Skip to main content
Fig. 6 | Molecular Medicine

Fig. 6

From: The cholesteryl-ester transfer protein isoform (CETPI) and derived peptides: new targets in the study of Gram-negative sepsis

Fig. 6

Analysis of the 69 kDa and 67 kDa bands identified by western blotting that correspond to CETPI and peptides derived from its C-terminal sequence. A Alignment parameters of peptides identified by HPLC-mass spectrometry contained in the 69 kDa CETPI band employing Homo sapiens CETP sequences (GenBank: AAV38867.1). Peptides identified by HPLC-mass spectrometry are highlighted in the CETP sequence. B Top: Immunodetection of CETPI in plasmas isolated from control subjects and patients before and after albumin depletion. Down: Same membrane stained with Ponceau S. Control plasma samples (lanes 1–3). Plasma samples from sepsis patient (lanes 4–6). Plasma samples from septic shock patient (lanes 7–9). Albumin-depleted plasma samples (lanes 2, 5, 8). Albumin fraction recovered after elution of plasmas through the column (lanes 3, 6, 9). C Protease activity prediction upon the C-terminal domain of CETPI employing Procleave (Li et al. 2020), indicates predicted cleaved sites. D Protease activity of plasmas obtained from control subjects (n = 21), infection (n = 28), sepsis (n = 25), and septic shock patients (n = 25). Data are shown as median with IQR. *p < 0.05, **p < 0.01

Back to article page