Alpha-1 antitrypsin, retinol binding protein and keratin 10 alterations in patients with psoriasis vulgaris, a proteomic approach

Abstract

Objective(s):

Psoriasis is an autoimmune disease that appears on the skin. Although psoriasis is clinically and histologically well characterized, its pathogenesis is unknown in detail. The aims of this study were to evaluate the proteome of psoriatic patients' sera and to compare them with those of normal healthy human to find valuable biomarkers.

Materials and Methods:

In a case-control study, twenty cases of white patients with psoriasis vulgaris, 10 males and 10 females and sixteen healthy controls, 8 males and 8 females were enrolled in the study. The serum protein expression patterns obtained after depletion of albumin were compared by using two dimensional gel electrophoresis (2-DE) coupled to MALDI/TOF-TOF to identify disease associated proteins.

Results:

Differential expression of nine protein spots representing four unique proteins including alpha-1 antitrypsin, retinol binding protein, keratin 10 and an unknown protein (with pI 6.47 and molecular weight of 19941 Da), between psoriatic and healthy human serum were found. Furthermore, expression of four new alpha-1 antitrypsin isoforms with different molecular weight and isoelectric point were observed in psoriatic serums in this research for the first time.

Conclusion:

A unique proteomic profiling with abnormal expression of alpha-1 antitrypsin and presence of keratin 10 in sera of psoriasis patients were observed that may constitute new and useful findings of psoriasis and offer a clue to a better understanding of the inflammatory pathway.