摘要
Background: It is wel known that peptides play a vital role in the nutrition and health of dairy cows. Bovine oligopeptide transporter 1(bP epT 1) is involved in the peptide transport process in the gastrointestinal tracts of dairy cows. However,little information is known in the characteristics of bP epT 1. Therefore, the purpose of this study was to characterize bP epT 1 functional y using a mammalian cel expression system. The uptake of radiolabeled dipeptide glycyl-sarcosine([3 H]-Gly-Sar)into the bP epT 1-transfected Chinese hamster ovary cel s was measured at various pH and substrate concentrations and with or without 15 other smal peptides that contained Met or Lys.Results: Western blot results showed that the abundance of bP epT 1 protein in the jejunum and ileum are the highest in the gastrointestinal tract of dairy cows. The uptake of [3 H]-Gly-Sar by b Pep T1-Chinese hamster ovary cells was dependent on time, p H, and substrate concentration, with a low Kmvalue of 0.94 ± 0.06 mmol/L and a maximum velocity of 20.80 ± 1.74 nmol/(mg protein · 5 min). Most of the di-and tripeptides were the substrates of b Pep T1,based on substrate-competitive studies. However, bP epT 1 has a higher affinity to the peptides with shorter chains, greater hydrophobicity, and negative or neutral charges.Conclusions: These results demonstrated for the first time the functional characteristics of bP epT 1, and they provide a new insight and better understanding into its vital role in absorbing a wide range of peptides from the digestive tract of dairy cows.
Background: It is wel known that peptides play a vital role in the nutrition and health of dairy cows. Bovine oligopeptide transporter 1(bP epT 1) is involved in the peptide transport process in the gastrointestinal tracts of dairy cows. However,little information is known in the characteristics of bP epT 1. Therefore, the purpose of this study was to characterize bP epT 1 functional y using a mammalian cel expression system. The uptake of radiolabeled dipeptide glycyl-sarcosine([3 H]-Gly-Sar)into the bP epT 1-transfected Chinese hamster ovary cel s was measured at various pH and substrate concentrations and with or without 15 other smal peptides that contained Met or Lys.Results: Western blot results showed that the abundance of bP epT 1 protein in the jejunum and ileum are the highest in the gastrointestinal tract of dairy cows. The uptake of [3 H]-Gly-Sar by b Pep T1-Chinese hamster ovary cells was dependent on time, p H, and substrate concentration, with a low Kmvalue of 0.94 ± 0.06 mmol/L and a maximum velocity of 20.80 ± 1.74 nmol/(mg protein · 5 min). Most of the di-and tripeptides were the substrates of b Pep T1,based on substrate-competitive studies. However, bP epT 1 has a higher affinity to the peptides with shorter chains, greater hydrophobicity, and negative or neutral charges.Conclusions: These results demonstrated for the first time the functional characteristics of bP epT 1, and they provide a new insight and better understanding into its vital role in absorbing a wide range of peptides from the digestive tract of dairy cows.
基金
supported by the grants from the National Key Basic Research Program of China Ministry of Science and Technology(Grant No.2011CB100801)
Funds for Distinguished Young Scientists of Zhejiang Province(R16C170002)
