Soy Protein Hydrolyzate with Bound Phospholipids Reduces Serum Cholesterol Levels in Hypercholesterolemic Adult Male Volunteers

Hori, Goro; Wang, Mingfu; Chan, Yin-Ching; Komtatsu, Tatsuji; Wong, Yueching; Chen, Tzu-Hsiu; Yamamoto, Kazuhiro; Nagaoka, Satoshi; Yamamoto, Shigeru

doi:10.1271/bbb.65.72

Cited by 79 publications

(38 citation statements)

References 20 publications

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“…In addition to being a source of nitrogen, peptides play beneficial roles in physiological activity. For example, soy peptides, the proteolytic products of soy proteins, can reduce serum lipid levels, scavenge free radicals, and reduce oxidative stress in mammalian cells (6)(7)(8). In yeast, soy peptides improve tolerance to freeze-thaw stress, repress the formation of lipid bodies (9), and accelerate ethanol fermentation (10,11).…”

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confidence: 99%

Functional Implications and Ubiquitin-Dependent Degradation of the Peptide Transporter Ptr2 in Saccharomyces cerevisiae

et al. 2014

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The peptide transporter Ptr2 plays a central role in di-or tripeptide import in Saccharomyces cerevisiae. Although PTR2 transcription has been extensively analyzed in terms of upregulation by the Ubr1-Cup9 circuit, the structural and functional information for this transporter is limited. Here we identified 14 amino acid residues required for peptide import through Ptr2 based on the crystallographic information of Streptococcus thermophilus peptide transporter PepT st and based on the conservation of primary sequences among the proton-dependent oligopeptide transporters (POTs). Expression of Ptr2 carrying one of the 14 mutations of which the corresponding residues of PepT st are involved in peptide recognition, salt bridge interaction, or peptide translocation failed to enable ptr2⌬trp1 cell growth in alanyl-tryptophan (Ala-Trp) medium. We observed that Ptr2 underwent rapid degradation after cycloheximide treatment (half-life, approximately 1 h), and this degradation depended on Rsp5 ubiquitin ligase. The ubiquitination of Ptr2 most likely occurs at the N-terminal lysines 16, 27, and 34. Simultaneous substitution of arginine for the three lysines fully prevented Ptr2 degradation. Ptr2 mutants of the presumed peptide-binding site (E92Q, R93K, K205R, W362L, and E480D) exhibited severe defects in peptide import and were subjected to Rsp5-dependent degradation when cells were moved to Ala-Trp medium, whereas, similar to what occurs in the wild-type Ptr2, mutant proteins of the intracellular gate were upregulated. These results suggest that Ptr2 undergoes quality control and the defects in peptide binding and the concomitant conformational change render Ptr2 subject to efficient ubiquitination and subsequent degradation.

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confidence: 99%

Functional Implications and Ubiquitin-Dependent Degradation of the Peptide Transporter Ptr2 in Saccharomyces cerevisiae

et al. 2014

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“…In particular, foods and beverages containing plant sterols [10,11] , fibers [12,13] , soy [14] , teas [15][16][17] and roughage [18] have been identified to lower blood cholesterols. Among the beverages, green tea has also been widely reported to display cholesterol-lowering and anti-oxidative effects, as well as exhibiting the ability to reduce abdominal fat.…”

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confidence: 99%

Efficacy and Safety of Chinese Black Tea (Pu-Ehr) Extract in Healthy and Hypercholesterolemic Subjects

Fujita¹,

Yamagami²

2008

Ann Nutr Metab

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Background/Aims: Water-extracted Chinese black tea (Pu-Ehr) exerts a precipitating effect on mixed bile salt micelles in foods. The amount of black tea extract (BTE) effective for hypercholesterolemia (HC) was examined in humans. Materials and Methods: Animals (test 1) and humans (tests 2–5) were given BTE in the following studies: (test 1) an acute 2-week toxicity test conducted in mice with 2,000 mg/kg BTE or saline; (test 2) a dose-finding 8-week toxicity study with excessive BTE ingestion (0.75 or 1 g/day) in 10 healthy and 10 borderline HC subjects; (test 3) a 1-day acute toxicity test using a (10 g) single-bolus study (n = 10); (test 4) a 5-week long-term safety test (5 g/day, n = 11), and (test 5) a 4-month noncomparative study in 21 HC patients ingesting 1 g/day. Results: The safety study showed no changes in hematological or relevant biochemical parameters in both mice and humans in the acute and long-term toxicity tests. In test 5, significant reductions in total and low-density lipoprotein cholesterol levels accompanied by significant decreases in body weight were observed without affecting other biochemical parameters. Conclusions: BTE significantly reduced blood cholesterol levels in humans and may prove safe and useful in preventing and improving metabolic syndrome-induced arteriosclerosis and/or obesity.

