Alternative splicing of the human IgA Fc receptor CD89 in neutrophils and eosinophils

Richard J. Pleass, Paul D. Andrews, Michael A. Kerr, Jenny M. Woof (Lead / Corresponding author)

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Receptors for the Fc portion of IgA (FcαR) trigger important immunological elimination processes against IgA-coated targets. Investigation of human FcαR (CD89) transcripts in neutrophils, eosinophils and a monocyte-like cell line, THP-1, with the use of reverse transcriptase PCR, Northern blotting and RNase protection analysis, has provided evidence in these cell types for at least two distinct transcripts generated by alternative splicing. The cDNAs derived from the two major transcripts of both neutrophils and eosinophils have been cloned and sequenced. For both cell types, the larger clone represents the previously described full-length receptor, whereas the second, shorter, splice variant lacks the entire second, membrane-proximal, Ig-like domain. Stable CHO-K1 transfectants have been obtained for both full-length and truncated variant neutrophil receptors. Whereas the full-length receptor is recognized by a panel of five anti-FcαR monoclonal antibodies (mAbs), the shorter variant is bound weakly by only two of the antibodies, suggesting that the epitopes recognized by the majority of the mAbs lie at least in part in the second Ig-like domain of FcαR. Both full-length and splice variant forms of the receptor bind secretory IgA, but the weak binding to serum IgA seen with the full-length receptor is not evident with the shorter variant. Alternative splicing might therefore serve as a means of diversifying FcαR structure and function.

Original languageEnglish
Pages (from-to)771-777
Number of pages7
JournalBiochemical Journal
Volume318
Issue number3
DOIs
Publication statusPublished - 15 Sep 1996

Fingerprint

Fc Receptors
Alternative Splicing
Eosinophils
Immunoglobulin A
Neutrophils
Monoclonal Antibodies
RNA-Directed DNA Polymerase
Ribonucleases
Epitopes
Complementary DNA
Cells
Reverse Transcriptase Polymerase Chain Reaction
Membranes
Northern Blotting
Antibodies
Monocytes
Clone Cells
Cell Line
Serum
IgA receptor

Cite this

Pleass, Richard J. ; Andrews, Paul D. ; Kerr, Michael A. ; Woof, Jenny M. / Alternative splicing of the human IgA Fc receptor CD89 in neutrophils and eosinophils. In: Biochemical Journal. 1996 ; Vol. 318, No. 3. pp. 771-777.
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Alternative splicing of the human IgA Fc receptor CD89 in neutrophils and eosinophils. / Pleass, Richard J.; Andrews, Paul D.; Kerr, Michael A.; Woof, Jenny M. (Lead / Corresponding author).

In: Biochemical Journal, Vol. 318, No. 3, 15.09.1996, p. 771-777.

Research output: Contribution to journalArticle

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