Protein Folding Diseases

3 Pages
Unlock Document

Western University
Anatomy and Cell Biology
Anatomy and Cell Biology 4429A
Paul Walton

Alpha1AntitrypsinIn the ER it is made with three carbohydrate chains Carbohydrate chains are recognized by calnexin Calnexinfound in the ER once the carbohydrate chains are put on in the ER it does not letproteins leave the ER if they are misfolded Calnexin protease recognizes a mutation and a typical mutation is the E342K mutation Typical mutationE342K mutation acidic group is changed to a basic charge and eventually it is dragged out of the ER and will be sent to the ERAD pathway and then to the proteosome This mutation causes the protein to aggregate What is the problem with this As we take it our of the ER and send it to the protesome the protein inhibits the protesomal degradation pathway and it could start to aggregate This is a gain of functionthe gain of inhibition of the proteosome This is a disease characterized by sending something to the proteosome which inhibits it and destroys the compartmentLiver cells lose the ability to degrade proteins through the proteosome As cells grow old they must be replaced Over a lifetime the liver now becomes challenged and goes through unnecessary rounds of mitosis This results in hypertrophy As these cells accumulate undigested protein they die and the cells that replace them have t
More Less

Related notes for Anatomy and Cell Biology 4429A

Log In


Don't have an account?

Join OneClass

Access over 10 million pages of study
documents for 1.3 million courses.

Sign up

Join to view


By registering, I agree to the Terms and Privacy Policies
Already have an account?
Just a few more details

So we can recommend you notes for your school.

Reset Password

Please enter below the email address you registered with and we will send you a link to reset your password.

Add your courses

Get notes from the top students in your class.