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Use of Platelet Proteomic Profiles to Distinguish Platelets Activated by Different Agonists
Author(s) -
Yin Wei,
Shanmugavelayudam Saravan Kumar,
Rubenstein David Alan
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.686.13
Subject(s) - platelet , chemistry , platelet activation , shear stress , proteomics , lysis , biophysics , medicine , biochemistry , biology , materials science , composite material , gene
The objective of this study was to identify platelet signature proteomic profiles that would distinguish platelets activated by mechanical agonists and biochemical agonists. Human platelet rich plasma were treated with TRAP or exposed to various shear stress waveforms at physiological and pathological level. Plasma proteins and platelet lysate were then applied to CM‐10 ProteinChip arrays and analyzed using a SELDI ProteinChip reader. In the low molecular range (2,000 to 10,000 M/Z), more than 100 protein/peptide peaks were identified, and platelets responded to TRAP and shear stress differently. For platelet proteins, TRAP not only modified the magnitudes of significantly differentiated protein peaks, but also altered the shape of the spectral patterns. Shear stress only affected the magnitudes of differentiated protein expression, but did not cause the spectral pattern change. For plasma proteins, TRAP treatment did not cause any changes. Shear stress led to a significant decrease in peak intensity at M/Z=7765, while the same peak increased significantly in platelet proteins, indicating platelets might have sequestered this protein in response to shear stress stimulation. Preliminary studies suggested that this protein was possibly platelet factor 4. This work is supported by NSF 1039913.