Identity, origin, environmental conditions (climate, soil structure, neighboring organisms) as well as harvest, processing and storage conditions of food are reflected in the composition of the whole of the proteins – the so-called proteomes. Proteom profiles can give very detailed information about the quality of food. An important technique for the preparation of proteome profiles is mass spectrometry, with which thousands of proteins, e.g. from truffles, can be recorded qualitatively and quantitatively. By comparing the proteome profiles of reference samples with samples exposed to defined changes, markers can be identified that are related to the changes, e.g. long drying periods before harvesting or improper storage. The aim is to identify identity-, origin- and quality-influencing protein markers in order to quickly detect fraud and to better assess the quality of food in the future.

References to specific research topics:

Identifizierung von Protein-Markern mit Proteomics

Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production.
Rösch K, Kwiatkowski M, Hofmann S, Schöbel A, Grüttner C, Wurlitzer M, Schlüter H, Herker E.
Cell Reports. 2016; 16:3219-31. IF: 7,87

Disseminated Tumor Cells Persist in the Bone Marrow of Breast Cancer Patients through Sustained Activation of the Unfolded Protein Response.
Bartkowiak K, Kwiatkowski M, Buck F, Gorges TM, Nilse L, Assmann V, Andreas A, Müller V, Wikman H, Riethdorf S, Schlüter H, Pantel K.
Cancer Res. 2015 Dec 15;75(24):5367-77. IF: 9,33

High molecular mass assemblies of amyloid-ß oligomers bind prion protein in Alzheimer diseased brain.
Dohler F, Sepulveda-Falla D, Krasemann S, Altmeppen H, Schlüter H.  Hildebrand D, Zerr I, Matschke J, Glatzel M.
Brain 2014; 137:873-86. IF: 9,91

MALDI mass spectrometric imaging based identification of clinically relevant signals in prostate cancer using large-scale tissue microarrays.
Steurer S, Borkowski C, Odinga S, Buchholz M, Koop C, Huland H, Becker M, Witt M, Trede D, Omidi M, Kraus O, Bahar AS, Seddiqi AS, Singer JM, Kwiatkowski M, Trusch M, Simon R, Wurlitzer M, Minner S, Schlomm T, Sauter G, Schlüter H.
Int J Cancer. 2013; 133:920-8. IF: 5,44

Probengewinnung durch kaltes & schonendes Verdampfen von Geweben mit PIRL

Homogenization of tissues via picosecond-infrared laser (PIRL) ablation: Giving a closer view on the in-vivo composition of protein species as compared to mechanical homogenization.
Kwiatkowski M, Wurlitzer M, Krutilin A, Kiani P, Nimer R, Omidi M, Mannaa A, Bussmann T, Bartkowiak K, Kruber S, Uschold S, Steffen P, Lübberstedt J, Küpker N, Petersen H, Knecht R, Hansen NO, Zarrine-Afsar A, Robertson WD, Miller RJ, Schlüter H.
J Proteomics. 2016 Feb 16;134:193-202. IF: 3,89

Ultrafast extraction of proteins from tissues using desorption by impulsive vibrational excitation.
Kwiatkowski M, Wurlitzer M, Omidi M, Ren L, Kruber S, Nimer R, Robertson WD, Horst A, Miller RJ, Schlüter H.
Angew Chem Int Ed Engl. 2015 Jan 2;54(1):285-8. IF: 11,34


Institut für Klinische Chemie und Laboratoriumsmedizin

Prof. Dr. Hartmut Schlüter
Massenspektrometrische Proteomanalytik
Campus Forschung, N27 Raum 00.008
Universitätsklinikum Hamburg-Eppendorf
Martinistr. 52
20246 Hamburg

Tel: +4940 / 7410-58795
Gruppe Proteom-Analytik des Universitätsklinikums Hamburg-Eppendorf