Abstract:Milk contains all the nutrients for the growth and development of the neonate. However, milk composition is not constant during lactation. To study the changes of the milk proteome over lactation, filter-aided sample preparation combined with dimethyl labeling followed by liquid chromatography tandem mass spectrometry was used to identify and quantify milk proteins from 4 cows. A total of 229 proteins were identified, of which 219 were quantified. An 80% overlap was found in identified and quantified proteins … Show more
“…Although the number of enzymes were similar, they were quite different in the type between human and bovine milk. The enzymes assisting nutrient digestion were bile salt-activated lipase (CEL), and lipoprotein lipase (LPL) alpha-trypsin chain 1 (PRSS1) in human milk (Table 1 ) [ 16 , 18 ], whereas pancreatic ribonuclease 1 (RNASE1), LPL, and ribonuclease 4 (RNASE4) were dominant in bovine milk [ 13 , 17 ]. Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Since milk serum protein content is far higher than MFGM protein content [ 20 ], the quantitative changes over lactation were only determined for milk serum. A total of 299 proteins were quantified in bovine milk serum [ 13 , 17 ] and 247 in human milk serum [ 16 , 18 ] by FASP and dimethyl labelling combined with LC-MS/MS. There were 71 common proteins quantified in human and bovine milk serum, with 34 of them quantified in every time point over lactation.…”
Section: Resultsmentioning
confidence: 99%
“…The high abundant enzymes related to lipid and protein degradation in human milk, such as bile salt-activated lipase, lipoprotein lipase, trypsin, and cathepsin D [ 31 ], suggests that human milk itself contributes to the digestive capacity, thereby being able to more effectively deal with immature luminal digestion [ 32 ]. The differences in the dominant digestive enzymes between human milk (bile salt-activated lipase) and bovine milk (ribonuclease pancreatic), which have been discussed in our previous papers [ 17 ] may thus reflect the differences in the needs for support of the digestion system between infants and calves.…”
BackgroundMilk is the most important food for growth and development of the neonate, because of its nutrient composition and presence of many bioactive proteins. Differences between human and bovine milk in low abundant proteins have not been extensively studied. To better understand the differences between human and bovine milk, the qualitative and quantitative differences in the milk proteome as well as their changes over lactation were compared using both label-free and labelled proteomics techniques. These datasets were analysed and compared, to better understand the role of milk proteins in development of the newborn.MethodsHuman and bovine milk samples were prepared by using filter-aided sample preparation (FASP) combined with dimethyl labelling and analysed by nano LC LTQ-Orbitrap XL mass spectrometry.ResultsThe human and bovine milk proteome show similarities with regard to the distribution over biological functions, especially the dominant presence of enzymes, transport and immune-related proteins. At a quantitative level, the human and bovine milk proteome differed not only between species but also over lactation within species. Dominant enzymes that differed between species were those assisting in nutrient digestion, with bile salt-activated lipase being abundant in human milk and pancreatic ribonuclease being abundant in bovine milk. As lactation advances, immune-related proteins decreased slower in human milk compared to bovine milk. Notwithstanding these quantitative differences, analysis of human and bovine co-expression networks and protein-protein interaction networks indicated that a subset of milk proteins displayed highly similar interactions in each of the different networks, which may be related to the general importance of milk in nutrition and healthy development of the newborn.ConclusionsOur findings promote a better understanding of the differences and similarities in dynamics of human and bovine milk proteins, thereby also providing guidance for further improvement of infant formula.Electronic supplementary materialThe online version of this article (doi:10.1186/s12953-016-0110-0) contains supplementary material, which is available to authorized users.
“…Although the number of enzymes were similar, they were quite different in the type between human and bovine milk. The enzymes assisting nutrient digestion were bile salt-activated lipase (CEL), and lipoprotein lipase (LPL) alpha-trypsin chain 1 (PRSS1) in human milk (Table 1 ) [ 16 , 18 ], whereas pancreatic ribonuclease 1 (RNASE1), LPL, and ribonuclease 4 (RNASE4) were dominant in bovine milk [ 13 , 17 ]. Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Since milk serum protein content is far higher than MFGM protein content [ 20 ], the quantitative changes over lactation were only determined for milk serum. A total of 299 proteins were quantified in bovine milk serum [ 13 , 17 ] and 247 in human milk serum [ 16 , 18 ] by FASP and dimethyl labelling combined with LC-MS/MS. There were 71 common proteins quantified in human and bovine milk serum, with 34 of them quantified in every time point over lactation.…”
Section: Resultsmentioning
confidence: 99%
“…The high abundant enzymes related to lipid and protein degradation in human milk, such as bile salt-activated lipase, lipoprotein lipase, trypsin, and cathepsin D [ 31 ], suggests that human milk itself contributes to the digestive capacity, thereby being able to more effectively deal with immature luminal digestion [ 32 ]. The differences in the dominant digestive enzymes between human milk (bile salt-activated lipase) and bovine milk (ribonuclease pancreatic), which have been discussed in our previous papers [ 17 ] may thus reflect the differences in the needs for support of the digestion system between infants and calves.…”
BackgroundMilk is the most important food for growth and development of the neonate, because of its nutrient composition and presence of many bioactive proteins. Differences between human and bovine milk in low abundant proteins have not been extensively studied. To better understand the differences between human and bovine milk, the qualitative and quantitative differences in the milk proteome as well as their changes over lactation were compared using both label-free and labelled proteomics techniques. These datasets were analysed and compared, to better understand the role of milk proteins in development of the newborn.MethodsHuman and bovine milk samples were prepared by using filter-aided sample preparation (FASP) combined with dimethyl labelling and analysed by nano LC LTQ-Orbitrap XL mass spectrometry.ResultsThe human and bovine milk proteome show similarities with regard to the distribution over biological functions, especially the dominant presence of enzymes, transport and immune-related proteins. At a quantitative level, the human and bovine milk proteome differed not only between species but also over lactation within species. Dominant enzymes that differed between species were those assisting in nutrient digestion, with bile salt-activated lipase being abundant in human milk and pancreatic ribonuclease being abundant in bovine milk. As lactation advances, immune-related proteins decreased slower in human milk compared to bovine milk. Notwithstanding these quantitative differences, analysis of human and bovine co-expression networks and protein-protein interaction networks indicated that a subset of milk proteins displayed highly similar interactions in each of the different networks, which may be related to the general importance of milk in nutrition and healthy development of the newborn.ConclusionsOur findings promote a better understanding of the differences and similarities in dynamics of human and bovine milk proteins, thereby also providing guidance for further improvement of infant formula.Electronic supplementary materialThe online version of this article (doi:10.1186/s12953-016-0110-0) contains supplementary material, which is available to authorized users.
