AI帮你理解科学

AI 生成解读视频

AI抽取解析论文重点内容自动生成视频


pub
生成解读视频

AI 溯源

AI解析本论文相关学术脉络


Master Reading Tree
生成 溯源树

AI 精读

AI抽取本论文的概要总结


微博一下
Angiotensin converting enzyme inhibitory peptides derived from soy protein had a significant hypotensive effect on spontaneously hypertensive rats at the 100 mg/kg of body weight of rat/day administration level; their effect was stable and progressive

Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, no. 1 (2001): 501-506

被引用300|浏览6
WOS SCOPUS
下载 PDF 全文
引用
微博一下

摘要

Angiotensin converting enzyme (ACE) inhibitory peptides prepared from soy protein by the action of alcalase enzyme was tested for its hypotensive effect on spontaneously hypertensive rats (SHR). Captopril, an ACE inhibitor used widely for hypertension treatment, was also applied in comparison. A significant (p < 0.05) decrease in systolic...更多

代码

数据

0
简介
  • The new relationship between food and health has drawn considerable attention; of interest are the physiological functions of some food components against certain ailments.
  • Hypertension is a worldwide problem of epidemic proportions, which presents in 1520% of all adults.
  • It is the most common serious chronic health problem because it carries with it a high risk of cardiovascular complication [1].
  • Few studies were available on soy protein derived ACE inhibitory peptides
重点内容
  • The new relationship between food and health has drawn considerable attention; of interest are the physiological functions of some food components against certain ailments
  • Oral administration was performed as follows: control group; soy Angiotensin converting enzyme (ACE) inhibitory peptides at three different levels [100, 500, and 1000 mg/kg of body weight of rat (BW)/day, indicated as low dose, intermediate dose, and high dose, respectively]; Captropril administrated as a positive control at a dose of 50 mg/kg of BW/day; and another normotensive rat group fed with the highest dose of ACE peptides to determine its effect on the blood pressure of normotensive rats
  • According to the theory of the renin-angiotensin system (RAS) system, the activity of ACE should be lowered after administration of ACE inhibitors, but we found this phenomenon only in aorta after Captopril adminstration, whereas the group fed soy ACE inhibitory peptides showed no significant effect on the ACE activity of those organs
  • ACE inhibitory peptides derived from soy protein had a significant hypotensive effect on spontaneously hypertensive rats (SHR) at the 100 mg/kg of BW/day administration level; their effect was stable and progressive
  • As the number of hypertensive people in the world is increasing, ACE inhibitory peptides derived from food proteins may play an indispensable role in prophylaxis and prevention of this ailments in the long term
  • It was interesting to note an Na+ excretion function after soy ACE inhibitory peptides administration; further work on wash-out experiments should be performed to study reversibility
方法
  • At the end of the feeding period, rats were sacrificed by exsanguination from the abdominal aorta; blood was collected and placed for 1 h at room temperature (25 °C) and was centrifuged at 1000g for 15 min to obtain serum, which was used for serum ACE activity, lipid content, hemoglobin content, and mineral content determinations.
  • Lung and thoracic aorta were washed with 0.9% saline, after chopping and homogenization with pre-cooled 100 mM borate buffer; the homogenate was centrifuged at 3000g for 20 min, and the supernatant was used as crude ACE extract of those tissues for ACE activity determination
结果
  • Hypertension is a worldwide problem of epidemic proportions, which presents in 1520% of all adults.
结论
  • ACE inhibitory peptides derived from soy protein had a significant hypotensive effect on SHR at the 100 mg/kg of BW/day administration level; their effect was stable and progressive.
  • Soy ACE inhibitory peptides were less active than synthetic drugs such as Captopril, their significance, lies in the fact that they were contained in food taken daily and met the need for naturalness and safety.
  • It was interesting to note an Na+ excretion function after soy ACE inhibitory peptides administration; further work on wash-out experiments should be performed to study reversibility
总结
  • Introduction:

