About: Cystine is a research topic. Over the lifetime, 5228 publications have been published within this topic receiving 156941 citations. The topic is also known as: (-)-cystine & cystine.
TL;DR: In this article, a reduction agent was used to destroy the excess performic acid before the initial reaction, and the subsequent exposure of cysteic acid residues to bromine would not be likely to be detrimental.
TL;DR: From a mechanistic standpoint, oxidative stress may be better defined as a disruption of redox signaling and control and adoption of such a definition could redirect research to identify key perturbations of red Oxidative stress-related disease processes and lead to new treatments for oxidative stressed disease processes.
Abstract: Oxidative stress is often defined as an imbalance of pro-oxidants and antioxidants, which can be quantified in humans as the redox state of plasma GSH/GSSG. Plasma GSH redox in humans becomes oxidized with age, in response to oxidative stress (chemotherapy, smoking), and in common diseases (type 2 diabetes, cardiovascular disease). However, data also show that redox of plasma GSH/GSSG is not equilibrated with the larger plasma cysteine/cystine (Cys/CySS) pool, indicating that the "balance" of pro-oxidants and antioxidants cannot be defined by a single entity. The major cellular thiol/disulfide systems, including GSH/GSSG, thioredoxin- 1 (-SH2/-SS-), and Cys/CySS, are not in redox equilibrium and respond differently to chemical toxicants and physiologic stimuli. Individual signaling and control events occur through discrete redox pathways rather than through mechanisms that are directly responsive to a global thiol/disulfide balance such as that conceptualized in the common definition of oxidative stress. ...
TL;DR: In this paper, the authors have isolated cDNA encoding the transporter for system xc- from mouse activated macrophages by expression in Xenopus oocytes, and the sequence analysis revealed that one is identical with the heavy chain of 4F2 cell surface antigen (4F2hc) and the other is a novel protein of 502 amino acids with 12 putative transmembrane domains.
TL;DR: Glutamate-induced cytotoxicity in N18-RE-105 cells is due to inhibition of cystine uptake, resulting in lowered glutathione levels leading to oxidative stress and cell death.