2019
DOI: 10.1016/j.ecoenv.2019.04.063
|View full text |Cite
|
Sign up to set email alerts
|

Induction of cystathionine gamma-lyase expression and metallothionein-1 S-sulfhydration alleviate cadmium-induced cell death in myoblast cells

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
7
0
1

Year Published

2020
2020
2024
2024

Publication Types

Select...
8
1
1

Relationship

1
9

Authors

Journals

citations
Cited by 19 publications
(8 citation statements)
references
References 53 publications
0
7
0
1
Order By: Relevance
“…For example, reactive sulfur species produced by CSE protect human fibroblasts from nickel-stimulation [53]. In vascular tissue, reactive sulfur species produced by CSE protect vascular endothelial cells [9] and myoblast cells [54] from cadmium cytotoxicity. Additionally, CSE overexpression protects against atherosclerosis progression [55], suggesting the importance of vascular CSE in preventing vascular lesions.…”
Section: Discussionmentioning
confidence: 99%
“…For example, reactive sulfur species produced by CSE protect human fibroblasts from nickel-stimulation [53]. In vascular tissue, reactive sulfur species produced by CSE protect vascular endothelial cells [9] and myoblast cells [54] from cadmium cytotoxicity. Additionally, CSE overexpression protects against atherosclerosis progression [55], suggesting the importance of vascular CSE in preventing vascular lesions.…”
Section: Discussionmentioning
confidence: 99%
“…Studies on frogs or chironoma showed an increase in CTH gene expression when exposed to heavy metals [ 38 , 39 ]. Furthermore, in myoblast cells, Zhang and colleagues proposed a pathway underlying the involvement of CTH and the produced H 2 S in cell protection against Cd-induced cell death [ 63 ]. The increased abundance of cystathionine γ-lyase is related to its critical position between glutathione synthesis and the integrated stress response, which helps to protect tissues from ER stress [ 64 ].…”
Section: Discussionmentioning
confidence: 99%
“…Furthermore, in USCP-Zn, the SH content signifcantly decreased (p < 0.05) from 20.46 ± 1.02 μmol/g to 13.82 ± 0.98 μmol/g as compared to SCP-Zn. Te reduction in sulfhydryl content can be ascribed to the impact of ultrasonication on the zinc-protein binding process, resulting in modifed interactions between zinc ions and sulfhydryl groups [73]. Ultrasonication generates mechanical stress and induces conformational changes in the protein structure, leading to the exposure or alteration of zinc-binding sites.…”
Section: Free Sulfhydryl Contentmentioning
confidence: 99%