Quantitative proteome profiling of normal human circulating microparticles
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Quantitative proteome profiling of normal human circulating microparticles. / Østergaard, Ole; Nielsen, Christoffer T; Iversen, Line V; Jacobsen, Søren; Tanassi, Julia T; Heegaard, Niels H H.
In: Journal of Proteome Research, Vol. 11, No. 4, 2012, p. 2154-63.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Quantitative proteome profiling of normal human circulating microparticles
AU - Østergaard, Ole
AU - Nielsen, Christoffer T
AU - Iversen, Line V
AU - Jacobsen, Søren
AU - Tanassi, Julia T
AU - Heegaard, Niels H H
PY - 2012
Y1 - 2012
N2 - Circulating microparticles (MPs) are produced as part of normal physiology. Their numbers, origin, and composition change in pathology. Despite this, the normal MP proteome has not yet been characterized with standardized high-resolution methods. We here quantitatively profile the normal MP proteome using nano-LC-MS/MS on an LTQ-Orbitrap with optimized sample collection, preparation, and analysis of 12 different normal samples. Analytical and procedural variation were estimated in triply processed samples analyzed in triplicate from two different donors. Label-free quantitation was validated by the correlation of cytoskeletal protein intensities with MP numbers obtained by flow cytometry. Finally, the validity of using pooled samples was evaluated using overlap protein identification numbers and multivariate data analysis. Using conservative parameters, 536 different unique proteins were quantitated. Of these, 334 (63%) were present in all samples and represent an MP core proteome. Technical triplicates showed
AB - Circulating microparticles (MPs) are produced as part of normal physiology. Their numbers, origin, and composition change in pathology. Despite this, the normal MP proteome has not yet been characterized with standardized high-resolution methods. We here quantitatively profile the normal MP proteome using nano-LC-MS/MS on an LTQ-Orbitrap with optimized sample collection, preparation, and analysis of 12 different normal samples. Analytical and procedural variation were estimated in triply processed samples analyzed in triplicate from two different donors. Label-free quantitation was validated by the correlation of cytoskeletal protein intensities with MP numbers obtained by flow cytometry. Finally, the validity of using pooled samples was evaluated using overlap protein identification numbers and multivariate data analysis. Using conservative parameters, 536 different unique proteins were quantitated. Of these, 334 (63%) were present in all samples and represent an MP core proteome. Technical triplicates showed
U2 - 10.1021/pr200901p
DO - 10.1021/pr200901p
M3 - Journal article
C2 - 22329422
VL - 11
SP - 2154
EP - 2163
JO - Journal of Proteome Research
JF - Journal of Proteome Research
SN - 1535-3893
IS - 4
ER -
ID: 48472659