{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,3]],"date-time":"2024-07-03T02:57:41Z","timestamp":1719975461955},"reference-count":52,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2007,8,31]],"date-time":"2007-08-31T00:00:00Z","timestamp":1188518400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Acad Dermatol Venereol"],"published-print":{"date-parts":[[2008,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:bold>Objective\u2002<\/jats:bold> The aim of this work was to assess whether psoriasis is associated with phenotype prevalence and altered activity of haptoglobin (Hpt).<\/jats:p><jats:p><jats:bold>Background\u2002<\/jats:bold> Hpt is a plasma acute\u2010phase glycoprotein, displaying in humans three phenotypes. Phenotype prevalence or structure modification of Hpt was associated with several diseases. The Hpt main function is to bind and carry to the liver free haemoglobin for degradation and iron recycling. Hpt was recently found able to bind the apolipoprotein A\u2010I (ApoA\u2010I), thus impairing its stimulation on the activity of the enzyme lecithin\u2010cholesterol acyl\u2010transferase (LCAT).<\/jats:p><jats:p><jats:bold>Study design\u2002<\/jats:bold> Hpt was isolated from patients with psoriasis vulgaris, and its activity in haemoglobin or ApoA\u2010I binding and LCAT inhibition was compared with that of normal protein.<\/jats:p><jats:p><jats:bold>Methods\u2002<\/jats:bold> Two affinity chromatography steps, the first using resin\u2010coupled haemoglobin and the second anti\u2010Hpt antibodies, were used to purify Hpt. The protein phenotype was assessed by electrophoresis. Binding experiments were performed by Enzyme\u2010linked immunosorbent assay with stationary haemoglobin or ApoA\u2010I, Hpt in solution and anti\u2010Hpt antibodies for detection of bound Hpt. Standard LCAT assays were carried out in the presence of Hpt purified from patients or healthy subjects.<\/jats:p><jats:p><jats:bold>Results\u2002<\/jats:bold> Phenotype prevalence of Hpt in psoriasis was not found. After affinity chromatography by haemoglobin, albumin and ApoA\u2010I were routinely found heavily contaminating only Hpt from normal subjects. Isolated Hpt from patients had lower activity than normal protein in both haemoglobin binding and LCAT inhibition.<\/jats:p><jats:p><jats:bold>Conclusions\u2002<\/jats:bold> In psoriasis, Hpt displays some structure modification(s), which might be associated with the protein function in the disease.<\/jats:p>","DOI":"10.1111\/j.1468-3083.2007.02444.x","type":"journal-article","created":{"date-parts":[[2007,9,6]],"date-time":"2007-09-06T03:05:44Z","timestamp":1189047944000},"page":"417-425","source":"Crossref","is-referenced-by-count":5,"title":["Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin\u2010cholesterol acyltransferase 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