).
  • 24) Matsui, T., Matsufuji, H., Seki, E., Osajima, K., Nakashima, M., and Osajima, Y., Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolysates derived from sardine muscle. Biosci. Biotechnol. Biochem., 57, 922–925 (1993).
  • 25) Li, G. H., Le, G. W., Shi, Y. H., and Shrestha, S., Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr. Res., 24, 469–486 (2004).
  • 26) Tanaka, K., Ikeda, I., Kase, A., Koba, K., Nishizono, S., Aoyama, T., and Imaizumi, K., Effects of feeding oyster, Crassostrea gigas, on serum and liver lipid levels in rats. J. Nutr. Sci. Vitaminol., 49, 100–106 (2003).
  • 27) Shibata, Y., Hattori, M., Takeuchi, F., Otsuka, H., Tsubouchi, R., Ugata, M., Shiraishi, S., Ohta, T., Sugino, M., Sotokawa, Y., Takahashi, R., Kotake, Y., and Kotake, Y., Influences of feeding oysters on the metabolism of serotonin in alloxan-diabetic rats. Progress in Tryptophan and Serotonin Research, 87, 87–90 (1987).
  • 28) Folch, J., Lees, M., and Sloane-Stanley, G. H., A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem., 226, 497–506 (1957).
  • 29) Sperry, W. M., and Webb, M. A., A revision of the Shoenheimer-Sperry method for cholesterol determination. J. Biol. Chem., 187, 97–106 (1950).
  • 30) Fletcher, M. J., A colorimetric method for estimating serum triglycerides. Clin. Chim. Acta, 22, 393–397 (1968).
  • 31) Rouser, G., Siakotos, A. N., and Fleischer, S., Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots. Lipids, 1, 85–86 (1966).
  • 32) Grundy, S. M., Ahrens, E. H., and Miettinen, T. A., A quantitative isolation and gas-liquid chromatographic analysis of total dietary and fecal neutral steroids. J. Lipid Res., 6, 411–421 (1965).
  • 33) Kuriyama, K., Ban, Y., and Nakashima, T., Simultaneous determination of biliary bile acids in rat: electron impact and ammonia chemical ionization mass spectrometric analysis of bile acids. Steroids, 34, 717–728 (1979).
  • 34) Kelly, D. S., Nelson, G. J., and Hunt, J. E., Effect of prior nutritional status on the activity of lipogenic enzymes in primary monolayer cultures of rat hepatocytes. Biochem. J., 235, 87–90 (1986).
  • 35) Kelly, D. S., and Kletzien, R. F., Ethanol modulation of the hormonal and nutritional regulation of glucose-6-phosphate dehydrogenase activity in primary cultures of rat hepatocytes. Biochem. J., 217, 543–549 (1984).
  • 36) Ochoa, S., Malic enzyme. In “Methods in Enzymology” Vol. 1, eds. Colowick, S. P., and Kaplan, N. O., Academic Press, New York, pp. 739–753 (1955).
  • 37) Walton, P. A., and Possmayer, F., Mg2+-dependent phosphatidate phosphohydrolase of rat lung: development of an assay employing a defined chemical substrate which reflects the phosphohydrolase activity measured using membrane-bound substrate. Anal. Biochem., 151, 479–486 (1985).
  • 38) Markwell, M. A. K., McGroarty, E. J., Bieber, L. L., and Tolbert, N. E., The subcellular distribution of carnitine acyltransferases in mammalian liver and kidney. J. Biol. Chem., 248, 3426–3432 (1973).
  • 39) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with Folin phenol reagent. J. Biol. Chem., 193, 265–275 (1951).
  • 40) Berthelin, C., Kellner, K., and Mathieu, M., Storage metabolism in the Pacific oyster (Crassostrea gigas) in relation to summer mortalities and reproductive cycle (west coast of France). Comp. Biochem. Physiol. B Biochem. Mol. Biol., 125, 359–369 (2000).
  • 41) Pennarun, A. L., Prost, C., Haure, J., and Demaimay, M., Comparison of two microalgal diets. 1. Influence on the biochemical and fatty acid compositions of raw oysters (Crassostrea gigas). J. Agric. Food Chem., 51, 2006–2010 (2003).
  • 42) Nagaoka, S., Awano, T., Nagata, N., Masaoka, M., Hori, G., and Hashimoto, K., Serum cholesterol reduction and cholesterol absorption inhibition in CaCo-2 cells by a soyprotein peptic hydrolyzate. Biosci. Biotechnol. Biochem., 61, 354–356 (1997).
  • 43) Iwami, K., Sakakibara, K., and Ibuki, F., Involvement of post-digestion ‘hydrophobic’ peptides in plasma cholesterol-lowering effect of dietary plant proteins. Agric. Biol. Chem., 50, 1217–1222 (1986).
  • 44) Raicht, R. F., Cohen, B. I., Shefer, S., and Mosbach, E. H., Sterol balance studies in the rat: effects of dietary cholesterol and beta-sitosterol on sterol balance and rate-limiting enzymes of sterol metabolism. Biochim. Biophys. Acta, 388, 374–384 (1975).
  • 45) Madani, S., Lopez, S., Blond, J. P., Prost, J., and Belleville, J., Highly purified soybean protein is not hypocholesterolemic in rats but stimulates cholesterol synthesis and excretion and reduces polyunsaturated fatty acid biosynthesis. J. Nutr., 128, 1084–1091 (1998).
  • 46) Maeno, M., Yamamoto, N., and Takano, T., Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790. J. Dairy Sci., 79, 1316–1321 (1996).
  • 47) Yokoyama, H., Chiba, H., and Yoshikawa, M., Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotechnol. Biochem., 56, 1541–1545 (1992).
  • 48) Nakashima, Y., Arihara, K., Mio, H., and Itoh, M., Antihypertensive activities of peptides derived from porcine skeletal muscle myosin in spontaneously hypertensive rats. J. Food Sci., 67, 434–437 (2002).
  • 49) Hoorfar, J., Scott, F. W., and Cloutier, H. E., Dietary plant materials and development of diabetes in the BB rat. J. Nutr., 121, 908–916 (1991).
  • 50) Visser, J., Brugman, S., Klatter, F., Vis, L., Groen, H., Strubbe, J., and Rozing, J., Short-term dietary adjustment with a hydrolyzed casein-based diet postpones diabetes development in the diabetes-prone BB rat. Metabolism, 52, 333–337 (2003).

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