Hydrogen peroxide enhanced Ca2+-activated BK currents and promoted cell injury in human dermal fibroblasts

Life Sciences ◽  
2012 ◽  
Vol 90 (11-12) ◽  
pp. 424-431 ◽  
Author(s):  
Bing Feng ◽  
Wen-Lei Ye ◽  
Lai-ji Ma ◽  
Yun Fang ◽  
Yan-Ai Mei ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cell Injury ◽  
Dermal Fibroblasts ◽  
Human Dermal Fibroblasts

Protective Effects and Mechanisms of Pourthiaea villosa (Thunb.) Decne. Extract on Hydrogen Peroxide-Induced Skin Aging in Human Dermal Fibroblasts

2019 ◽  
Vol 22 (8) ◽  
pp. 841-850
Author(s):  
Sun-Il Choi ◽  
Jong Seok Lee ◽  
Sarah Lee ◽  
Bong-Yeon Cho ◽  
Seung-Hyun Choi ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Skin Aging ◽  
Dermal Fibroblasts ◽  
Protective Effects ◽  
Human Dermal Fibroblasts

scholarly journals Polyphenol-Rich Strawberry Extract Protects Human Dermal Fibroblasts against Hydrogen Peroxide Oxidative Damage and Improves Mitochondrial Functionality

Molecules ◽  
2014 ◽  
Vol 19 (6) ◽  
pp. 7798-7816 ◽  
Author(s):  
Francesca Giampieri ◽  
José Alvarez-Suarez ◽  
Luca Mazzoni ◽  
Tamara Forbes-Hernandez ◽  
Massimiliano Gasparrini ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Damage ◽  
Dermal Fibroblasts ◽  
Human Dermal Fibroblasts

scholarly journals Endoplasmic reticulum resident proteins of normal human dermal fibroblasts are the major targets for oxidative stress induced by hydrogen peroxide

2002 ◽  
Vol 366 (3) ◽  
pp. 825-830 ◽  
Author(s):  
Dennis van der VLIES ◽  
Eward H.W. PAP ◽  
Jan Andries POST ◽  
Julio E. CELIS ◽  
Karel W.A. WIRTZ
Keyword(s):  
Hydrogen Peroxide ◽  
Endoplasmic Reticulum ◽  
Laser Scanning ◽  
Dermal Fibroblasts ◽  
Laser Scanning Microscopy ◽  
Confocal Laser ◽  
Human Dermal Fibroblasts ◽  
Normal Human ◽  
Covalently Linked ◽  
Normal Human Dermal Fibroblasts

The membrane-permeable fluorescein-labelled tyramine conjugate (acetylTyrFluo) was used to identify the proteins of normal human dermal fibroblasts most susceptible to oxidation by hydrogen peroxide [Van der Vlies, Wirtz and Pap (2001) Biochemistry 40, 7783—7788]. By exposing the cells to H2O2 (0.1mM for 10min), TyrFluo was covalently linked to target proteins. TyrFluo-labelled and [35S]Met-labelled cell lysates were mixed and subjected to two-dimensional PAGE. After Western blotting the 35S-labelled proteins were visualized by autoradiography and the TyrFluo-labelled proteins by using anti-fluorescein antibody. The TyrFluo-labelled proteins were matched with the 35S-labelled proteins and identified by comparison with our mastermap of proteins. Protein disulphide isomerase (PDI), IgG-binding protein (BiP), calnexin, endoplasmin and glucose-regulated protein 58 (endoplasmic reticulum protein 57/GRP58) were identified as targets of oxidation. All these proteins reside in the endoplasmic reticulum and are part of the protein folding machinery. In agreement, confocal laser scanning microscopy showed co-localization of TyrFluo-labelled proteins and the KDEL receptor ERD-2, a marker for the endoplasmic reticulum.

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