Differing effect of protein isolates from different cultivars of blue lupin on plasma lipoproteins of hypercholesterolemic rats

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 12, 2008, Pages 3114-3121

  Bettzieche, Anja ^a   Brandsch, Corinna ^a   Schmidt, Manja ^a   Weiße, Kristin ^a   Eder, Klaus ^a   Stangl, Gabriele I ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Hepatic gene expression; Lupin protein; Plasma lipoprotein; Rat

Indexed keywords

BIOACTIVITY; CASEIN; CHOLESTEROL; GENE EXPRESSION; GENES; LIPIDS; PLASMAS; RATS;

BENEFICIAL EFFECTS; CHOLESTEROL SYNTHESES; DENSITY LIPOPROTEINS; HEPATIC GENE EXPRESSION; LIPID SYNTHESES; LUPIN PROTEIN; PLASMA LIPIDS; PLASMA LIPOPROTEIN; PROTEIN ISOLATES; TOTAL PROTEINS; WHITE LUPIN;

PLASMA DIAGNOSTICS;

BILE ACID; CHOLESTEROL; LIPOPROTEIN; MESSENGER RNA; TRIACYLGLYCEROL; VEGETABLE PROTEIN;

ANIMAL; ARTICLE; BLOOD; BODY WEIGHT; CHEMISTRY; DRUG EFFECT; GENE EXPRESSION REGULATION; GENETICS; HYPERCHOLESTEROLEMIA; ISOLATION AND PURIFICATION; LIVER; LUPIN; MALE; METABOLISM; ORGAN SIZE; PATHOLOGY; RAT; SPRAGUE DAWLEY RAT;

ANIMALS; BILE ACIDS AND SALTS; BODY WEIGHT; CHOLESTEROL; GENE EXPRESSION REGULATION; HYPERCHOLESTEROLEMIA; LIPOPROTEINS; LIVER; LUPINUS; MALE; ORGAN SIZE; PLANT PROTEINS; RATS; RATS, SPRAGUE-DAWLEY; RNA, MESSENGER; TRIGLYCERIDES;

RATTUS;

EID: 58149098877     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80221     Document Type: Article

References (41)

