Complete sequence of the bovine β-lactoglobulin cDNA

Alexander, L. J.; Hayes, Geoffrey; Pearse, Martin J.; Stewart, A. Francis; Willis, Ian M.; Mackinlay, Antony G.

doi:10.1093/nar/17.16.6739

Cited by 60 publications

(24 citation statements)

References 3 publications

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“…This study using LC/MS/MS demonstrated for the first time that whey protein hydrolysates contained the BCAA-containing bioactive dipeptides, Ile-Val, Leu-Val, Val-Leu, Ile-Ile, Leu-Ile, IleLeu and Leu-Leu. As shown in Table 1, ␤-lactoglobulin, the main component of whey protein, has numerous amino acid sequences of BCAA-containing dipeptides compared to other protein sources (36)(37)(38). Recently, Foltz et al (19) reported that dietary tri-peptides are absorbed intact into the circulation in humans.…”

Section: Discussionmentioning

confidence: 99%

Branched-Chain Amino Acid-Containing Dipeptides, Identified from Whey Protein Hydrolysates, Stimulate Glucose Uptake Rate in L6 Myotubes and Isolated Skeletal Muscles

Morifuji

Koga²,

Kawanaka

et al. 2009

J Nutr Sci Vitaminol

116

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SummaryIn earlier studies we showed that dietary whey protein increased skeletal muscle and liver glycogen content in exercise-trained rats. However, little is known about whether ingredients of whey protein stimulate skeletal muscle glycogen accumulation. The aim of this study was to identify bioactive peptides in whey protein hydrolysates (WPH) which stimulated glucose uptake and glycogen synthesis rate in skeletal muscles. Branchedchain amino acid (BCAA)-containing dipeptides in WPH were identified using LC/MS/MS. L6 myotubes and isolated epitrochlearis muscles were used for the glucose uptake assays. The myotubes and muscles were incubated with or without 1 m M dipeptides, LY294002 a phosphoinositide 3-kinase (PI3-kinase) inhibitor, or GF102903X an atypical protein kinase C (aPKC) inhibitor, followed by measurement of 2-deoxyglucose uptake. Isolated muscles were incubated for 3 h with or without 1 m M Ile-Leu to determine glycogen synthesis rate. The BCAA-containing dipeptides, Ile-Val, Leu-Val, Val-Leu, Ile-Ile, Leu-Ile, Ile-Leu, and LeuLeu were detected in the WPH by LC/MS/MS. These dipeptides caused significant stimulation in glucose uptake rate in the L6 myotubes. Ile-Leu, the main component in WPH, also stimulated glucose uptake in isolated skeletal muscles. Stimulation of glucose uptake by IleLeu was completely inhibited by treatment with either LY294002, or GF109203X in both L6 cells and isolated muscles. Ile-Leu increased glycogen contents in isolated muscles. These results suggest that BCAA-containing bioactive dipeptides in WPH stimulate glucose uptake in skeletal muscles via the PI3-kinase and aPKC pathways, resulting in increased skeletal muscle glycogen contents.

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Section: Discussionmentioning

confidence: 99%

Branched-Chain Amino Acid-Containing Dipeptides, Identified from Whey Protein Hydrolysates, Stimulate Glucose Uptake Rate in L6 Myotubes and Isolated Skeletal Muscles

Morifuji

Koga²,

Kawanaka

et al. 2009

J Nutr Sci Vitaminol

116

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“…The leader peptides described for other members of the lipocalin protein family are almost as short as that of BBP [e.g. retinol binding-protein, 16 residues (Colantuoni et al, 1983); insecticyanin a and b, 17 residues (Li and Riddiford, 1992) ; P-lactoglobulin, 16 residues (Alexander et al, 1989)l. Remarkably, the 5' untranslated regions of the mRNAs of these lipocalins are also very similar in length, i.e., 51 nucleotides for BBP and the mammalian retinol-binding protein and 52 nucleotides in the insecticyanin a and b transcripts.…”

Section: Discussionmentioning

confidence: 99%

The bilin‐binding protein of Pieris brassicae

Schmidt

Skerra

1994

European Journal of Biochemistry

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The bilin‐binding protein (BBP) is a blue pigment protein which is abundant in the butterfly Pieris brassicae. In an attempt to clarify the physiological role of this member of the lipocalin family of proteins, its complete cDNA was cloned and expression of the BBP gene in P. brassicae was investigated. It was found that synthesis of the BBP mRNA is highly regulated during the insect's ontogenesis. In larvae after the third ecdysis as well as in pupae and adults, large amounts of the mRNA are present. Each of these stages itself displays a distinct time course of mRNA synthesis. In addition, BBP is expressed tissue specifically, with the fat body being the major source of this secretory protein in the larvae. Hence, the expression pattern of BBP in this organism is markedly different from the closely related pigment protein insecticyanin in Manduca sexta. Finally, the bacterial expression of BBP in a functional state was established as a basis for the future analysis of its ligand‐binding functions by protein engineering.

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“…This claim is supported by our eDNA sequence, which was almost identical to the sequence reported by Alexender e t al. 18 ) Simons et a!. reported the expression and secretion of ovine /3-LG into the milk of transgenic mice.…”

Section: Discussionmentioning

confidence: 99%