Human keratinocytes release the endogenous β-galactoside-binding soluble lectin immunoglobulin E (IgE-binding protein) which binds to Langerhans cells where it modulates their binding capacity for IgE clycoforms

Andreas Wollenberg, Henri De La Salle, Daniel Hanau, Fu-Tong Liu, Thomas Bieber

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

A better understanding of the pathophysiological role of Langerhans cells (LC) in atopic diseases is dictated by the characterization of the structures involved in immunoglobulin (IgE)-binding on their cell surface. We previously reported that human LC express the high affinity receptor for IgE (Fc∈RI), as well as the low affinity receptor for IgE (Fc∈RII/CD23). In the present study, we document the presence of a third IgE-binding structure on human LC, the IgE-binding protein (∈BP), an endogenous soluble β-galactoside binding lectin. Immunohistochemical studies performed on normal human skin revealed an anti-∈BP reactivity in the cytoplasm of keratinocytes and in that of acinous cells of eccrine sweat glands. ∈BP was also found on the cell surface of LC, as shown by anti-∈BP/anti-CD1a double labeling and flow cytometric analysis. Anti-∈BP binding to the surface of LC was completely abolished by preincubation with lactose and restored by addition of recombinant human ∈BP, indicating that ∈BP binds to LC surface by virtue of its lectin property. Immunoblot analysis of anti-∈BP-reactive material in keratinocytes and purified LC disclosed a protein with an apparent molecular weight of 33,000 consistent with ∈BP. Interestingly, mRNA transcripts for ∈BP were detected only in keratinocytes but not in purified LC isolated from normal skin. ∈BP was found to be released in culture supernatants of keratinocytes. Incubation of LC with these supernatants resulted in ∈BP-binding to LC surface via protein-carbohydrate interaction. Most importantly, we could show that binding of human myeloma IgE to LC was inhibited by ∈BP. In contrast, neuraminidase-treated human myeloma IgE binds to LC only in the presence of ∈BP. In situ binding studies revealed that keratinocytes, although containing ∈BP intracytoplasmatically, failed to exhibit any IgE-binding properties. Collectively, our results suggest that human keratinocytes produce the β-galactoside-binding lectin ∈BP, which subsequently binds to the surface of LC where it is functional in modulating their binding capacity for IgE glycoforms.

Original languageEnglish (US)
Pages (from-to)777-785
Number of pages9
JournalJournal of Experimental Medicine
Volume178
Issue number3
StatePublished - Sep 1 1993

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Galectin 3
Galactosides
Langerhans Cells
Keratinocytes
Lectins
Immunoglobulin E
Carrier Proteins
Protein Binding
IgE Receptors
Eccrine Glands
Sweat Glands
Skin
Acinar Cells
Neuraminidase
Lactose

ASJC Scopus subject areas

  • Immunology

Cite this

Human keratinocytes release the endogenous β-galactoside-binding soluble lectin immunoglobulin E (IgE-binding protein) which binds to Langerhans cells where it modulates their binding capacity for IgE clycoforms. / Wollenberg, Andreas; De La Salle, Henri; Hanau, Daniel; Liu, Fu-Tong; Bieber, Thomas.

In: Journal of Experimental Medicine, Vol. 178, No. 3, 01.09.1993, p. 777-785.

Research output: Contribution to journalArticle

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abstract = "A better understanding of the pathophysiological role of Langerhans cells (LC) in atopic diseases is dictated by the characterization of the structures involved in immunoglobulin (IgE)-binding on their cell surface. We previously reported that human LC express the high affinity receptor for IgE (Fc∈RI), as well as the low affinity receptor for IgE (Fc∈RII/CD23). In the present study, we document the presence of a third IgE-binding structure on human LC, the IgE-binding protein (∈BP), an endogenous soluble β-galactoside binding lectin. Immunohistochemical studies performed on normal human skin revealed an anti-∈BP reactivity in the cytoplasm of keratinocytes and in that of acinous cells of eccrine sweat glands. ∈BP was also found on the cell surface of LC, as shown by anti-∈BP/anti-CD1a double labeling and flow cytometric analysis. Anti-∈BP binding to the surface of LC was completely abolished by preincubation with lactose and restored by addition of recombinant human ∈BP, indicating that ∈BP binds to LC surface by virtue of its lectin property. Immunoblot analysis of anti-∈BP-reactive material in keratinocytes and purified LC disclosed a protein with an apparent molecular weight of 33,000 consistent with ∈BP. Interestingly, mRNA transcripts for ∈BP were detected only in keratinocytes but not in purified LC isolated from normal skin. ∈BP was found to be released in culture supernatants of keratinocytes. Incubation of LC with these supernatants resulted in ∈BP-binding to LC surface via protein-carbohydrate interaction. Most importantly, we could show that binding of human myeloma IgE to LC was inhibited by ∈BP. In contrast, neuraminidase-treated human myeloma IgE binds to LC only in the presence of ∈BP. In situ binding studies revealed that keratinocytes, although containing ∈BP intracytoplasmatically, failed to exhibit any IgE-binding properties. Collectively, our results suggest that human keratinocytes produce the β-galactoside-binding lectin ∈BP, which subsequently binds to the surface of LC where it is functional in modulating their binding capacity for IgE glycoforms.",
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T1 - Human keratinocytes release the endogenous β-galactoside-binding soluble lectin immunoglobulin E (IgE-binding protein) which binds to Langerhans cells where it modulates their binding capacity for IgE clycoforms

