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前沿:专职抗原呈递细胞对热休克蛋白的受体介导内吞作用。

Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells.

作者信息

Arnold-Schild D, Hanau D, Spehner D, Schmid C, Rammensee H G, de la Salle H, Schild H

机构信息

Abteilung Immunologie, Institut für Zellbiologie, Universität Tübingen, Germany.

出版信息

J Immunol. 1999 Apr 1;162(7):3757-60.

Abstract

Immunization with heat shock proteins (HSPs) induces Ag-specific CTL responses. The specificity of the immune response is based on peptides associated with HSPs. To investigate how exogenous HSP/peptide complexes gain access to the MHC class I-restricted Ag presentation pathway, we incubated the monocytic cell line P388D1 and the dendritic cell line D2SC/1 with gold-labeled HSPs gp96 and HSC70. We show that HSPs bind specifically to the surface of these APCs and are internalized spontaneously by receptor-mediated endocytosis, demonstrating the existence of specific receptors for HSPs on these cells. In addition, we observe colocalization of internalized HSPs and surface MHC class I molecules in early and late endosomal structures. These findings provide possible explanations for the immunogenicity of HSP/peptide complexes and for the transfer of HSP-associated peptides onto MHC class I molecules.

摘要

用热休克蛋白(HSPs)进行免疫可诱导抗原特异性CTL反应。免疫反应的特异性基于与HSPs相关的肽段。为了研究外源性HSP/肽复合物如何进入MHC I类限制的抗原呈递途径,我们用金标记的HSPs gp96和HSC70孵育单核细胞系P388D1和树突状细胞系D2SC/1。我们发现HSPs特异性结合这些抗原呈递细胞(APCs)的表面,并通过受体介导的内吞作用自发内化,证明这些细胞上存在HSPs的特异性受体。此外,我们观察到内化的HSPs与早期和晚期内体结构中的表面MHC I类分子共定位。这些发现为HSP/肽复合物的免疫原性以及HSP相关肽段向MHC I类分子的转移提供了可能的解释。

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