Literature DB >> 1622544

A case for chaperones in antigen processing.

D C DeNagel1, S K Pierce.   

Abstract

The assembly of peptide-MHC-class-II molecule complexes by antigen-presenting cells is far more efficient than would be predicted from studies of peptide binding to purified MHC class II molecules in vitro. One possible explanation for this discrepancy is that proteins in the antigen-presenting cell facilitate the assembly process. Here, Diane DeNagel and Susan Pierce present the case for involvement of members of the chaperone/heat shock protein 70 family in the intracellular assembly of processed-antigen-MHC-class-II-molecule complexes.

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Year:  1992        PMID: 1622544     DOI: 10.1016/0167-5699(92)90147-Y

Source DB:  PubMed          Journal:  Immunol Today        ISSN: 0167-5699


  30 in total

1.  The septic shock associated HSPA1B1267 polymorphism influences production of HSPA1A and HSPA1B.

Authors:  Suzanna E L Temple; Karey Y Cheong; Kristin G Ardlie; David Sayer; Grant W Waterer
Journal:  Intensive Care Med       Date:  2004-06-30       Impact factor: 17.440

2.  Increased proteolysis of diphtheria toxin by human monocytes after heat shock: a subsidiary role for heat-shock protein 70 in antigen processing.

Authors:  Barbara S Polla; Françoise Gabert; Brigitte M-N Peyrusse; Muriel R Jacquier-Sarlin
Journal:  Immunology       Date:  2006-11-20       Impact factor: 7.397

Review 3.  Hsp70--a multi-gene, multi-structure, multi-function family with potential clinical applications.

Authors:  U Feige; B S Polla
Journal:  Experientia       Date:  1994-11-30

Review 4.  Molecular chaperones in the processing and presentation of antigen to helper T cells.

Authors:  S K Pierce
Journal:  Experientia       Date:  1994-11-30

5.  Sequence and characterization of two HSP70 genes in the colonial protochordate Botryllus schlosseri.

Authors:  M B Fagan; I L Weissman
Journal:  Immunogenetics       Date:  1996       Impact factor: 2.846

6.  Heat-shock protein expression on the membrane of T cells undergoing apoptosis.

Authors:  F Poccia; P Piselli; S Vendetti; S Bach; A Amendola; R Placido; V Colizzi
Journal:  Immunology       Date:  1996-05       Impact factor: 7.397

7.  Legionella pneumophila heat-shock protein-induced increase of interleukin-1 beta mRNA involves protein kinase C signalling in macrophages.

Authors:  C Retzlaff; Y Yamamoto; S Okubo; P S Hoffman; H Friedman; T W Klein
Journal:  Immunology       Date:  1996-10       Impact factor: 7.397

8.  Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family.

Authors:  S Z Domanico; D C DeNagel; J N Dahlseid; J M Green; S K Pierce
Journal:  Mol Cell Biol       Date:  1993-06       Impact factor: 4.272

9.  Presence of hsp65 in bacterial extracts (OM-89): a possible mediator of orally-induced tolerance?

Authors:  B S Polla; S Baladi; K Fuller; G Rook
Journal:  Experientia       Date:  1995-08-16

10.  Exercise-induced extracellular 72 kDa heat shock protein (Hsp72) stimulates neutrophil phagocytic and fungicidal capacities via TLR-2.

Authors:  Esther Giraldo; Leticia Martin-Cordero; Juan Jose Garcia; Mathias Gehrmann; Mathias Gerhmann; Gabriele Multhoff; Eduardo Ortega
Journal:  Eur J Appl Physiol       Date:  2009-09-22       Impact factor: 3.078

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