    The new relationship between food and health has drawn considerable attention; of interest are the physiological functions of some food components against certain ailments.
  • Hypertension is a worldwide problem of epidemic proportions, which presents in 1520% of all adults.
  • It is the most common serious chronic health problem because it carries with it a high risk of cardiovascular complication [1].
  • Few studies were available on soy protein derived ACE inhibitory peptides
  • Objectives:

    The objectives of this study were to investigate the bloodlowering and physiological effect of ACE inhibitory.
  • Methods:

    At the end of the feeding period, rats were sacrificed by exsanguination from the abdominal aorta; blood was collected and placed for 1 h at room temperature (25 °C) and was centrifuged at 1000g for 15 min to obtain serum, which was used for serum ACE activity, lipid content, hemoglobin content, and mineral content determinations.
  • Lung and thoracic aorta were washed with 0.9% saline, after chopping and homogenization with pre-cooled 100 mM borate buffer; the homogenate was centrifuged at 3000g for 20 min, and the supernatant was used as crude ACE extract of those tissues for ACE activity determination
  • Results:

    Hypertension is a worldwide problem of epidemic proportions, which presents in 1520% of all adults.
  • Conclusion:

    ACE inhibitory peptides derived from soy protein had a significant hypotensive effect on SHR at the 100 mg/kg of BW/day administration level; their effect was stable and progressive.
  • Soy ACE inhibitory peptides were less active than synthetic drugs such as Captopril, their significance, lies in the fact that they were contained in food taken daily and met the need for naturalness and safety.
  • It was interesting to note an Na+ excretion function after soy ACE inhibitory peptides administration; further work on wash-out experiments should be performed to study reversibility
表格
  • Table1: Basal Compositions of the Dietsa g/100 g diet
  • Table2: Soy ACE Inhibitory Peptides Composition (Percent, Dry Weight)
  • Table3: Effect of Oral Administration of Soybean Protein ACE Inhibitory Peptides on Blood Pressure (Mean ( SD)a dose
  • Table4: Effect of Oral Administration of Soybean Protein ACE Inhibitory Peptides on Serum Lipids and Hemoglobin Contenta
Download tables as Excel
基金
  • Hypertension is a worldwide problem of epidemic proportions, which presents in 1520% of all adults
研究对象与分析
groups of four rats: 5
The total recovery of peptide was 14.55% (w/w) in this procedure. SHR were randomly divided into five groups of four rats each. Oral administration was performed as follows: control group (no peptide or drug administration); soy ACE inhibitory peptides at three different levels [100, 500, and 1000 mg/kg of body weight of rat (BW)/day, indicated as low dose, intermediate dose, and high dose, respectively]; Captropril administrated as a positive control at a dose of 50 mg/kg of BW/day; and another normotensive rat group fed with the highest dose of ACE peptides to determine its effect on the blood pressure of normotensive rats.

Wu and Ding peptide (N × 6.25) total glycoside 91.79 4.18 ash 0.54 moisture

The dose range was set by our pretest result (unpublished data)

groups of four rats: 5
Experimental Methods. SHR were randomly divided into five groups of four rats each. Oral administration was performed as follows: control group (no peptide or drug administration); soy ACE inhibitory peptides at three different levels [100, 500, and 1000 mg/kg of body weight of rat (BW)/day, indicated as low dose, intermediate dose, and high dose, respectively]; Captropril administrated as a positive control at a dose of 50 mg/kg of BW/day; and another normotensive rat group fed with the highest dose of ACE peptides to determine its effect on the blood pressure of normotensive rats

