PXD017537

PXD017537 is an original dataset announced via ProteomeXchange.

Title	Quantitative proteomic analysis of seminal plasma, sperm membrane proteins and seminal extracellular vesicles suggests vesicular mechanisms aid in the removal and addition of proteins to the ram sperm membrane.
Description	Quantitative proteomic studies are contributing greatly to our understanding of the spermatozoon through the provision of detailed information on the proteins spermatozoa acquire and shed in the acquisition of fertility. Extracellular vesicles (EVs) are thought to aid in the delivery of proteins to spermatozoa in the male reproductive tract. The aim of this study was to identify EV proteins isolated from ram seminal plasma. High-speed centrifugation using Optiprep sucrose gradients was used to purify two EV populations from seminal plasma. Liquid chromatography and tandem mass spectrometry (LC-MS/MS) with quantitative SWATH was used to identify proteins enriched in the extracellular vesicle preparation (e.g. EDIL3) and those that were co-isolated with vesicular preparations due to their abundance or adhesive nature (e.g. BSPs). Ram sperm plasma membrane proteins were also isolated using nitrogen cavitation and identified with LC-MS/MS to better understand the interplay of proteins between the sperm membrane and extracellular environment. The categorisation of proteins enriched in the EV population (P<0.05, 2-fold increase compared to whole seminal plasma) according to their function revealed three main groupings: vesicle biogenesis, metabolism and membrane adhesion and remodelling. The latter group contained many reproduction-specific proteins that show demonstrable links to sperm fertility. Many of these membrane-bound proteins show testicular expression and are shed from the sperm surface during epididymal maturation (e.g. TEX101, LY6K). Their association with seminal EVs suggests that EVs may not only deliver protein cargo to spermatozoa but also assist in the removal of proteins from the sperm membrane.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:03:21.233.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Taylor Pini
SpeciesList	scientific name: Ovis aries; NCBI TaxID: 9940;
ModificationList	No PTMs are included in the dataset
Instrument	TripleTOF 6600

Revision	Datetime	Status	ChangeLog Entry
0	2020-02-17 03:04:53	ID requested
1	2020-05-07 22:21:46	announced
2	2020-06-09 23:30:55	announced	2020-06-10: Updated publication reference for PubMed record(s): 32383290.
⏵ 3	2024-10-22 05:03:28	announced	2024-10-22: Updated project metadata.

Leahy T, Rickard JP, Pini T, Gadella BM, de Graaf SP, Quantitative Proteomic Analysis of Seminal Plasma, Sperm Membrane Proteins, and Seminal Extracellular Vesicles Suggests Vesicular Mechanisms Aid in the Removal and Addition of Proteins to the Ram Sperm Membrane. Proteomics, 20(12):e1900289(2020) [pubmed]

10.1002/pmic.201900289;

submitter keyword: prostasomes, microvesicles, EDIL3,epididysomes, sperm surface

Taylor Pini
contact affiliation	Colorado Center for Reproductive Medicine
contact email	tpini@flcolo.com
lab head
Taylor Pini
contact affiliation	University of Sydney
contact email	tpini@flcolo.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/2020/05/PXD017537

PRIDE project URI

• PRIDE
  1. PXD017537
     1. Label: PRIDE project
     2. Name: Quantitative proteomic analysis of seminal plasma, sperm membrane proteins and seminal extracellular vesicles suggests vesicular mechanisms aid in the removal and addition of proteins to the ram sperm membrane.