Improved diagnosis of psoriasis, by new biomarkers, is required for evaluating the progression rate of the disease and the
response to treatment. Haptoglobin (Hpt), a glycoprotein secreted by hepatocytes and other types of cells including
keratinocytes, was found with glycan changes in psoriasis and other diseases. We previously reported that Hpt isolated from
plasma of psoriatic patients is more fucosylated than Hpt of healthy subjects. The aim of this study was to compare the
glycosylation pattern of Hpt isolated from skin scales or plasma of patients with psoriasis with that of Hpt from cornified
epidermal layer or plasma of healthy subjects. High performance liquid chromatography analysis of the glycans isolated
from the protein backbone revealed that glycan patterns from skin and plasma of patients were similar, and mostly
displayed quantitative rather than qualitative differences from normal pattern. Biotin-labeled lectins were used to evaluate
quantitative differences in the glycoforms of Hpt from plasma and psoriatic skin scales. Hpt from skin and plasma of patients
showed more fucosylated and branched glycans than Hpt from plasma of healthy subjects. Tryptic glycopeptides of Hpt
were also analyzed by mass spectrometry, and a decreased amount of sialylated glycan chains was found in glycopeptides
of skin Hpt, as compared with Hpt from plasma. High levels of glycans with fucosylated and tetra-antennary chains were
detected on the peptide NLFLNHSENATAK from Hpt of psoriatic patients. Our data demonstrate that specific changes in
glycan structures of Hpt, such as enhanced glycan branching and fucose content, are associated with psoriasis, and that
differences between circulating and skin Hpt do exist. A lower extent of glycan fucosylation and branching was found in Hpt
from plasma of patients in disease remission. Altered glycoforms might reflect changes of Hpt function in the skin, and
could be used as markers of the disease
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