Open Access Research

Urine proteome of autosomal dominant polycystic kidney disease patients

Magda Bakun1, Mariusz Niemczyk2, Dominik Domanski1, Radek Jazwiec1, Anna Perzanowska1, Stanislaw Niemczyk3, Michal Kistowski1, Agnieszka Fabijanska1, Agnieszka Borowiec1, Leszek Paczek2 and Michal Dadlez14*

Author Affiliations

1 Mass Spectrometry Laboratory, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5A, 02-106, Warsaw, Poland

2 Department of Immunology, Transplant Medicine and Internal Medicine, Medical University of Warsaw, Warsaw, Poland

3 Department of Internal Diseases, Nephrology and Dialysis; Military Institute of Medicine, Warsaw, Poland

4 Department of Biology, Warsaw University, Warsaw, Poland

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Clinical Proteomics 2012, 9:13  doi:10.1186/1559-0275-9-13

Published: 11 December 2012



Autosomal dominant polycystic kidney disease (ADPKD) is responsible for 10% of cases of the end stage renal disease. Early diagnosis, especially of potential fast progressors would be of benefit for efficient planning of therapy. Urine excreted proteome has become a promising field of the search for marker patterns of renal diseases including ADPKD. Up to now however, only the low molecular weight fraction of ADPKD proteomic fingerprint was studied. The aim of our study was to characterize the higher molecular weight fraction of urinary proteome of ADPKD population in comparison to healthy controls as a part of a general effort aiming at exhaustive characterization of human urine proteome in health and disease, preceding establishment of clinically useful disease marker panel.


We have analyzed the protein composition of urine retentate (>10‚ÄČkDa cutoff) from 30 ADPKD patients and an appropriate healthy control group by means of a gel-free relative quantitation of a set of more than 1400 proteins. We have identified an ADPKD-characteristic footprint of 155 proteins significantly up- or downrepresented in the urine of ADPKD patients. We have found changes in proteins of complement system, apolipoproteins, serpins, several growth factors in addition to known collagens and extracellular matrix components. For a subset of these proteins we have confirmed the results using an alternative analytical technique.


Obtained results provide basis for further characterization of pathomechanism underlying the observed differences and establishing the proteomic prognostic marker panel.

ADPKD; Urine proteome; Differential proteomics; Mass spectrometry; iTRAQ; MRM