AU - Wollenberg, Andreas

AU - De La Salle, Henri

AU - Hanau, Daniel

AU - Liu, Fu-Tong

AU - Bieber, Thomas

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N2 - A better understanding of the pathophysiological role of Langerhans cells (LC) in atopic diseases is dictated by the characterization of the structures involved in immunoglobulin (IgE)-binding on their cell surface. We previously reported that human LC express the high affinity receptor for IgE (Fc∈RI), as well as the low affinity receptor for IgE (Fc∈RII/CD23). In the present study, we document the presence of a third IgE-binding structure on human LC, the IgE-binding protein (∈BP), an endogenous soluble β-galactoside binding lectin. Immunohistochemical studies performed on normal human skin revealed an anti-∈BP reactivity in the cytoplasm of keratinocytes and in that of acinous cells of eccrine sweat glands. ∈BP was also found on the cell surface of LC, as shown by anti-∈BP/anti-CD1a double labeling and flow cytometric analysis. Anti-∈BP binding to the surface of LC was completely abolished by preincubation with lactose and restored by addition of recombinant human ∈BP, indicating that ∈BP binds to LC surface by virtue of its lectin property. Immunoblot analysis of anti-∈BP-reactive material in keratinocytes and purified LC disclosed a protein with an apparent molecular weight of 33,000 consistent with ∈BP. Interestingly, mRNA transcripts for ∈BP were detected only in keratinocytes but not in purified LC isolated from normal skin. ∈BP was found to be released in culture supernatants of keratinocytes. Incubation of LC with these supernatants resulted in ∈BP-binding to LC surface via protein-carbohydrate interaction. Most importantly, we could show that binding of human myeloma IgE to LC was inhibited by ∈BP. In contrast, neuraminidase-treated human myeloma IgE binds to LC only in the presence of ∈BP. In situ binding studies revealed that keratinocytes, although containing ∈BP intracytoplasmatically, failed to exhibit any IgE-binding properties. Collectively, our results suggest that human keratinocytes produce the β-galactoside-binding lectin ∈BP, which subsequently binds to the surface of LC where it is functional in modulating their binding capacity for IgE glycoforms.

AB - A better understanding of the pathophysiological role of Langerhans cells (LC) in atopic diseases is dictated by the characterization of the structures involved in immunoglobulin (IgE)-binding on their cell surface. We previously reported that human LC express the high affinity receptor for IgE (Fc∈RI), as well as the low affinity receptor for IgE (Fc∈RII/CD23). In the present study, we document the presence of a third IgE-binding structure on human LC, the IgE-binding protein (∈BP), an endogenous soluble β-galactoside binding lectin. Immunohistochemical studies performed on normal human skin revealed an anti-∈BP reactivity in the cytoplasm of keratinocytes and in that of acinous cells of eccrine sweat glands. ∈BP was also found on the cell surface of LC, as shown by anti-∈BP/anti-CD1a double labeling and flow cytometric analysis. Anti-∈BP binding to the surface of LC was completely abolished by preincubation with lactose and restored by addition of recombinant human ∈BP, indicating that ∈BP binds to LC surface by virtue of its lectin property. Immunoblot analysis of anti-∈BP-reactive material in keratinocytes and purified LC disclosed a protein with an apparent molecular weight of 33,000 consistent with ∈BP. Interestingly, mRNA transcripts for ∈BP were detected only in keratinocytes but not in purified LC isolated from normal skin. ∈BP was found to be released in culture supernatants of keratinocytes. Incubation of LC with these supernatants resulted in ∈BP-binding to LC surface via protein-carbohydrate interaction. Most importantly, we could show that binding of human myeloma IgE to LC was inhibited by ∈BP. In contrast, neuraminidase-treated human myeloma IgE binds to LC only in the presence of ∈BP. In situ binding studies revealed that keratinocytes, although containing ∈BP intracytoplasmatically, failed to exhibit any IgE-binding properties. Collectively, our results suggest that human keratinocytes produce the β-galactoside-binding lectin ∈BP, which subsequently binds to the surface of LC where it is functional in modulating their binding capacity for IgE glycoforms.

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