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Polymeric IgA are sulfated proteins
Author(s) -
Boisgard Raphaël,
Charpigny Gilles,
Chanat Eric
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01631-2
Subject(s) - sulfation , transcytosis , secretory component , secretion , chemistry , biochemistry , antibody , j chain , immunoglobulin light chain , immunoglobulin a , secretory protein , polymeric immunoglobulin receptor , biology , microbiology and biotechnology , immunoglobulin g , immunology , receptor , endocytosis
The main sulfated proteins secreted by rabbit mammary gland tissue had M r of ∼67 000, 63 000 and 23 000, and one component which most likely corresponded to proteoglycans had a diffuse electrophoretic mobility ( M r >200 000). The sulfate groups in the 67–63 kDa proteins were mostly linked to carbohydrates. These proteins and the 23 kDa protein were co‐purified and identified to heavy chains of immunoglobulin A (IgA) and J chain, respectively. Sulfation of α‐chains also occurred in rat mammary and rabbit lacrimal glands. We conclude that polymeric IgA which are produced by plasma cells and released in secretion fluids after transcytosis through epithelia are sulfated.