Poster Presentation 29th Annual Lorne Proteomics Symposium 2024

Understanding storage associated changes in platelet components using glycomics: A pilot study (#180)

Jessica Halliday 1 , Dianne Van Der Wal 2 , I. Darren Grice 1 3 , Daniel Kolarich 1 4
  1. Institute for Glycomics, Griffith University, Gold Coast Campus, QLD, Australia
  2. Research and Development, Australian Red Cross Lifeblood, Alexandria, NSW, Australia
  3. School of Pharmacy and Medical Science, Griffith University, Gold Coast Campus, QLD, Australia
  4. School of Environment and Science, Griffith University, Gold Coast Campus, QLD, Australia

Platelets are  lifesaving for bleeding and oncology patients. In Australia, the current recommended storage conditions are 22-24°C for up to 7 days. However, even within these conditions’ platelets are slowly deteriorating. Currently, there are no laboratory markers available to assess the donation’ quality prior to transfusion. To date, various -omics studies have been conducted to investigate this deterioration, however, the glycome and (glyco)proteome have been neglected until recently.

 

The aims of this study were to (i) characterise the platelet glycome, (ii) investigate its development throughout room-temperature storage, and (iii) investigate any storage-dependent (glyco)protein changes using state-of-the-art glycomics and proteomics technologies. The platelet glycome and (glyco)proteome of 14 donors across three-time points (days 1, 5 and 7) was investigated using well-established porous graphitized carbon (PGC)-liquid chromatography (LC)-Electrospray (ESI) tandem Mass Spectrometry (MS/MS) workflows and reversed-phase (RP) nanoLC-Orbitrap MS/MS glycoproteomics workflows, respectively.

 

This study identified the platelet glycome to consists of 119 N- and 28 O-glycans with only ~20 structures being present in high abundance (>0.2% relative intensity). 583 proteins were successfully identified, of which 33 were identified as N-glycosylated (glyco)proteins. Donor-specific variation appeared to impact the glycome and (glyco)proteome composition stronger compared to storage. Though no specific glycan or protein degradation markers were identified within this study, some proteins such as VAMP associated protein A exhibited a similar storage-dependent trend across the majority of donors.