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1.
Figure 7

Figure 7. From: Proteomic analysis of endothelial cold-adaptation.

Cytoskeletal proteins that were significantly up- or down-regulated at 25°C.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
2.
Figure 1

Figure 1. From: Proteomic analysis of endothelial cold-adaptation.

Glycolytic proteins that were significantly up- or down-regulated at 25°C.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
3.
Figure 2

Figure 2. From: Proteomic analysis of endothelial cold-adaptation.

Proteins that participate in redox reactions and were significantly up- or down- regulated at 25°C.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
4.
Figure 5

Figure 5. From: Proteomic analysis of endothelial cold-adaptation.

Proteins that may regulate gene expression and were significantly up- or down-regulated at 25°C.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
5.
Figure 6

Figure 6. From: Proteomic analysis of endothelial cold-adaptation.

Response-to-stress proteins that were significantly up- or down-regulated at 25°C. (Note: the complete list for Oxidoreductase Activity is in Figure 2).

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
6.
Figure 4

Figure 4. From: Proteomic analysis of endothelial cold-adaptation.

Effect of cold-adaptation (25°C/72 h) and cold storage (0°C/48 h) on thioredoxin (Trx), thioredoxin reductase (TrxR) and GST (glutathione S transferase) activity. (A) Cold-adaptation increases Trx activity before or after 0°C storage (*P < 0.05 vs. 37°C control; **P < 0.001 vs. 37°C + 0°C/48 h + RW; n = 5 experiments). (B) TrxR activity is greater in cold-adapted cells following 0°C storage and rewarming (*P < 0.05 vs. 37°C + 0°C/48 h + RW; n = 4 experiments). (C) GST activity in cold-adapted cells following 0°C storage and rewarming exceeds that of control cells (*P < 0.05 vs. 37°C + 0°C/48 h + RW; n = 4 experiments). Open bars represent cell cold-adapted at 25°C for 72 h; closed bars represent cells maintained at 37°C for 72 h.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
7.
Figure 3

Figure 3. From: Proteomic analysis of endothelial cold-adaptation.

Effect of cold-adaptation (25°C/72 h) and cold storage (0°C/48 h) on protein and non-protein thiols. (A) Cold-adaptation prevents the significant loss of protein thiols (PSH) that occurs during cold storage/rewarming (*P < 0.01 vs. 37°C control; ** P < 0.001 vs. 37°C+0°C+RW; n = 5 experiments), possibly by the reduction of oxidized proteins during the rewarming phase (+P < 0.05 vs. 25°C+0°C; n = 5 experiments). (B) Cold-adapted cells have a significantly higher level of glutathiolated protein (PSSG) than non-adapted cells (37°C) following cold storage/rewarming (**P < 0.05 vs. 37°C+0°C+RW; n = 5 experiments). (C). Cold-adaptation attenuates the increase in GSSG/tGSH, indicative of oxidative stress, that occurs during cold storage/rewarming (*P < 0.001 vs. 37°C control; **P < 0.001 vs. 37°C+0°C+RW; n = 3 experiments). Open bars represent cell cold-adapted at 25°C for 72 h; closed bars represent cells maintained at 37°C for 72 h.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
8.
Figure 8

Figure 8. From: Proteomic analysis of endothelial cold-adaptation.

Hypothetical changes in the energy metabolism of cold-adapted endothelial cells. The rate-limiting enzyme, phosphofructokinase (PFK), was down-regulated at 25°C and potentially redirects the carbohydrate flux into the pentose phosphate pathway for increased reduction of NADP+ to NADPH. Aldolase (ALDOA, ALDOC), glyceraldehyde phosphate dehydrogenase (GAPDH), phosphoglycerate kinase (PGK1), enolase (ENO1, ENO2, ENO3), pyruvate kinase (PKM2). were up-regulated at 25°C, implicating a possible inflow of intermediate metabolites, like glycerol, into the glycolytic pathway. The increase in lactate dehydrogenase (LDHA, LDHAL6A, LDHAL6B) suggests that cold-adapted endothelium may have a greater reliance on aerobic glycolysis and a lesser reliance on mitochondrial respiration for their energy requirements. 6-PGL, 6-phosphoglucono-δ-lactone; 6-PG, 6-phosphogluconate; G-3-P, glycerol-3-phosphate; DHAP, dihydroxyacetone phosphate; 1,3-DPG, 1,3-diphosphoglycerate; 3-PG, 3-phosphoglycerate; 2-PG, 2-phosphoglycerate; PEP, phosphoenolpyruvate.

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.
9.
Figure 9

Figure 9. From: Proteomic analysis of endothelial cold-adaptation.

Endothelial adaptive response to moderate hypothermia (25°C/72 h). See Conclusions for details. Thioredoxin (Trx), thioredoxin reductase (TrxR), tyrosine hydroxylase (TH), reduced glutathione (GSH), glutathione S-transferase (GST), protein disulfide isomerase (PDIA1 and 4), reduced protein thiols (P(SH)2), protein disulfide (PSSP), glutathionylated protein (P-SSG), oxidized protein (P-S•), S-adenosylhomocysteine hydrolase (SAHH), peroxiredoxin 1 (Prx1), aldehyde dehydrogenase (ALDH), nicotinamide phosphoribosyltransferase (Nampt), reduced/oxidized nicotinamide adenine dinucleotide phosphate (NADPH/NADP+), fatty acid synthase (FAS), ribonucleotide reductase M1 (RRM1), inosine-5'-monophosphate dehydrogenase 2 (IMPDH2), phosphofructokinase (PFK), pentose phosphate pathway (PPP), histone (H2AV, H2BFC, H2BFQ), histone binding proteins (NASP or nuclear autoantigenic sperm protein), chromatin binding proteins (High-mobility group protein B1 (HMGB1), high-mobility group protein 1-like10 (HMG1L10), barrier to autointegration factor 1 (BANF1)), RNA binding motif protein 3 (RBM3), Y-box binding protein 1 (YB-1), cold-shock domain protein A (CSDA), prohibitin (PHB), enolase 1 (ENO1), lethal(3)malignant brain tumor-like 2 protein (L3MBTL2), heterogeneous nuclear ribonucleoprotein D-like (HNRNPDL), Zinc finger protein 224 (ZNF224).

Michael AJ Zieger, et al. BMC Genomics. 2011;12:630-630.

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