引用论文
  • (1) Manger, W. M.; Page, I. H. An overview of current concepts regarding the pathogenesis and pathophysiology of hypertension. In Arterial Hypertension: Pathogenesis, Diagnosis, and Therapy; Rosenthal, J., Ed.; Springer-Verlag: New York, 1982; pp 1-40.
    Google ScholarFindings
  • (2) Laragh, J. H.; Bear, L.; Brunner, H. R.; Buhler, F. G.; Ealey, J. E.; Vaughan, E. D. Renin, angiotensin and aldosterone system in pathogenesis and management of hypertensive vascular disease. Am. J. Med. 1972, 52, 633-652.
    Google ScholarLocate open access versionFindings
  • (3) Soffer, R. L. Angiotensin converting enzyme and the regulation of vascoactive peptides. Annu. Rev. Biochem. 1976, 45, 73-94.
    Google ScholarLocate open access versionFindings
  • (4) Kato, H.; Suzuki, T. Bradykinin-potentiating peptides from the venom of Agkistrodon half blomhoffii. Isolation of five bradykinin potentiators and the amino avid sequences of two of them: potentiators B and C. Biochemistry 1971, 10, 972-980.
    Google ScholarLocate open access versionFindings
  • (5) Miguel, A.; Ondetti, N. J.; Williame, E. F.; Saba, A. Angiotensin I-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry 1971, 19, 40334039.
    Google ScholarLocate open access versionFindings
  • (6) Ondetti, M. A.; Rubin, B.; Cushman, D. W. Design of specific inhibitors of angiotensin converting enzyme: a new class of orally active antihypertensive agents. Science 1977, 196, 441-444.
    Google ScholarLocate open access versionFindings
  • (7) Laffan, R. J.; Goldberg, M. E.; High, J. P.; Schaffer, T. R.; Waugh, M. H.; Rubin, B. Antihypertensive activity in rats of SQ 14,225, an orally active inhibitor of angiotensin converting enzyme. J. Pharmacol. Exp. Ther. 1978, 204, 281-288.
    Google ScholarLocate open access versionFindings
  • (8) Fujita, H.; Yokoyama, K.; Yasumoto, R.; Yoshikawa, M. Antihypertensive effect of thermolysis digest of dried bonito spontaneously hypertensive rats. Clin. Exp. Pharmacol. Physiol. 1995, Suppl. 1, s304-s305.
    Google ScholarLocate open access versionFindings
  • (9) Cheung, H. S.; Cushman, D. W. Inhibition of homogeneous angiotensin I-converting enzyme of rabbit lung by synthetic venom peptides of Bothrops jararaca. Biochim. Biophys. Acta 1973, 293, 451-463.
    Google ScholarLocate open access versionFindings
  • (10) Suetsuna, K.; Saojima, K. Blood pressure reduction and vasodilatory effects in vivo of peptides originating from sardine muscle. J. Jpn. Soc. Nutr. Food Sci. 1989, 42 (2), 47-54.
    Google ScholarLocate open access versionFindings
  • (11) Sekiya, S.; Kobayashi, Y.; Kita, E. Antihypertensive effects of tryptic hydrolysate of casein on normotensive and hypertensive volunteers. J. Jpn. Soc. Nutr. Food Sci. 1992, 45, 513-517.
    Google ScholarLocate open access versionFindings
  • (12) Oshima, G.; Shimabukuro, H.; Nagasawa, K. Peptide inhibitors of angiotensin-converting enzyme in digests of gelatin by bacterial collagenase. Biochim. Biophys. Acta 1979, 566, 128-137.
    Google ScholarLocate open access versionFindings
  • (13) Kohmura, M.; Nio, N.; Kubo, K.; Minoshima, Y.; Munekata, E.; Ariyoshi, Y. Inhibition of angiotensinconverting enzyme by synthetic peptides of human -casein. Agric. Biol. Chem. 1989, 53, 2107-2114.
    Google ScholarLocate open access versionFindings
