Human milk proteins: strides in proteomics and benefits in nutrition research

D’Alessandro, Angelo; Scaloni, Andrea; Zolla, Lello

doi:10.3920/978-90-8686-764-6_14

Cited by 2 publications

(2 citation statements)

References 53 publications

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“…To evaluate the level of isolation capability reached by each fractionation approach tested, proteins from untreated human milk, whey, and CN extracts were subjected to digestion and analysis by LC–MS/MS (see sections , , and ). A total of 123 proteins (see Supporting Information) were identified in the human milk sample, all of them previously reported. ,,− Venn diagrams, jointly with normalized areas of the relevant proteins present in whey and CN fractions, were used as an indicator of cross-contamination degree. From Venn diagrams (Figure ), it can be derived that only 35 proteins are recognized in all three extracts of CaP precipitation, whereas 40 and 44 proteins are found for CaP (2×) and isoelectric precipitation protocols, respectively.…”

Section: Results and Discussionmentioning

confidence: 99%

“…Only peptide and protein identifications with ≥95% confidence (unused score ≥ 1.3) were validated. Protein identifications were accepted either if they contained at least two identified peptides or if they contained only one peptide but they have been previously reported in any of the following references: refs , , and − . The proteomics data and result files from the analysis have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository, with the data set identifier PXD010315 and 10.6019/PXD010315.…”

Section: Materials and Methodsmentioning

confidence: 99%

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Improving Fractionation of Human Milk Proteins through Calcium Phosphate Coprecipitation and Their Rapid Characterization by Capillary Electrophoresis

2018

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This work describes a simple sample pretreatment method for the fractionation of human milk proteins (into their two main groups, whey and caseins) prior to their analysis. The protein-extraction protocol is based on the addition of calcium phosphate to nonadjusted pH human milk. The combination of calcium ions with phosphate results in an effective coprecipitation of caseins. To assess the suitability of this fractionation protocol, the protein extracts were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), LC-MS/MS, and capillary electrophoresis (CE) analysis. The results evidence a significant decrease in contamination of casein fraction with whey proteins and vice versa compared with the conventional isoelectric precipitation of caseins. In addition, CE fraction collection coupled to LC-MS/MS (off-line coupling) has been successfully applied to the identification of minor proteins in this complex matrix. The methodology presented here constitutes a promising tool to enlarge the knowledge of human milk proteome.

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Section: Results and Discussionmentioning

confidence: 99%

Section: Materials and Methodsmentioning

confidence: 99%

Improving Fractionation of Human Milk Proteins through Calcium Phosphate Coprecipitation and Their Rapid Characterization by Capillary Electrophoresis

2018

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Sweating the small stuff: Glycoproteins in human sweat and their unexplored potential for microbial adhesion

et al. 2015

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There is increasing evidence that secretory fluids such as tears, saliva and milk play an important role in protecting the human body from infection via a washing mechanism involving glycan-mediated adhesion of potential pathogens to secretory glycoproteins. Interaction of sweat with bacteria is well established as the cause of sweat-associated malodor. However, the role of sweat glycoproteins in microbial attachment has received little, if any, research interest in the past. In this review, we demonstrate how recent published studies involving high-throughput proteomic analysis have inadvertently, and fortuitously, exposed an abundance of glycoproteins in sweat, many of which have also been identified in other secretory fluids. We bring together research demonstrating microbial adhesion to these secretory glycoproteins in tears, saliva and milk and suggest a similar role of the sweat glycoproteins in mediating microbial attachment to sweat and/or skin. The contribution of glycan-mediated microbial adhesion to sweat glycoproteins, and the associated impact on sweat derived malodor and pathogenic skin infections are unchartered new research areas that we are beginning to explore.

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Human milk proteins: strides in proteomics and benefits in nutrition research

Cited by 2 publications

References 53 publications

Improving Fractionation of Human Milk Proteins through Calcium Phosphate Coprecipitation and Their Rapid Characterization by Capillary Electrophoresis

Improving Fractionation of Human Milk Proteins through Calcium Phosphate Coprecipitation and Their Rapid Characterization by Capillary Electrophoresis

Sweating the small stuff: Glycoproteins in human sweat and their unexplored potential for microbial adhesion

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