Proteomic Analysis of Polypeptides Captured from Blood during Extracorporeal Albumin Dialysis in Patients with Cholestasis and Resistant Pruritus
2011

Proteomic Analysis of Blood Proteins in Patients Undergoing Albumin Dialysis

Sample size: 5 publication 10 minutes Evidence: moderate

Author Information

Author(s): Gay Marina, Pares Albert, Carrascal Montserrat, Bosch-i-Crespo Pau, Gorga Marina, Mas Antoni, Abian Joaquin

Primary Institution: CSIC/UAB Proteomics Laboratory, Instituto de Investigaciones Biomédicas de Barcelona-Consejo Superior de Investigaciones Científicas/Institut d'investigacions Biomèdiques August Pi i Sunyer (IIBB-CSIC/IDIBAPS), Bellaterra, Spain

Hypothesis

The study aims to characterize the peptides and proteins captured by the MARS system from patients' blood during albumin dialysis.

Conclusion

The study identified over 1,500 peptide sequences corresponding to 144 proteins, including several that may have therapeutic or adverse effects related to albumin dialysis.

Supporting Evidence

  • Over 1,500 peptide sequences corresponding to 144 proteins were identified.
  • Five proteins were confirmed to be removed by the dialysis procedure using targeted selected-reaction monitoring MS/MS.
  • SLURP1 levels were significantly higher in cholestatic patients than in controls.

Takeaway

Doctors used a special machine to clean blood from patients with liver problems, and they found many proteins that could help understand how the treatment works.

Methodology

The study used a shotgun proteomic approach combined with targeted mass spectrometry to analyze proteins captured by the MARS system.

Limitations

The study's findings may be limited by the complexity of the albumin matrix and the low concentration of some proteins.

Participant Demographics

Patients included four with cholestasis and resistant pruritus and one with Wilson's disease.

Statistical Information

P-Value

p<0.005

Statistical Significance

p<0.005

Digital Object Identifier (DOI)

10.1371/journal.pone.0021850

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication