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(A)
CPLL
beads
Elution 1
Elution 2
Elution 3
(C)
(D)
(B)
FIGURE 3 2-DE analysis of sequential elution of human plasma captured proteins by CPLL. (A) Initial untreated sample;
(B) protein desorption from beads using 1 M sodium chloride; (C) protein desorption by 2 M thiourea, 7.7 M urea, 4% CHAPS;
(D) protein desorption by 8 M urea, 2% CHAPS, 0.1 M citric acid. The latter completed the desorption of all captured proteins.
(Adapted from Leger et al. 49 ).
to 2-DE images of each fraction was assessed
throughout the analyses of all samples.
In addition to biological
plaques was already known and con
rmed in
this study, novel low-abundance proteins were
detected correlating very well with investigated
biological alterations. These proteins were moe-
sin, protein kinase C delta-binding protein, alde-
hyde dehydrogenase, and an unknown isoform
of heat shock protein 27, all of them involved in
atherosclerotic mechanisms. Interestingly, it was
discovered that the heat shock protein 27 isoform
signed the transition from stable to unstable
plaque. The discovered low-abundance proteins
in conjunction with the stage of atherosclerotic
plaque support the hypothesis of potential
protein markers that need to be validated.
Also 2D-DIGE was combined with CPLL-
treated samples to investigate the capability of
fluids, CPLL-treated
tissue extracts have been analyzed by 2-DE
with interesting results. In a recent report,
Malaud et al. 56 compared human carotid athero-
sclerotic plaque extracts from endarterectomy.
The aim of the study was to determine possible
differences between stable and unstable plaques,
an important notion for therapy. 2-DE analysis
revealed clear differences for some protein
expression assessed by spot dimension and
identi
ed by mass spectrometry. While the
expression difference found for hemoglobin
beta-chain and heat shock protein 27 between
noncomplicated and hemorrhagic complicated
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