Proteomic and Phospho-Proteomic Profile of Human Platelets in Basal, Resting State: Insights into Integrin Signaling

Qureshi, Amir H.; Chaoji, Vineet; Maiguel, Dony; Faridi, Mohd Hafeez; Barth, Constantinos J.; Salem, Saeed M.; Singhal, Mudita; Stoub, Darren; Krastins, Bryan; Ogihara, Mitsunori; Zaki, Mohammed J.; Gupta, Vineet

doi:10.1371/journal.pone.0007627

Title: Proteomic and Phospho-Proteomic Profile of Human Platelets in Basal, Resting State: Insights into Integrin Signaling

Journal Article · 27 October 2009 · PLoS ONE

DOI: https://doi.org/10.1371/journal.pone.0007627 · OSTI ID:1627388

Qureshi, Amir H. ^[1]; Chaoji, Vineet ^[2]; Maiguel, Dony ^[3]; Faridi, Mohd Hafeez ^[3]; Barth, Constantinos J. ^[3]; Salem, Saeed M. ^[2]; Singhal, Mudita ^[4]; Stoub, Darren ^[5]; Krastins, Bryan ^[6]; Ogihara, Mitsunori ^[3]; Zaki, Mohammed J. ^[2]; Gupta, Vineet ^[7]

Harvard Medical School, Boston, MA (United States); University of Miami, Miami, FL (United States); DOE/OSTI
Rensselaer Polytechnic Institute, Troy, NY (United States)
University of Miami, Miami, FL (United States)
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Rollins College, Winter Park, FL (United States)
Thermo-Fisher BRIMS Center, Cambridge, MA (United States)
Harvard Medical School, Boston, MA (United States); University of Miami, Miami, FL (United States)

During atherogenesis and vascular inflammation quiescent platelets are activated to increase the surface expression and ligand affinity of the integrin aIIbβ3 via inside-out signaling. Diverse signals such as thrombin, ADP and epinephrine transduce signals through their respective GPCRs to activate protein kinases that ultimately lead to the phosphorylation of the cytoplasmic tail of the integrin aIIbβ3 and augment its function. The signaling pathways that transmit signals from the GPCR to the cytosolic domain of the integrin are not well defined. In an effort to better understand these pathways, we employed a combination of proteomic profiling and computational analyses of isolated human platelets. We analyzed ten independent human samples and identified a total of 1507 unique proteins in platelets. This is the most comprehensive platelet proteome assembled to date and includes 190 membrane-associated and 262 phosphorylated proteins, which were identified via independent proteomic and phospho-proteomic profiling. We used this proteomic dataset to create a platelet protein-protein interaction (PPI) network and applied novel contextual information about the phosphorylation step to introduce limited directionality in the PPI graph. This newly developed contextual PPI network computationally recapitulated an integrin signaling pathway. Most importantly, our approach not only provided insights into the mechanism of integrin aIIbβ3 activation in resting platelets but also provides an improved model for analysis and discovery of PPI dynamics and signaling pathways in the future.

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Research Organization:: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); National Science Foundation (NSF); National Institutes of Health (NIH)

Grant/Contract Number:: AC05-76RL01830

OSTI ID:: 1627388

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 10 Vol. 4; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Protein Phosphatase 1 Associates with the Integrin αIIb Subunit and Regulates Signaling Vijayan, K. Vinod; Liu, Yan; Li, Tong-Tong Journal of Biological Chemistry, Vol. 279, Issue 32 https://doi.org/10.1074/jbc.C400239200	journal	August 2004
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Biological Variation of the Platelet Proteome in the Elderly Population and Its Implication for Biomarker Research Winkler, Wolfgang; Zellner, Maria; Diestinger, Michael Molecular & Cellular Proteomics, Vol. 7, Issue 1 https://doi.org/10.1074/mcp.M700137-MCP200	journal	January 2008
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