Jena. On June 5, our Scientific Director, Prof. Dr. Dario Riccardo Valenzano, cordially invites you to the 5th lecture in the “FLI Inauguration Lecture Series” at 3 p.m. We are honored to have Prof. Dr. Janine Kirstein present her research titled “Protein folding challenges in aging and disease” in the seminar room “Nucleus”.
Janine and her team study protein folding challenges and their role in aging and pathologies. A focus is on amyloid proteins whose aggregation is associated with the development of late age of onset neurodegenerative diseases.
They study the complete folding landscape of the amyloid proteins mutant Huntingtin, Abeta and tau in vitro and in vivo in the nematode C. elegans. For that, her lab has established neurodegenerative disease models for several amyloid proteins. Using these C. elegans models, they could show that the aggregation of amyloid proteins is associated with an early decline of neuronal activity and observed that certain neurons are more vulnerable towards the expression of these disease proteins then others and that this is specific for distinct amyloid proteins.
Their aim is to comprehensively understand how different nodes of the proteostasis network can be modulated to counteract the proteotoxicity of aggregating amyloid proteins. The proteostasis network is composed of molecular chaperones and proteolytic pathways including the proteasome and the autophagic flux. Her lab has developed several sensors to study the reciprocal relationship between molecular chaperones, the proteasome and the autophagic flux to cope with amyloid proteins as aging progresses. They could show that autophagy is activated when chaperone-mediated folding processes fail. Her lab has further identified specific chaperones that can suppress e.g. Huntingtin aggregation and reverse the aggregation by disaggregating Huntingtin fibrils.
Janine is a W3-professor for Biochemistry of Aging at the Friedrich Schiller University Jena, an Allen Distinguished Investigator, project leader in several DFG-funded consortia and member of the DFG study section “Biochemistry”.
