Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity

L. Cigliano, B. Maresca, A. Salvatore, M. Nino, G. Monfrecola, F. Ayala, A. Carlucci, R. C. Pugliese, C. Pedone, Paolo Abrescia

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Objective: The aim of this work was to assess whether psoriasis is associated with phenotype prevalence and altered activity of haptoglobin (Hpt). Background: Hpt is a plasma acute-phase glycoprotein, displayingin 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-I (ApoA-I), thus impairing its stimulation on the activity of the enzyme lecithin-cholesterol acyl-transferase (LCAT). Study design: Hpt was isolated from patients with psoriasis vulgaris, and its activity in haemoglobin or ApoA-I binding and LCAT inhibition was compared with that of normal protein. Methods: Two affinity chromatography steps, the first using resin-coupled haemoglobin and the second anti-Hpt antibodies, were used to purify Hpt. The protein phenotype was assessed by electrophoresis. Binding experiments were performed by Enzyme-linked immunosorbent assay with stationary haemoglobin or ApoA-I, Hpt in solution and anti-Hpt antibodies for detection of bound Hpt. Standard LCAT assays were carried out in the presence of Hpt purified from patients or healthy subjects. Results: Phenotype prevalence of Hpt in psoriasis was not found. After affinity chromatography by haemoglobin, albumin and ApoA-I 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. Conclusions: In psoriasis, Hpt displays some structure modification(s), which might be associated with the protein function in the disease.

Original languageEnglish
Pages (from-to)417-425
Number of pages9
JournalJournal of the European Academy of Dermatology and Venereology
Volume22
Issue number4
DOIs
Publication statusPublished - Apr 2008

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Phosphatidylcholine-Sterol O-Acyltransferase
Haptoglobins
Hemoglobins
Lecithins
Apolipoprotein A-I
Transferases
Hemoglobin A
Psoriasis
Phenotype
Cholesterol
Affinity Chromatography
Anti-Idiotypic Antibodies
Proteins
Acute-Phase Proteins
Recycling

Keywords

  • Apolipoprotein A-I
  • Haemoglobin
  • Haptoglobin
  • Lecithin-cholesterol acyltransferase
  • Psoriasis vulgaris

ASJC Scopus subject areas

  • Dermatology
  • Infectious Diseases

Cite this

Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity. / Cigliano, L.; Maresca, B.; Salvatore, A.; Nino, M.; Monfrecola, G.; Ayala, F.; Carlucci, A.; Pugliese, R. C.; Pedone, C.; Abrescia, Paolo.

In: Journal of the European Academy of Dermatology and Venereology, Vol. 22, No. 4, 04.2008, p. 417-425.

Research output: Contribution to journalArticle

Cigliano, L. ; Maresca, B. ; Salvatore, A. ; Nino, M. ; Monfrecola, G. ; Ayala, F. ; Carlucci, A. ; Pugliese, R. C. ; Pedone, C. ; Abrescia, Paolo. / Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity. In: Journal of the European Academy of Dermatology and Venereology. 2008 ; Vol. 22, No. 4. pp. 417-425.
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abstract = "Objective: The aim of this work was to assess whether psoriasis is associated with phenotype prevalence and altered activity of haptoglobin (Hpt). Background: Hpt is a plasma acute-phase glycoprotein, displayingin 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-I (ApoA-I), thus impairing its stimulation on the activity of the enzyme lecithin-cholesterol acyl-transferase (LCAT). Study design: Hpt was isolated from patients with psoriasis vulgaris, and its activity in haemoglobin or ApoA-I binding and LCAT inhibition was compared with that of normal protein. Methods: Two affinity chromatography steps, the first using resin-coupled haemoglobin and the second anti-Hpt antibodies, were used to purify Hpt. The protein phenotype was assessed by electrophoresis. Binding experiments were performed by Enzyme-linked immunosorbent assay with stationary haemoglobin or ApoA-I, Hpt in solution and anti-Hpt antibodies for detection of bound Hpt. Standard LCAT assays were carried out in the presence of Hpt purified from patients or healthy subjects. Results: Phenotype prevalence of Hpt in psoriasis was not found. After affinity chromatography by haemoglobin, albumin and ApoA-I 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. Conclusions: In psoriasis, Hpt displays some structure modification(s), which might be associated with the protein function in the disease.",
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T1 - Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity

AU - Cigliano, L.

AU - Maresca, B.

AU - Salvatore, A.

AU - Nino, M.

AU - Monfrecola, G.

AU - Ayala, F.

AU - Carlucci, A.

AU - Pugliese, R. C.

AU - Pedone, C.

AU - Abrescia, Paolo

PY - 2008/4

Y1 - 2008/4

N2 - Objective: The aim of this work was to assess whether psoriasis is associated with phenotype prevalence and altered activity of haptoglobin (Hpt). Background: Hpt is a plasma acute-phase glycoprotein, displayingin 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-I (ApoA-I), thus impairing its stimulation on the activity of the enzyme lecithin-cholesterol acyl-transferase (LCAT). Study design: Hpt was isolated from patients with psoriasis vulgaris, and its activity in haemoglobin or ApoA-I binding and LCAT inhibition was compared with that of normal protein. Methods: Two affinity chromatography steps, the first using resin-coupled haemoglobin and the second anti-Hpt antibodies, were used to purify Hpt. The protein phenotype was assessed by electrophoresis. Binding experiments were performed by Enzyme-linked immunosorbent assay with stationary haemoglobin or ApoA-I, Hpt in solution and anti-Hpt antibodies for detection of bound Hpt. Standard LCAT assays were carried out in the presence of Hpt purified from patients or healthy subjects. Results: Phenotype prevalence of Hpt in psoriasis was not found. After affinity chromatography by haemoglobin, albumin and ApoA-I 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. Conclusions: In psoriasis, Hpt displays some structure modification(s), which might be associated with the protein function in the disease.

AB - Objective: The aim of this work was to assess whether psoriasis is associated with phenotype prevalence and altered activity of haptoglobin (Hpt). Background: Hpt is a plasma acute-phase glycoprotein, displayingin 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-I (ApoA-I), thus impairing its stimulation on the activity of the enzyme lecithin-cholesterol acyl-transferase (LCAT). Study design: Hpt was isolated from patients with psoriasis vulgaris, and its activity in haemoglobin or ApoA-I binding and LCAT inhibition was compared with that of normal protein. Methods: Two affinity chromatography steps, the first using resin-coupled haemoglobin and the second anti-Hpt antibodies, were used to purify Hpt. The protein phenotype was assessed by electrophoresis. Binding experiments were performed by Enzyme-linked immunosorbent assay with stationary haemoglobin or ApoA-I, Hpt in solution and anti-Hpt antibodies for detection of bound Hpt. Standard LCAT assays were carried out in the presence of Hpt purified from patients or healthy subjects. Results: Phenotype prevalence of Hpt in psoriasis was not found. After affinity chromatography by haemoglobin, albumin and ApoA-I 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. Conclusions: In psoriasis, Hpt displays some structure modification(s), which might be associated with the protein function in the disease.

KW - Apolipoprotein A-I

KW - Haemoglobin

KW - Haptoglobin

KW - Lecithin-cholesterol acyltransferase

KW - Psoriasis vulgaris

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JO - Journal of the European Academy of Dermatology and Venereology

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