PXD000688

PXD000688 is an original dataset announced via ProteomeXchange.

Title	Human milk and gastric peptidomics
Description	It is unclear to what degree protein degradation occurs in the infant stomach and whether peptides previously annotated for bioactivity are released. This study combined nanospray liquid chromatography separation with time of flight mass spectrometry, comprehensive structural libraries and informatics to interrogate milk of three human mothers and the gastric aspirates from their 4–12 day post-partum infants. Milk from the mothers contained almost two hundred distinct peptides, demonstrating enzymatic degradation of milk proteins beginning either during lactation or between milk collection and feeding. In the gastric samples, 649 milk peptides were identified, demonstrating that digestion continues in the infant stomach. The majority of peptides in both the intact milk and gastric samples were derived from β-casein. The numbers of peptides from β-casein, lactoferrin, α-lactalbumin, lactadherin, κ-casein, serum albumin, bile-salt associated lipase and xanthine dehydrogenase/oxidase were significantly higher in the gastric samples than the milk samples (p<0.05). Six hundred three peptides were significantly different in abundance between milk and gastric samples (p<0.05). Most of the identified peptides have previously identified biological activity. Gastric proteolysis occurs in the term infant in the first two weeks of life releasing biologically active milk peptides with immunomodulatory, antibacterial, and calcium-binding activity of clinical relevance to the proximal intestinal tract.
HostingRepository	PRIDE
AnnounceDate	2014-07-28
AnnouncementXML	Submission_2014-07-28_00:53:01.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD000688
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	David Dallas
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	deamidated residue; monohydroxylated residue; dehydrated residue; acetylated residue; phosphorylated residue; deaminated residue
Instrument	6520 Quadrupole Time-of-Flight LC/MS

Revision	Datetime	Status	ChangeLog Entry
0	2014-01-17 02:52:12	ID requested
1	2014-04-15 05:40:20	announced
⏵ 2	2014-07-28 00:53:02	announced	Updated project metadata.

Dallas DC, Guerrero A, Khaldi N, Borghese R, Bhandari A, Underwood MA, Lebrilla CB, German JB, Barile D, A peptidomic analysis of human milk digestion in the infant stomach reveals protein-specific degradation patterns. J Nutr, 144(6):815-20(2014) [pubmed]

submitter keyword: human milk, peptidomics

David Dallas
contact affiliation	UC Davis
contact email	dcdallas@ucdavis.edu
lab head
David Dallas
contact affiliation	University of California, Davis
contact email	dcdallas@ucdavis.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD000688
     1. Label: PRIDE project
     2. Name: Human milk and gastric peptidomics