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Cystamine attenuates lupus-associated apoptosis of ventricular tissue by suppressing both intrinsic and extrinsic pathways.

Tzang BS, Hsu TC, Kuo CY, Chen TY, Chiang SY, Li SL, Kao SH - J. Cell. Mol. Med. (2012)

Bottom Line: In addition, cystamine reduced level of Fas and inhibited activation of caspase-8.Cystamine also increased level of Bcl-2 and phosphorylation of Bad, and decreased level of Bad and truncated Bid (tBid).Therefore, cystamine is considered beneficial to alleviating lupus-associated cardiac damages.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, School of Medicine, Chung Shan Medical University, Taichung City, Taiwan.

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Related in: MedlinePlus

Effects of cystamine treatment on expression level of pro-apoptotic proteins and survival signal. LV samples were obtained from NZB/W-F1 mice and Balb/c mice, which were treated with PBS or cystamine as described in Materials and methods. (A) Immunoblot for expression level of Bcl-2, Bad, phosphorylated Bad (p-Bad) and truncated Bid (tBid). (B) Quantitative data for tested targets from NZB/W-F1 mice were obtained by densitometric analysis and presented as ratio of the tested protein/α-tubulin (α-TN). (C) Immunoblot for level of phosphorylation of Erk1/2 (p-Erk1/2), quantitative data were obtained by densitometric analysis and presented as ratio of p-Erk1/2/α-TN. *P < 0.05 as compared to PBS control. n.s.: not significant.
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fig05: Effects of cystamine treatment on expression level of pro-apoptotic proteins and survival signal. LV samples were obtained from NZB/W-F1 mice and Balb/c mice, which were treated with PBS or cystamine as described in Materials and methods. (A) Immunoblot for expression level of Bcl-2, Bad, phosphorylated Bad (p-Bad) and truncated Bid (tBid). (B) Quantitative data for tested targets from NZB/W-F1 mice were obtained by densitometric analysis and presented as ratio of the tested protein/α-tubulin (α-TN). (C) Immunoblot for level of phosphorylation of Erk1/2 (p-Erk1/2), quantitative data were obtained by densitometric analysis and presented as ratio of p-Erk1/2/α-TN. *P < 0.05 as compared to PBS control. n.s.: not significant.

Mentions: Proapoptotic proteins involved in intrinsic apoptosis pathway including Bcl-2, Bad and tBid were investigated. As shown in Figure 5A, cystamine treatment increased levels of Bcl-2 and phosphorylated Bad (p-Bad) parallel to decreases in levels of Bad and tBid. Quantitative analysis revealed that ratios of Bcl-2/α-TN and p-Bad/α-TN were increased from 0.17 ± 0.02 to 0.39 ± 0.05 (P < 0.05) and from 0.42 ± 0.02 to 0.52 ± 0.54 (P < 0.05), respectively, in LV tissues of NZB/W-F1 treated with cystamine compared with those of PBS-treated ones (Fig. 5B). Significantly decreased ratios of Bad/α-TN (0.42 ± 0.05 to 0.23 ± 0.04; P < 0.005) and tBid/α-TN (0.46 ± 0.06 to 0.23 ± 0.11; P < 0.05) were discovered in LV tissues of NZB/W-F1 mice in comparison with PBS–treated group (Fig. 5B). In addition, slight effect of cystamine on levels of tested proapoptotic proteins in LV tissues of Balb/c mice was discovered (Fig. 5A).


Cystamine attenuates lupus-associated apoptosis of ventricular tissue by suppressing both intrinsic and extrinsic pathways.

Tzang BS, Hsu TC, Kuo CY, Chen TY, Chiang SY, Li SL, Kao SH - J. Cell. Mol. Med. (2012)

Effects of cystamine treatment on expression level of pro-apoptotic proteins and survival signal. LV samples were obtained from NZB/W-F1 mice and Balb/c mice, which were treated with PBS or cystamine as described in Materials and methods. (A) Immunoblot for expression level of Bcl-2, Bad, phosphorylated Bad (p-Bad) and truncated Bid (tBid). (B) Quantitative data for tested targets from NZB/W-F1 mice were obtained by densitometric analysis and presented as ratio of the tested protein/α-tubulin (α-TN). (C) Immunoblot for level of phosphorylation of Erk1/2 (p-Erk1/2), quantitative data were obtained by densitometric analysis and presented as ratio of p-Erk1/2/α-TN. *P < 0.05 as compared to PBS control. n.s.: not significant.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC3822980&req=5

fig05: Effects of cystamine treatment on expression level of pro-apoptotic proteins and survival signal. LV samples were obtained from NZB/W-F1 mice and Balb/c mice, which were treated with PBS or cystamine as described in Materials and methods. (A) Immunoblot for expression level of Bcl-2, Bad, phosphorylated Bad (p-Bad) and truncated Bid (tBid). (B) Quantitative data for tested targets from NZB/W-F1 mice were obtained by densitometric analysis and presented as ratio of the tested protein/α-tubulin (α-TN). (C) Immunoblot for level of phosphorylation of Erk1/2 (p-Erk1/2), quantitative data were obtained by densitometric analysis and presented as ratio of p-Erk1/2/α-TN. *P < 0.05 as compared to PBS control. n.s.: not significant.
Mentions: Proapoptotic proteins involved in intrinsic apoptosis pathway including Bcl-2, Bad and tBid were investigated. As shown in Figure 5A, cystamine treatment increased levels of Bcl-2 and phosphorylated Bad (p-Bad) parallel to decreases in levels of Bad and tBid. Quantitative analysis revealed that ratios of Bcl-2/α-TN and p-Bad/α-TN were increased from 0.17 ± 0.02 to 0.39 ± 0.05 (P < 0.05) and from 0.42 ± 0.02 to 0.52 ± 0.54 (P < 0.05), respectively, in LV tissues of NZB/W-F1 treated with cystamine compared with those of PBS-treated ones (Fig. 5B). Significantly decreased ratios of Bad/α-TN (0.42 ± 0.05 to 0.23 ± 0.04; P < 0.005) and tBid/α-TN (0.46 ± 0.06 to 0.23 ± 0.11; P < 0.05) were discovered in LV tissues of NZB/W-F1 mice in comparison with PBS–treated group (Fig. 5B). In addition, slight effect of cystamine on levels of tested proapoptotic proteins in LV tissues of Balb/c mice was discovered (Fig. 5A).

Bottom Line: In addition, cystamine reduced level of Fas and inhibited activation of caspase-8.Cystamine also increased level of Bcl-2 and phosphorylation of Bad, and decreased level of Bad and truncated Bid (tBid).Therefore, cystamine is considered beneficial to alleviating lupus-associated cardiac damages.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, School of Medicine, Chung Shan Medical University, Taichung City, Taiwan.

Show MeSH
Related in: MedlinePlus