Intracellular delivery of major histocompatibility complex class I-binding epitopes: dendritic cells loaded and matured with cationic peptide/poly(I:C) complexes efficiently activate T cells

2010 ◽  
Vol 19 (1) ◽  
pp. 19-28 ◽  
Author(s):  
Holger A. Haenssle ◽  
Petra Riedl ◽  
Timo Buhl ◽  
Anke Schardt ◽  
Albert Rosenberger ◽  
...  
Keyword(s):  
T Cells ◽  
Dendritic Cells ◽  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Intracellular Delivery ◽  
Class I ◽  
Poly I:C ◽  
Complex Class ◽  
Cationic Peptide ◽  
Histocompatibility Complex

scholarly journals Activation of Stat-3 Is Involved in the Induction of Apoptosis After Ligation of Major Histocompatibility Complex Class I Molecules on Human Jurkat T Cells

Blood ◽  
1998 ◽  
Vol 91 (10) ◽  
pp. 3566-3573 ◽  
Author(s):  
Søren Skov ◽  
Mette Nielsen ◽  
Søren Bregenholt ◽  
Niels Ødum ◽  
Mogens H. Claesson
Keyword(s):  
T Cells ◽  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Jurkat T Cells ◽  
Class I Mhc ◽  
Mhc I ◽  
Histocompatibility Complex

Abstract Activation of Janus tyrosine kinases (Jak) and Signal transducers and activators of transcription (Stat) after ligation of major histocompatibility complex class I (MHC-I) was explored in Jurkat T cells. Cross-linking of MHC-I mediated tyrosine phosphorylation of Tyk2, but not Jak1, Jak2, and Jak3. In addition, the transcription factor Stat-3 was tyrosine phosphorylated in the cytoplasma and subsequently translocated to the cell nucleus. Data obtained by electrophoretic mobility shift assay suggested that the activated Stat-3 protein associates with the human serum-inducible element (hSIE) DNA-probe derived from the interferon-γ activated site (GAS) in the c-fos promoter, a common DNA sequence for Stat protein binding. An association between hSIE and Stat-3 after MHC-I ligation was directly demonstrated by precipitating Stat-3 from nuclear extracts with biotinylated hSIE probe and avidin-coupled agarose. To investigate the function of the activated Stat-3, Jurkat T cells were transiently transfected with a Stat-3 isoform lacking the transactivating domain. This dominant-negative acting Stat-3 isoform significantly inhibited apoptosis induced by ligation of MHC-I. In conclusion, our data suggest the involvement of the Jak/Stat signal pathway in MHC-I–induced signal transduction in T cells.

scholarly journals Exogenous antigens gain access to the major histocompatibility complex class I processing pathway in B cells by receptor-mediated uptake.

1996 ◽  
Vol 184 (3) ◽  
pp. 1179-1184 ◽  
Author(s):  
Y Ke ◽  
J A Kapp
Keyword(s):  
Dendritic Cells ◽  
Major Histocompatibility Complex ◽  
B Cells ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Receptor Mediated Endocytosis ◽  
Histocompatibility Complex ◽  
Antigen Presenting ◽  
Gain Access

Professional antigen-presenting cells, such as macrophages, dendritic cells, or B cells, take up soluble, exogenous antigens (Ags) and process them through the class II pathway. Several reports have shown that phagocytic macrophages also process particulate or soluble forms of exogenous Ag via the class I pathway. By contrast, B cells normally do not process soluble, exogenous Ag by way of the class I pathway unless Ags are directly introduced into the cytoplasm. Here we report that B cells present exogenous Ag via the class I pathway when Ags are taken up by receptor-mediated endocytosis. Thus, specialized methods of Ag uptake such as phagocytosis or receptor-mediated endocytosis deliver exogenous Ag into the class I pathway of Ag processing and presentation.

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