  • (14) Miyoshi, S.; Ishikawa, H.; Kaneko, T.; Fukui, F.; Tanaka, H.; Marayama, S. Structures and activity of angiotensin converting enzyme inhibitors in a R-zein hydrolysate. Agric. Biol. Chem. 1991, 55, 1313-1318.
    Google ScholarLocate open access versionFindings
  • (15) Yano, S.; Suzuki, K.; Funatsu, G. Isolation from R-zein hydrolysate of thermolysin peptides with angiotensin converting inhibitory activity. Biosci., Biotechnol., Biochem. 1996, 60, 661-663.
    Google ScholarLocate open access versionFindings
  • (16) Saito, S.; Nakamura, K.; Kawato, A.; Imayasu, S. Structure and activity of angiotensin converting inhibitory peptides from sake and sake lees. Biosci., Biotechnol., Biochem. 1994, 58, 1767-1771.
    Google ScholarLocate open access versionFindings
  • (17) Suetsuna, K. Study in the inhibitory activity against angiotensin converting enzyme of the peptides derived from sardine muscle. Ph.D. Thesis, Tokohu University, Miyagi, Sendai, Japan, 1992.
    Google ScholarFindings
  • (18) Kohama, Y.; Oka, H.; Kayamori, Y.; Tsujikawa, K.; Mimura, T.; Nagase, Y.; Satske, M. Potent synthetic analogues of angiotensin-converting enzyme inhibitors derived from tuna muscle. Agric. Biol. Chem. 1991, 55, 2169-2170.
    Google ScholarLocate open access versionFindings
  • (19) Kinoshita, E.; Yamakoshi, J.; Kikuchi, M. Purification and Identification of an Angiotensin I-Converting Enzyme Inhibitor from Soy Sauce. Biosci., Biotechnol., Biochem. 1993, 57, 1107-1110.
    Google ScholarLocate open access versionFindings
  • (20) Akiko, O.; Hiroshi, H.; Eiko, M. Antihypertensive substances in viscous material of fermented soybean (NATTO). In Food Hydrocolloids: Structures, Properties, and Functions; Nishinar, K., Doi, E., Eds.; Plenum Press: New York, 1994; pp 497-502.
    Google ScholarFindings
  • (21) Wu, J. P. Development of antihypertensive peptides from soy protein. Ph.D. Thesis,Wuxi University of Light Industry, Wuxi, China, 1998.
    Google ScholarFindings
  • (22) Cushman, D. W.; Cheung, H. S. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 1971, 20, 1637-1648.
    Google ScholarLocate open access versionFindings
  • (23) Grahl-Nielsn. Oligopeptides as sources of indispensable amino acids for mammalian cells in culture. In Vitro 1974, 9, 414-420.
    Google ScholarLocate open access versionFindings
  • (24) Lombardo, Y. B.; Morse, E. L.; Adibi, S. A. Specificity and mechanism of influence of amino acid residues on hepatic clearance of oligopeptides. J. Biol. Chem. 1988, 263, 12920-12926.
    Google ScholarLocate open access versionFindings
  • (25) Marayama, S.; Suzuki, H. A peptide inhibitor of angiotensin I-converting enzyme in the tryptic hydrolysate of casein. Agric. Biol. Chem. 1982, 46, 1393-1394.
    Google ScholarLocate open access versionFindings
  • (26) Marayama, S.; Mitachi, H.; Awaya, J.; Kurono, M.; Tomizuka, N.; Suzuki, H. Angiotensin converting enzyme inhibitory activity of C-terminal hexapeptide of RS1-casein. Agric. Biol. Chem. 1987, 51, 2557-2561.
    Google ScholarLocate open access versionFindings
  • (27) Astawan, M.; Wahyuni, M.; Yasuhara, T.; Yamada, K.; Tadokora, T.; Maokawa, A. Effects of angiotensin converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats. Biosci., Biotechnol., Biochem. 1995, 59 (3), 425-429.
    Google ScholarLocate open access versionFindings
  • (28) Murakami, T.; Hayashi, M.; Yoshizumi, Y. Hypotensive effect of Euglena (Euglena gracilis Z) pepsin hydrolysate. J. Jpn. Soc. Nutr. Food Sci. 1995, 48, 399-405.