1. Anderson, J. W., Johnstone, B. M., and Cook-Newell, M. E., Meta-analysis of the effects of soybean protein intake on serum lipids. N. Engl. J. Med., 333, 276-282 (1995).
2. Sirtori, C. R., Lovati, M. R., Manzoni, C., Gianazza, E., Bondioli, A., Staels, B., and Auwerx, J., Reduction of serum cholesterol by soybean proteins: clinical experience and potential molecular mechanisms. Nutr. Metab. Cardiovasc. Dis., 8, 334-340 (1998).
3. Koba, K., Liu, J. W., Bobik Jr., E., Mills, D. E., Sugano, M., and Huang, Y. S., Effect of phytate in soy protein on the serum and liver cholesterol levels and fatty acid profile in rats. Biosci. Biotechnol. Biochem., 67, 15-22 (2003).
4. Sirtori, C. R., Lovati, M. R., Manzoni, C., Castiglioni, S., Duranti, M., Magni, C., Moranti, S., D'Agostina, A., and Arnoldi, A., Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells. J. Nutr., 134, 18-23 (2004).
5. Shukla, A., Brandsch, C., Bettzieche, A., Hirche, F., Stangl, G. I., and Eder, K., Isoflavone-poor soy protein alters the lipid metabolism of rats by SREBP-mediated down-regulation of hepatic genes. J. Nutr. Biochem., 18, 313-321 (2007).
6. Bettzieche, A., Brandsch, C., Weiße, K., Hirche, F., Eder, K., and Stangl, G. I., Lupin protein influences the expression of hepatic gene involved in fatty acid synthesis and triacylglycerol hydrolysis of adult rats. Br. J. Nutr., 99, 952-962 (2008).
7. Spielmann, J., Shukla, A., Brandsch, C., Hirche, F., Stangl, G. I., and Eder, K., Dietary lupin protein lowers triglyceride concentrations in liver and plasma in rats by reducing hepatic gene expression of sterol regulatory element-binding protein-1c. Ann. Nutr. Metab., 51, 387-392 (2007).
8. Petterson, D. S., Composition and food uses of lupins. In "Lupins as Crop Plants: Biology, Production, and Utilization," eds. Gladstones, J. S., Atkins, C. A., and Hamblin, J., CAB International, Wallingford, pp. 353-384 (1998).
9. Katagiri, Y., Ibrahim, R. K., and Tahara, S., HPLC analysis of white lupin isoflavonoids. Biosci. Biotechnol. Biochem., 64, 1118-1125 (2000).
10. Muzquiz, M., Pedrosa, M. M., Cuadrado, C., Ayet, G., Burbano, C., and Brenes, A., Variation of alkaloids, alkaloid esters, phytic acid, and phytase activity in germinated seed of Lupinus albus and L. luteus. In "Recent Advances of Research in Antinutritional Factors in Legume Seeds and Rape Seeds," eds. Jasman, A. J. M., Hill, G. D., Huisman, J., and van der Poel, A. F. B., Wageningen Press, Wageningen, pp. 387-390 (1998).
11. Martins, J. M., Riottot, M., de Abreu, M. C., Viegas-Crespo, A. M., Lança, M. J., Almeida, J. A., Freire, J. B., and Bento, O. P., Cholesterol-lowering effects of dietary blue lupin (Lupinus angustifolius L.) in intact and ileorectal anastomosed pigs. J. Lipid Res., 46, 1539-1547 (2005).
12. 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).
13. Yang, L., Kumagai, T., Kawamura, H., Watanabe, T., Kubota, M., Fujimura, S., Watanabe, R., and Kadowaki, M., Effects of rice proteins from two cultivars, Koshihikari and Shunyo, on cholesterol and triglyceride metabolism in growing and adult rats. Biosci. Biotechnol. Biochem., 71, 694-703 (2007).
14. Manzoni, C., Duranti, M., Eberini, I., Scharnag, H., März, W., Castiglioni, S., and Lovati, M. R., Subcellular localization of soybean 7S globulin in HepG2 cells and LDL receptor up-regulation by its alpha′ constituent subunit. J. Nutr., 133, 2149-2155 (2003).
15. Kohno, M., Hirotsuka, M., Kito, M., and Matsuzawa, Y., Decreases in serum triacylglycerol and visceral fat mediated by dietary soybean beta-conglycinin. J. Atheroscler. Thromb., 13, 247-255 (2006).
16. Brown, M. S., and Goldstein, J. L., The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell, 89, 331-340 (1997).
17. Vallett, S. M., Sanchez, H. B., Rosenfeld, J. M., and Osborne, T. F., A direct role of sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene. J. Biol. Chem., 271, 12247-12253 (1996).
18. Horton, J. D., Goldstein, J. L., and Brown, M. S., SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J. Clin. Invest., 109, 1125-1131 (2002).
19. Shimano, H., Yahagi, N., Amemiya-Kudo, M., Hastry, A. H., Osuga, J., Tamura, Y., Shionoiri, F., Iizuka, Y., Ohashi, K., Harada, K., Gotoda, T., Ishibashi, S., and Yamada, N., Sterol regulatory element-binding protein-1 as a key transcription factor for nutritional induction of lipogenic enzyme genes. J. Biol. Chem., 274, 35832-35839 (1999).
