β-Lactotensin and neurotensin rapidly reduce serum cholesterol via NT2 receptor

Yamauchi, Rena; Ohinata, Kousaku; Yoshikawa, Masaaki

doi:10.1016/j.peptides.2003.10.003

Cited by 68 publications

(31 citation statements)

References 13 publications

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“…For example, the hydrophobic peptides 38) and undigested high molecular fraction of soy protein 39) were proposed as a mechanism of soy protein's cholesterol-lowering effect through acceleration of fecal excretion by these peptides. Recently, from bovine milk -lactoglobulin, a novel pentapeptide (IIAEK) 40) and -lactotensin 41) were discovered to be hypocholesterolemic peptides. The identification of these peptides was remarkable and might explain the parent protein's effect.…”

Section: Discussionmentioning

confidence: 99%

Effects of Rice Proteins from Two Cultivars,KoshihikariandShunyo, on Cholesterol and Triglyceride Metabolism in Growing and Adult Rats

Yang¹,

Kumagai²,

Kawamura³

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

Effects of Rice Proteins from Two Cultivars,KoshihikariandShunyo, on Cholesterol and Triglyceride Metabolism in Growing and Adult Rats

Yang¹,

Kumagai²,

Kawamura³

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…However, the biological function of this protein in addition to the transport of retinol and fatty acids has not yet been satisfactorily resolved. Recent studies have shown that ␤-LG produces hypocholesterolemic (44,45) and antioxidant effects (46,47) and may also serve as a growth factor for mammalian cells (48). The protein is acid-resistant in the gastrointestinal tract with a superior absorption capability via a receptor-mediated process (49 -51).…”

Section: Figmentioning

confidence: 99%

Epitope Mapping of a Monoclonal Antibody Specific to Bovine Dry Milk

Song

Chen

Yang

et al. 2005

Journal of Biological Chemistry

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␤-Lactoglobulin (␤-LG) is a bovine milk protein sensitive to thermal denaturation. Previously, we demonstrated that such structural change can be detected by a monoclonal antibody (mAb) specific to denatured ␤-LG. In the present study, we show a dramatic increase in ␤-LG immunoreactivity when heating raw milk between 70 and 80°C. To map out the specific epitope of ␤-LG recognized by this mAb, we used a combined strategy including tryptic and CNBr fragments, chemical modifications (acetylation and carboxymethylation), peptide array containing in situ synthesized peptides, and a synthetic soluble peptide for immunoassays. The antigenic determinant we defined was exactly located within the D strand (residues 66 -76) of ␤-LG. Circular dichroic spectral analysis shows that carboxymethylation on ␤-LG not only resulted in a substantial loss of ␤-configuration but also exerted a 10 times increase in immunoreactivity as compared with heated ␤-LG. The result suggests that a further disordered structure occurred in ␤-LG and thus rendered the mAb recognition. Mutations on each charged residue (three Lys and one Glu) revealed that Lys-69 and Glu-74 were extremely essential in maintaining the antigenic structure. We also show an inverse relationship between the immunoreactivity in heated ␤-LG and its binding to retinol or palmitic acid. Most interestingly, pH 9 -10, which neutralizes the Lys groups of ␤-LG, not only reduced its immunoreactivity but also its binding to palmitic acid implicating a role of Lys-69. Taken together, we concluded that strand D of ␤-LG participated in the thermal denaturation between 70 and 80°C and the binding to retinol and palmitic acid. The antigenic and biochemical roles of mAb specific to D strand are discussed in detail.

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“…Likewise, lactoferrin inhibits the build up of cellular cholesteryl esters by acting as scavenger (Kajikawa et al, 1994). Additionally, b-lactoglobulin showed hypocholesterolaemic activity in mice when provided at a dose of 30 mg kg À1 for 2 d in the diet or given orally at a dose of 100 mg kg À1 body weight (Yamauchi, Ohinata, & Yoshikawa, 2003).…”

Section: Resultsmentioning

confidence: 99%