“…The higher concentrations of ApoE in CM and HM were found in early lactation, and signi cantly decreased over lactation, indicating the importance of cholesterol in the development of the neonate [25,26]. Cholesterol plays an important role in the synthesis of vitamin D and the steroid hormones, which is critical to the development of the newborns [26]. In our study, DM provides a higher level of cholesterol transporters than HM and CM, which may help the newborns acquire a large amount of cholesterol.…”
Section: Discussionmentioning
confidence: 96%
“…ApoE and ApoH are also crucial elements in the lipoprotein metabolism and cholesterol transport [23,24]. The higher concentrations of ApoE in CM and HM were found in early lactation, and signi cantly decreased over lactation, indicating the importance of cholesterol in the development of the neonate [25,26]. Cholesterol plays an important role in the synthesis of vitamin D and the steroid hormones, which is critical to the development of the newborns [26].…”
Background: Donkey milk (DM), similar to human milk (HM) in compositions, has been suggested as the best potential hypoallergenic replacement diet for babies suffering from cow milk (CM) protein allergens. Despite advances in proteomics technologies, studies of the DM whey proteome are relatively sparse. In this study, label-free mass spectrometry analysis was conducted to quantitatively identify the differentially expressed whey proteins (DEPs) in DM vs HM group and DM vs CM group. Results: In total, 249 and 418 DEPs were found in these two groups respectively. DEPs were then subjected to intensive bioinformatic analysis. Results revealed that the majority of DEPs participated in lipid metabolic process, regulation of cytokine production, chemical homeostasis and catabolic process. Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways analysis found that these DEPs mainly participated in complement and coagulation cascades, and cholesterol metabolism. Conclusion: These results may provide valuable information in the composition of milk whey proteins in DM, HM and CM, especially for low abundant components, and expand our knowledge of different biological functions between DM and HM or CM.
BackgroundAlthough there are studies on colostrum and milk proteomics of different species in the literature, there is no published report about different quality bovine colostrums’ proteomics.ObjectivesThe aim of this study was to compare the proteome content of high‐ and low‐quality bovine colostrums for the first time.MethodsColostrum samples were collected from 32 Holstein cows from the same farm that had just calved. Brix% levels of colostrums were measured, and then, those with a Brix% value of ≥27% were classified as high‐quality and those with a Brix% value of ˂22% as low‐quality. Three samples from high‐quality and low‐quality colostrums were selected and proteomic analyses were performed by pooling separately.ResultsTotally 95 proteins were identified in the colostrums, and 19 of them showed significant changes between high‐ and low‐quality colostrums. Expressions in colostrum of glycosylation‐dependent cell adhesion molecule‐1, cofilin‐1, alpha‐S2‐casein, alpha‐lactalbumin, alpha‐1B‐glycoprotein, actin_cytoplasmic‐1, nucleobindin‐1, cathelicidin‐4, inter‐alpha‐trypsin inhibitor heavy chain H4, chitinase‐3‐like protein 1 and monocyte differentiation antigen CD14 were lower, whereas tetranectin, secreted frizzled‐related protein‐1 (SFRP1), perilipin‐2, coatomer subunit epsilon (COPE), butyrophilin subfamily 1 member A1, polyubiquitin‐B, lactadherin and albumin levels were higher in high‐quality colostrum than low‐quality colostrum. Moreover, SFRP1, COPE and cathelicidin‐4 proteins were identified for the first time in bovine colostrum. In high‐quality colostrum, the most prominently down‐regulated proteins were cathelicidin‐4 (26.01‐fold) and cofilin‐1 (17.42‐fold), and the most prominently up‐regulated proteins were COPE (3.37‐fold) and tetranectin (3.07‐fold).ConclusionsIt was detected that the proteome contents of high‐ and low‐quality bovine colostrums were different from each other. As new functions are added to the protein databases regarding these proteins detected in colostrums, the interactions of proteins with each other and with other molecules will be detailed and the effects of high‐quality colostrums on passive transfer immunity and calf health will be understood in full detail.
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