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Human Resident Langerhans Cells Display a Lysosomal compartment Enriched in MHC Class II

Data up to Jan 2025

Published1994
Citations68
References48

Total Citations Per Year

Abstract

References (48)

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Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules.

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Antigen processing by epidermal Langerhans cells correlates with the level of biosynthesis of major histocompatibility complex class II molecules and expression of invariant chain.

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The MHC class II-associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail.

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Processed antigen binds to newly synthesized mhc class II molecules in antigen-specific B lymphocytes

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Class II MHC molecules are present in macrophage lysosomes and phagolysosomes that function in the phagocytic processing of Listeria monocytogenes for presentation to T cells.

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Class II major histocompatibility complex molecules of murine dendritic cells: synthesis, sialylation of invariant chain, and antigen processing capacity are down-regulated upon culture.

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Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigens.

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Invariant chain targets HLA class II molecules to acidic endosomes containing internalized influenza virus.

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Intracellular transport and localization of major histocompatibility complex class II molecules and associated invariant chain.

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Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis.

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Immunogenic peptides bind to class II MHC molecules in an early lysosomal compartment.

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Rapid intracellular pathway gives rise to cell surface expression of the MHC class II-associated invariant chain (CD74).

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Human Resident Langerhans Cells Display a Lysosomal compartment Enriched in MHC Class II (1994) – Journal of Investigative Dermatology | Metascience Observatory Explorer