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“…The hypocholesterolemiant effect of active peptides can be attributed to two different action mechanisms: (a) inhibiting cholesterol absorption, by decreasing micellar cholesterol in the intestine; (b) some peptides may activate LDL receptors, typically blocked by hypercholesterolemia or excessive intake of cholesterol by diet [104]. [110] and have been partially attributed to soy 7S globulin (β-conglycinin). This protein's α+α' subunits strongly increase the expression of the Low Density Lipoprotein (LDL) receptor in hepatocyte cultures, resulting in increased LDL inactivation and degradation [111].…”

Section: Antihyperlipidemic and Antithrombotic Peptidesmentioning

confidence: 99%

“…Most of the literature on peptides with hypolipidemic property has been obtained from soy proteinhydrolysates. The hypocholesterolemic and hypolipidemic properties of soy protein hydrolysates have been studied in animals [109] and in humans [110] and have been partially attributed to soy 7S globulin (β-conglycinin). This protein's α+α' subunits strongly increase the expression of the Low Density Lipoprotein (LDL) receptor in hepatocyte cultures, resulting in increased LDL inactivation and degradation [111].…”

Section: Antihyperlipidemic and Antithrombotic Peptidesmentioning

confidence: 99%

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

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Throughout the second half of the last century and early this century the concept of the biological function of food proteins has changed significantly. While in the past the food proteins were regarded only as macronutrients capable of providing the amino acids to form the protein component of organs and tissues, also participating in the generation of metabolic energy for the normal functioning of living organisms, today it is known that certain proteins present in food, as well as fragments or peptides derived thereof, may participate in the general metabolism in a much more interactive manner, through bioactivities that go far beyond the nutritional functions that had been established by the end of the first half of the prior century.By making an analogy with the aeronautical activity we can say that in the past the food proteins functioned as black boxes holding numerous important pieces of information, which research and technology have only revealed, in part, in recent decades. In this period it Received: August 07, 2017; Accepted: September 12, 2017; Published: September 26, 2017 was found that certain proteins present in foods are naturally bioactive, and can be absorbed from the Gastrointestinal System (GIS) in their intact or slightly modified form and exercise specific bioactivities in the systemic metabolism [1], or, in addition, resist the action of digestive enzymes exercising different bioactivities in the gastrointestinal system [2]. Even more interesting were the findings that food proteins, of both plant and animal origin, contain, in their primary structures, specific amino acid sequences in their polypeptide chains, which when cleaved in the form of peptides by proteolytic enzymes or by specific chemical reagents may exercise diverse bioactivities that were latent in the original structure of the protein from which they originated.Bioactive peptides have been obtained from precursor proteins through the use of methodologies that have reached a high degree of sophistication and complexity, such as: (a) enzymatic hydrolysis by digestive enzymes; (b) proteolysis of the protein source by enzymes derived from microorganisms or plants; (c) fermentation process using culture with high proteolytic power and specificity. The bioactive potential of the peptides originating from the proteolysis of food proteins can be explored in the integral hydrolysates, produced in special conditions. However, in the current literature there are numerous research works and literature reviews emphasizing the importance of the isolation, purification, characterization, study of mechanisms and impact of these peptides on human health [3][4][5][6][7][8]. Production and Processing of Bioactive Peptides Derived from Food ProteinsA large number of plants and animals have been object of study as source of Bioactive Peptides (BAPs). Several studies were conducted, particularly with milk proteins [9,10], eggs [11,12], and muscle proteins from pigs [13], cattle [14], poultry [15], and fish [16]. BAPs have been obtained from...

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Soy Protein Hydrolyzate with Bound Phospholipids Reduces Serum Cholesterol Levels in Hypercholesterolemic Adult Male Volunteers

Cited by 79 publications

References 20 publications

Functional Implications and Ubiquitin-Dependent Degradation of the Peptide Transporter Ptr2 in Saccharomyces cerevisiae

Functional Implications and Ubiquitin-Dependent Degradation of the Peptide Transporter Ptr2 in Saccharomyces cerevisiae

Efficacy and Safety of Chinese Black Tea (Pu-Ehr) Extract in Healthy and Hypercholesterolemic Subjects

Food Proteins and Bioactive Peptides, Functional Diets

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