Sie sind hier: FRIAS School of Life Sciences … Veranstaltungen Probevorträge - Besetzung der …

Probevorträge - Besetzung der W2-Professur für Medical Proteomics

Wann 12.02.2013
von 14:00 bis 15:00
Wo FRIAS Seminarraum, Albertstrasse 19, 79104 Freiburg
Kontakttelefon +49 (0)761-203 97418
Teilnehmer universitätsoffen - open for University employees
Termin übernehmen vCal


Im Zusammenhang mit der Besetzung der W2-Professur für Medical Proteomics finden folgende Vorträge statt:


14.00 Uhr - Vortrag von René P. Zahedi
"Quantitative proteomics for targeting human diseases"

14.30 Uhr - Vortrag von Jörn Dengjel
"Skin proteomics in health and disease"





Quantitative proteomics for targeting human diseases

René P. Zahedi
Leibniz-Institut für Analytische Wissenschaften, Dortmund
14.00 Uhr

Many diseases are related to alterations in protein expression and/or post-translational modification (PTM) states, rendering MS-based proteomics a powerful tool to study underlying mechanisms and monitor patient samples. In the past years, we developed and established a variety of analytical strategies allowing for a thorough characterization of “complete” proteomes and PTM patterns from minute sample amounts in a reproducible manner. We utilize these methods to study changes in model systems and patient samples, e.g. generated a comprehensive and quantitative proteomic map of human platelets which serves as starting point for disease-related follow-up studies.



Skin proteomics in health and disease

Jörn Dengjel
FRIAS-LifeNet, Universität Freiburg
14.30 Uhr

The skin protects the entire organism against external dangers, including physical, chemical and microbial insults. The two major cell types in human skin are fibroblasts and keratinocytes. We have established quantitative mass spectrometry-based proteomics protocols to study protein dynamics of primary human skin cells in health and disease. Firstly, I will present a comprehensive profiling of the proteome of primary human keratinocytes with respect to gender, age, and skin localization. Compared to model cell lines the proteomes of keratinocytes exhibit high consistency. Secondly, using epidermolysis bullosa as model a disease proteomics approach was taken to study differences in the microenvironment of primary human skin fibroblasts. Loss of collagen VII had a global impact on the cellular microenvironment and was associated with proteome alterations highly relevant for disease pathogenesis including decrease of basement membrane components, increase of dermal matrix proteins, TGF-b, and metalloproteases, but not higher protease activity. The definition of the proteome of fibroblast microenvironment and its plasticity in health and disease identified novel disease mechanisms and potential targets of intervention.