    Google ScholarLocate open access versionFindings
  • (29) Murakami, T.; Soga, M.; Mitsunaga, T. The vascular tissue angiotensin I-converting enzyme activity and aortic elastin content in stroke-prone spontaneously hypertensive rats after fed fish diet. Clin. Exp. Pharmacol. Physiol. 1994, 21, 453-461.
    Google ScholarLocate open access versionFindings
  • (30) Fyhrquist, F.; Horting, L.; Gronhagen-Riska, C. Induction of angiotensin converting enzyme by captopril in cultured human endothelial cells. J. Clin. Endocrinol. Metab. 1982, 55, 783-786.
    Google ScholarLocate open access versionFindings
  • (31) Kohzuki, M.; Johnston, C. I.; Chai, S. Y.; Jackson, B.; Perich, R.; Paxton, D.; Mendelsohn, F. A. O. Measurement of angiotensin converting enzyme induction and inhibition using quantitative in vitro autoradiography: tissue selective induction after chronic Lisinopril treatment. J. Hypertens. 1991, 9, 579-587.
    Google ScholarLocate open access versionFindings
  • (32) Chai, S. Y.; Perich, R.; Jackson, B.; Mendelsohn, F. A. O. Acute and chronic effects of angiotensin converting enzyme inhibitors in tissue angiotensin converting enzyme. Clin. Exp. Pharmacol. Physiol. 1992, 19 (Suppl.), 7-12.
    Google ScholarLocate open access versionFindings
  • (33) Weidmann, P. Current antihypertensive drugs and serum lipoproteins. In Hypertension, Atherosclerosis and Lipids; Zwieten, V., Ed.; Royal Society of Medicine Series: London, U.K., 1992; pp 35-37.
    Google ScholarFindings
  • (34) MacGregor, G. A. Sodium is more important than calcium in essential hypertension. Hypertersion 1985, 7, 628-637.
    Google ScholarLocate open access versionFindings
  • (35) Weinberger, M. H. Salt sensitivity of blood pressure in humans. Hypertension 1996, 37 (Part 2), 481-490.
    Google ScholarFindings
  • (36) Joint National Committee on Detection, Re-evaluation, and Treatment of High Blood Pressure. The Fifth Report (JNC V). Arch Intern. Med. 1993, 153, 154-183.
    Google ScholarLocate open access versionFindings
  • (37) Tobian, L. The protective effects of high- potassium diets in hypertension, and the mechanisms by which highNaCl diets produce hypertension. In Hypertension: Pathophysiology; Diagnosis and Management, 2nd ed.; Laragh, J. H., Brenner, B. M., Eds.; Raven Press: New York, 1995.
    Google ScholarFindings
  • (38) Khaw, K. T.; Barrett-Connor, E. Dietary potassium and stroke-controlled trial of potassium chloride in the treatment of mild hypertension. Hypertension 1987, 9, 445-450.
    Google ScholarLocate open access versionFindings
  • (39) McCarron, D. A. Is calcium more important than sodium in the pathogenesis of essential hypertension? J. Hypertens. 1985, 607-627.
    Google ScholarLocate open access versionFindings
  • (40) Martınez, R. M.; Gimnenez, I.; Lou, Jose M.; Mayoral, Jose A.; Alda, Jose O. Soy isoflavonoids exhibit in vitro biological activities of loop diuretics. Am. J. Clin. Nutr. 1998, 68 (Suppl.), 1354s-1357s.
    Google ScholarLocate open access versionFindings
  • (41) Karaki, H.; Doi, K.; Sugano, S.; Uchiwa, H.; Sugai, R.; Murakami, U.; Takemoto, S. Antihypertensive effect of tryptic hydrolysate of milk casein in spontaneously hypertensive rats. Comp. Biochem. Physiol. 1990, 96C (2), 367-372.
    Google ScholarLocate open access versionFindings
作者
您的评分 :
0

 

标签
评论
小科