PXD000906

PXD000906 is an original dataset announced via ProteomeXchange.

Title	Deciphering changes to human platelet proteome and degradome during storage before transfusion
Description	Proteases, and specifically metalloproteinases, have been linked to the loss of platelet function during storage before transfusion, albeit the mechanism remains unknown. We used a dedicated N-terminomics technique, multiplex iTRAQ-TAILS (Terminal Amine Isotope Labeling of Substrates), to characterize the human platelet proteome, N-terminome, and their post-translational modifications throughout platelet storage under blood banking conditions. From the identified 2,938 proteins and 7,503unique peptides we characterized N-terminal methionine excision, co- and post-translational N-acetylation, maturation and proteolytic processing of proteins in human platelets. We also identified for the first time in platelets 10 proteins previously classified as “missing” in the human proteome. Most of identified N-termini (77%) were internal, of which 105 were novel potential alternative translation start sites, with 2,180 representing stable proteolytic products, thus highlighting a prominent previously uncharacterized role of proteolytic processing during platelet storage. Protease inhibitor studies revealed metalloproteinases as being primarily responsible for proteolytic processing (as opposed to degradation) during storage. System-wide identification of metallo- and other proteinase substrates and their respective cleavage sites offers novel potential mechanisms of their effect on protein activity and platelet function during storage.
HostingRepository	PRIDE
AnnounceDate	2014-10-24
AnnouncementXML	Submission_2014-10-24_02:53:14.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Anna Prudova
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	deamidated residue; monohydroxylated residue; iTRAQ8plex-116 reporter+balance reagent acylated residue; acetylated residue; iodoacetamide derivatized residue; iTRAQ4plex-116 reporter+balance reagent acylated residue
Instrument	QSTAR

Revision	Datetime	Status	ChangeLog Entry
0	2014-04-15 01:38:25	ID requested
⏵ 1	2014-10-24 02:53:15	announced

Prudova A, Serrano K, Eckhard U, Fortelny N, Devine DV, Overall CM, TAILS N-terminomics of human platelets reveals pervasive metalloproteinase-dependent proteolytic processing in storage. Blood, 124(26):e49-60(2014) [pubmed]

ProteomeXchange project tag: Human Proteome Project

curator keyword: Biomedical

submitter keyword: human, platelets, LS-MSMS, TAILS, degradome, metalloproteinases, proteases

Christopher Mark Overall
contact affiliation	Centre for Blood Research, Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, BC, Canada.
contact email	chris.overall@ubc.ca
lab head
Anna Prudova
contact affiliation	University of British Columbia
contact email	aprudova@gmail.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2014/10/PXD000906

PRIDE project URI

• PRIDE
  1. PXD000906
     1. Label: PRIDE project
     2. Name: Deciphering changes to human platelet proteome and degradome during storage before transfusion