Antihypertensive effect of ACE inhibitory oligopeptides from chicken egg yolks

Yoshii, Hiroshi; Tachi, Norihide; Ohba, Riichiro; Sakamura, Osamu; Takeyama, Hidemaro; Itani, Toru

doi:10.1016/s1532-0456(00)00172-1

Cited by 68 publications

(42 citation statements)

References 27 publications

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“…These peptides, which are inactive within the sequence of the parent protein, are liberated during enzymatic digestion or food processing. Among these bioactive peptides, a variety of angiotensin I-converting enzyme (ACE) inhibitory peptides with various amino acid sequences have been found in hydrolysates from food proteins digested with different proteases under different hydrolysis conditions, such as milk protein (Gobbetti, Ferranti, Smacchi, Goffredi, & Addeo, 2000;Jérôme, Laurent, & Jean-Luc, 2002;Meisel, 1998;Rober, Razaname, Mutter, & Juillerat, 2004), soy-protein (Wu & Ding, 2002), egg protein (Yoshii et al, 2001), fish protein (Fujita & Yoshikawa, 1999;Sugiyama et al, 1991) and porcine muscle protein (Arihara, Nakashima, Mukai, Ishikawa, & Itoh, 2001). In contrast to the many ACE-inhibitory peptides derived from vertebrate muscle, very few studies on ACE-inhibitory peptides from invertebrate muscles have been conducted.…”

Section: Introductionmentioning

confidence: 99%

Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases

Balti

Nedjar‐Arroume²,

Bougatef

et al. 2010

Food Research International

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Section: Introductionmentioning

confidence: 99%

Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases

Balti

Nedjar‐Arroume²,

Bougatef

et al. 2010

Food Research International

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“…[1][2][3][4][5][6][7][8][9][10][11] pointed out that three dipeptides, including AW (IC 50 = 18.8 µmol L −1 ), VW (IC 50 = 3.3 µmol L −1 ) and LW (IC 50 = 23.6 µmol L −1 ), were potential ACE inhibitory peptides. However, none of them were able effectively to reduce the blood pressure of SHRs in animal models.…”

Section: Introductionmentioning

confidence: 99%

Effects of tuber storage protein of yam (Dioscorea alata cv. Tainong No. 1) and its peptic hydrolyzates on spontaneously hypertensive rats

Lin

et al. 2006

J Sci Food Agric

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Yam storage protein (YSP) was purified from tubers of Dioscorea alata L. Tainong No. 1 (TN1) to homogeneity by DE-52 ion-exchange chromatography. The short-term (24 h) and long-term (25 days) antihypertensive effects of YSP-TN1 and its peptic hydrolyzates (PH-TN1) were measured in spontaneously hypertensive rats (SHRs). For 24-h antihypertensive measurements, SHRs (age 10 weeks, body weight from 240 to 250 g) were administered orally once (YSP-TN1 and PH-TN1, 40 mg kg −1 SHR) to measure the mean blood pressure (MBP), systolic blood pressure (SBP) and diastolic blood pressure (DBP). For a long-term antihypertensive measurement, SHRs (age 12 weeks, body weight from 250 to 270 g) were administered orally once a day for 25 days (YSP-TN1, 40 mg kg −1 SHR) to measure SBP, DBP and MBP. Captopril (10 or 15 mg kg −1 SHR) was used as a positive control. It was found that short-term administration of 40 mg kg −1 SHR of YSP-TN1 and PH-TN1 effectively lowered SHRs' MBP, SBP and DBP (For YSP-TN1, the lowest blood pressure was reached in the fourth hour and for PH-TN1 in the eighth hour). The lasting effects of PH-TN1 on reduced SHRs' BP were better than those of YSP-TN1 for one oral administration. For oral administration of 40 mg YSP-TN1 kg −1 SHR, the reduced MBP was 21.5 mmHg, which was comparable to 25.2 mmHg (the fourth hour) of 10 mg captopril kg −1 SHR oral administration. For oral administration of 40 mg PH-TN1 kg −1 SHR, the reduced MBP was 33.7 mmHg, comparable to 38.4 mmHg (the fourth hour) of 15 mg captopril kg −1 SHR. For long-term 25-day oral administration of 40 mg YSP-TN1 kg −1 SHR once a day, it was found that a feeding trial of YSP-TN1 effectively lowered SHRs' SBP, DBP and MBP. The greatest reduction in SHRs' blood pressure was reached on the ninth day, for the reduced SBP, 27.7 mmHg; for the reduced DBP, 28.3 mmHg; and for the reduced MBP, 27.5 mmHg.Keywords: antihypertension; diastolic blood pressure (DBP); means of blood pressure (MBP); peptic hydrolyzates; systolic blood pressure (SBP); spontaneously hypertensive rat (SHR); storage protein; yam INTRODUCTIONSeveral peptide-derived angiotensin-convertingenzyme (ACE) inhibitors have been used in the animal model of spontaneously hypertensive rats (SHRs) to evaluate the antihypertensive effects. [1][2][3][4][5][6][7][8][9][10][11] pointed out that three dipeptides, including AW (IC 50 = 18.8 µmol L −1 ), VW (IC 50 = 3.3 µmol L −1 ) and LW (IC 50 = 23.6 µmol L −1 ), were potential ACE inhibitory peptides. However, none of them were able effectively to reduce the blood pressure of SHRs in animal models. Fujita et al. 3 also found that the octapeptides of FFGRCVSP (IC 50 = 0.4 µmol L −1 ) and ERKIKVYL (IC 50 = 1.2 µmol L −1 ) were potent ACE inhibitors, but none of them were effective in animal models to reduce the blood pressure of SHRs.

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“…Milk proteins (Lopez-Fandin˜o, Otte, & Camp, 2006;Saito, 2008) and fermented dairies (Gonza´lez-Co´rdova et al, 2011;Sieber et al, 2010) are the main sources of ACE-inhibitory peptides. Other sources include soybean (Hang & Zhao, 2012), fish (Chen, Wang, Zhong, Wu, & Xia, 2012) and eggs (Yoshii et al, 2001). Proteolysis or microorganism fermentation of food proteins results in the release of some peptides with ACE inhibition; unfortunately, the sequences of the released ACE-inhibitory peptides are same as the peptide fractions held in the parent proteins.…”

Section: Introductionmentioning

confidence: 99%

In vitroangiotensin-converting enzyme inhibition or digestive stability of casein hydrolysates treated by plastein reaction in propanol–water medium

Zhao

2013

CyTA - Journal of Food

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Antihypertensive effect of ACE inhibitory oligopeptides from chicken egg yolks

Cited by 68 publications

References 27 publications

Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases

Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases

Effects of tuber storage protein of yam (Dioscorea alata cv. Tainong No. 1) and its peptic hydrolyzates on spontaneously hypertensive rats

In vitroangiotensin-converting enzyme inhibition or digestive stability of casein hydrolysates treated by plastein reaction in propanol–water medium

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