20. Santamarina-Fojo, S., Gonalez-Navarro, H., Freeman, L., Wagner, E., and Nong, Z., Hepatic lipase, lipoprotein metabolism, and atherogenesis. Arterioscler. Thromb. Vasc. Biol., 24, 1750-1754 (2004).
21. Merkel, A., and Heeren, J., Give me A5 for lipoprotein hydrolysis! J. Clin. Invest., 115, 2694-2696 (2005).
22. Reeves, P. G., Nielsen, F. H., and Fahey Jr., G. C., AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc Writing Committee on the reformulation of the AIN-76A rodent diet. J. Nutr., 123, 1939-1951 (1993).
23. Wäsche, A., Müller, K., and Knauf, U., New processing of lupin protein isolates and functional properties. Nahrung, 45, 393-395 (2001).
24. Naumann, C., and Bassler, R., "Methodenbuch Band III. Die chemische Untersuchung von Futtermitteln," VDLUFA-Verlag, Darmstadt (1993).
25. Sung, J. H., Choi, S. J., Lee, S. W., Park, K. H., and Moon, T. W., Isoflavones found in Korean soybean paste as 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors. Biosci. Biotechnol. Biochem., 68, 1051-1058 (2004).
26. Bassler, R., and Buchholz, H., "Methodenbuch Band III. Die chemische Untersuchung von Futtermitteln," VDLUFA-Verlag, Darmstadt (1993).
27. Schuster, R., Determination of amino acids in biological, pharmaceutical, plant and food samples by automated precolumn derivatization and high-performance liquid chromatography. J. Chromatogr., 431, 271-284 (1988).
28. Fontaine, J., Bech-Andersen, S., Bütikofer, U., and De Froidmont-Görtz, I., Determination of tryptophan in feed by HPLC - development of an optimal hydrolysis and extraction procedure by the EU Commission DG XII in three international collaborative studies. Agribiol. Res., 51, 97-108 (1998).
29. Eder, K., Peganova, S., and Kluge, H., Studies on the tryptophan requirement of piglets. Arch. Tierernahr., 55, 281-297 (2001).
30. Hara, A., and Radin, N. S., Lipid extraction of tissues with a low toxicity solvent. Anal. Biochem., 90, 420-426 (1978).
31. De Hoff, J. L., Davidson, J. H., and Kritchevsky, D., An enzymatic assay for determining free and total cholesterol in tissues. Clin. Chem., 24, 433-435 (1978).
32. Shimano, H., Sterol regulatory element-binding proteins (SREBPs): transcriptional regulators of lipid synthetic genes. Prog. Lipid Res., 40, 439-452 (2001).
33. Hasty, A. H., Shimano, H., Yahagi, N., Ameniya-Kudo, M., Perrey, S., Yoshikawa, T., Osuga, J., Okazaki, H., Tamura, Y., Iizuka, Y., Shionoiri, F., Ohashi, K., Harada, K., Gotoda, T., Nagai, R., Ishibashi, S., and Yamada, N., Sterol regulatory element-binding protein-1 is regulated by glucose at the transcription level. J. Biol. Chem., 275, 31069-31077 (2000).
34. Gómez-Pérez, F. J., Bustamante, F., Vergara, A., Villaseñor, J., Wong, B., and Rull, J. A., A controlled trial of pravastatin vs. probucol in the treatment of primary hypercholesterolemia. Rev. Invest. Clin., 44, 53-61 (1992).
35. Espenshade, P. J., and Hughes, A. L., Regulation of sterol synthesis in eukaryotes. Annu. Rev. Genet., 41, 401-427 (2007).
36. Scharnagl, H., Winkler, K., Mantz, S., Baumstark, M. W., Wieland, H., and März, W., Inhibition of HMG-CoA reductase with cerivastatin lowers dense low density lipoproteins in patients with elevated fasting glucose, impaired glucose tolerance and type 2 diabetes mellitus. Exp. Clin. Endocrinol. Diabetes, 112, 269-277 (2004).
37. Chiang, J. Y., Kimmel, R., and Stroup, D., Regulation of cholesterol 7 alpha-hydroxylase gene (CYP7A1) transcription by the liver orphan receptor (LXRalpha). Gene, 262, 257-265 (2001).
38. Makishima, M., Okamoto, A. Y., Repa, J. J., Tu, H., Learned, R. M., Luk, A., Hull, M. V., Lustig, K. D., Mangelsdorf, D. J., and Shan, B., Identification of a nuclear receptor for bile acids. Science, 284, 1362-1365 (1999).
39. Yu, L., Hammer, R. E., Li-Hawkins, J., Von Bergmann, K., Lutjohann, D., Cohen, J. C., and Hobbs, H. H., Disruption of Abcg5 and Abcg8 in mice reveals their crucial role in biliary cholesterol secretion. Proc. Natl. Acad. Sci. USA, 99, 16237-16242 (2002).
40. Makishima, M., Nuclear receptors as targets for drug development: regulation of cholesterol and bile acid metabolism by nuclear receptors. J. Pharmacol. Sci., 97, 177-183 (2005).
41. Kim, I., Ahn, S. H., Inagaki, T., Choi, M., Ito, S., Guo, G. L., Kliewer, S. A., and Gonzalez, F. J., Differential regulation of bile acid homeostasis by the farnesoid X receptor in liver and intestine. J. Lipid Res., 48, 2664-2672 (2007).