PROTEIN CONFORMATION DISEASES (BMB 518/CAMB 615)

Fall, every year
204 Stellar-Chance Labs
W, 3 - 5 p.m.

Instructors: Argon and Ischiropoulos

Prerequistes: BIOM 600 or equivalent

Protein misfolding and aggregation has been associated with a number of human diseases, ranging from Alzhemier's and Parkinson's disease to Respiratory Distress Syndrome, alpha(1)-antitrypsin deficiency and "mad cow" disease. This course will include lectures, directed readings and student presentations to cover seminal and current papers on the cell biology of conformational diseases including topics such as aggresome formation, protein degradation pathways (proteosome vs ER-associated degradation), effects of protein aggregation on cell function and mutations which lead to autosomal dominant diseases.

Sample Schedule

1

Introduction: Course structure and administration
Principles of protein folding  

Argon

2

Protein folding in the cell  

Argon

3

Protein folding in the cell  

Argon

4

Prion diseases 

Kal

5

Proteomic methods

Speicher

6

Protein aggregation in neurodegenerative diseases

Giasson

7

Protein aggregation in cells / Systemic amyloidosis

Argon 

8

Misfolding of cell surface receptors

Rubenstein

9

Pulmonary surfactant proteins and diseases

Beers

10 - end

Students' Presentations

No textbook will be used. Each instructor will assign 1-2 papers that will be discussed in class.

Each students will pick a topic, e.g. a disease, to cover, assign papers to the class and will be expected to lead a discussion.

Grades will be based on the quality of the student's participation throughout the course.