Intracellular Colocalization of Molecules Involved in Antigen Processing and Presentation by B Cells

Brodsky, FM; Koppelman, Bruce; Blum, Janice S.; Marks, Michael S.; Cresswell, Peter; Guagliardi, Lynne E.

doi:10.1101/sqb.1989.054.01.040

Cited by 4 publications

(2 citation statements)

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“…However, the mechanisms by which lipid rafts and CTB are endocytosed in B cells remain poorly understood. Although BCR endocytosis is mainly mediated by a clathrin-dependent pathway, it also requires lipid rafts ( Brodsky et al, 1989 ; Guagliardi et al, 1990 ; Stoddart et al, 2002 ). Lipid rafts are thought to provide the platform where clathrin is phosphorylated and gains access to the BCR to be endocytosed ( Pierce, 2002 ; Stoddart et al, 2002 ).…”

Section: Discussionmentioning

confidence: 99%

Lipid raft–dependent plasma membrane repair interferes with the activation of B lymphocytes

Miller

Castro-Gomes

Corrotte

et al. 2015

Journal of Cell Biology

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Section: Discussionmentioning

confidence: 99%

Lipid raft–dependent plasma membrane repair interferes with the activation of B lymphocytes

Miller

Castro-Gomes

Corrotte

et al. 2015

Journal of Cell Biology

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“…The cubes were dehydrated in 50, 70, 90 and 95% ethanol by gentle rotation for 15 min each rinse and for three 10-min intervals in 100% ethanol. 39 They were suspended in 50% LR White resin (London Resin Company ± distributed by Agar Scienti®c Limited)-50% ethanol, rotated for 1 hr, then in LR White (London Resin Company) and rotated overnight at room temperature. Resin-embedded samples were placed in gelatin capsules and kept at 52u for 24 hr.…”

Section: Electron Microscopymentioning

confidence: 99%

Endocytosis and recycling of the complex between CD23 and HLA‐DR in human B cells

et al. 2001

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SUMMARYThe presentation of extremely low doses of antigen to T cells is enhanced by immunoglobulin E (IgE)-dependent antigen focusing to CD23, the low-af®nity receptor for IgE, expressed on activated B cells. CD23 contains a C-type lectin domain in its extracellular sequence and a targeting signal for coated pits, required for endocytosis, in its cytoplasmic sequence. CD23 is non-covalently associated with the major histocompatibility complex class II antigen, human leucocyte antigen HLA-DR, on the surface of human B cells, but the fate of this complex following endocytosis is unknown. To answer this question we have labelled these proteins on the surface of RPMI 8866 B cells and traced their route through the cytoplasm. Endocytosis mediated by anti-CD23 antibodies (BU38 and MHM6) led to the loss of CD23 from the cells. Endocytosis mediated by an antibody to HLA-DR (CR3/43) or an antigen±IgE complex (NP-BSA±anti-NP IgE), however, led to recycling of the HLA-DR±CD23 complex to the cell surface on a time scale (3±6 hr) consistent with the recycling of HLA-DR in antigen presentation. Along the latter pathway CD23 label was observed in cytoplasmic organelles that resembled the`compartments for peptide loading' or`class II vesicles' described by previous authors. Two features of the recycling process may contribute to the ef®ciency of antigen presentation. Peptide exchange may be facilitated by the proximity of HLA-DR and antigen in peptide loading compartments of the endosomal network. The return of CD23 with HLA-DR to the cell surface may then help to stabilize speci®c B-cell±T-cell interactions, contributing to T-cell activation.

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Cellular and Molecular Basis for Antigen Transport in the Intestinal Epithelium

Neutra¹,

Kraehenbuhl²

1994

Handbook of Mucosal Immunology

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Intracellular Colocalization of Molecules Involved in Antigen Processing and Presentation by B Cells

Cited by 4 publications

References 0 publications

Lipid raft–dependent plasma membrane repair interferes with the activation of B lymphocytes

Lipid raft–dependent plasma membrane repair interferes with the activation of B lymphocytes

Endocytosis and recycling of the complex between CD23 and HLA‐DR in human B cells

Cellular and Molecular Basis for Antigen Transport in the Intestinal Epithelium

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