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Periostin forms a functional complex with IgA in human serum.

Junya Ono1, Masayuki Takai1, Ayami Kamei2

  • 1Division of Medical Biochemistry, Department of Biomolecular Sciences, Saga Medical School, Saga, Japan; Shino-Test Corporation, Sagamihara, Japan.

Allergology International : Official Journal of the Japanese Society of Allergology
|July 6, 2019
PubMed
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Serum periostin forms a complex with immunoglobulin A1 (IgA1), maintaining its function and potentially impacting diagnostic antibody assays. This discovery offers new avenues for understanding allergic diseases and developing targeted therapies.

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ComplexIgAIntegrinPeriostinSerum

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Area of Science:

  • Immunology
  • Biochemistry
  • Allergy Research

Background:

  • Periostin, a fasciclin family matricellular protein, is implicated in allergic disease pathogenesis by interacting with cell surface integrins.
  • Elevated serum periostin levels in allergic diseases indicate type 2 inflammation and tissue remodeling, suggesting its potential as a biomarker.
  • Previous research indicated that serum periostin primarily exists in an oligomeric form due to disulfide bonds.

Purpose of the Study:

  • To investigate the complex formation of periostin in serum.
  • To determine the functionality of serum periostin complexes.
  • To assess if complex formation affects the reactivity of anti-periostin antibodies.

Main Methods:

  • Analysis of periostin complex formation in human and mouse serum.
  • Assessment of IgA's role in periostin oligomerization.
  • Functional assays to evaluate the integrin-binding capacity of periostin-IgA complexes.
  • Investigation of antibody binding interference with periostin-IgA complexes.

Main Results:

  • Periostin forms a 1:1 complex with IgA1, containing at least five isoforms.
  • IgA is not essential for periostin oligomerization in mouse or IgA-deficient serum.
  • The periostin-IgA complex retains functionality, binding to αVβ3 integrin.
  • Periostin-IgA complex formation interferes with the binding of most anti-periostin antibodies, except those targeting the R4 domain.

Conclusions:

  • Periostin is identified as a novel molecule associated with IgA.
  • These findings enhance understanding of periostin's pathological roles in allergic diseases.
  • The results provide a basis for developing novel periostin-based diagnostics and therapeutics.