Skip to main content
Search

The protein disulfide isomerase code for cell signaling

Published on September 28, 2023   37 min

A selection of talks on Cell Biology

Please wait while the transcript is being prepared...
0:00
I am Francisco Laurindo, Associate Professor at the Heart Institute, University of São Paulo, School of Medicine, in Brazil. Today, we'll talk about protein disulfide isomerase as a code for cell signaling. I used to say it's not just another thiol protein. Oxidative stress is
0:22
not actually a balance between pro and anti oxidant mechanisms, as it's usually discussed. Nowadays, we know that oxidative stress is actually the disequilibrium of redox signaling. Redox signaling occurs through receptors such as cysteine thiols or metals. Today we'll focus on cysteine thiols and as you know, cysteine is a very important amino acid to promote the tertiary structure of proteins. We know nowadays that cysteine have several oxidative forms, as we'll see in the next slide, which we analyze the landscape of thiol modifications in redox signaling, we have oxidant reactions and in the upper part, disulphide exchange reactions. As you can see, the thiol group, the SH, are also called sulfide group. Normally it's ionized to its thiolate, an ion here as minus and this confers enhanced reactivity towards oxidants such as hydrogen peroxide for example and this promotes several oxo forms or oxidized forms like sulfenic acid, sulfenic acid, and sulphonic acid. Sulphonic and sulfenic are reversible, while sulphonic is irreversible modification. There are also several other modifications like sulfenamides, sulfenyl amides and persulfide, which confer a significant amount of versatility to thiol groups.

Quiz available with full talk access. Request Free Trial or Login.

Show
Hide

The protein disulfide isomerase code for cell signaling

Embed in course/own notes