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Hsp70 translocates into a cytoplasmic aggregate during lymphocyte activation
1Department of Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo, New York 14263, USA.
Journal of Cellular Physiology
|November 1, 1995
Summary
Heat shock protein 70 (hsp70) is part of lymphocyte aggregates, interacting with spectrin. ATP addition dissociates these aggregates, suggesting hsp70
Area of Science:
- Immunology
- Cell Biology
- Protein Biochemistry
Background:
- Lymphocyte activation involves a distinct cytoplasmic aggregate enriched in spectrin, ankyrin, and protein kinase C.
- Heat shock proteins (hsp70) are known for stabilizing unfolded proteins, crucial for proper protein folding and assembly.
Purpose of the Study:
- To investigate the association of hsp70 with lymphocyte aggregates.
- To determine the role of hsp70 in the structure and dynamics of these activation-associated organelles.
Main Methods:
- Double immunofluorescence analysis to detect hsp70 and spectrin colocalization.
- Immunoprecipitation and Western blot to assess hsp70-spectrin interaction.
- ATP treatment to observe aggregate dissipation and hsp70 repositioning.
Main Results:
- hsp70 was found to be a component of lymphocyte aggregates, colocalizing with spectrin.
- hsp70 and spectrin coprecipitated, and this interaction was abolished by ATP.
- Exogenous ATP addition led to the dissipation of the aggregate structure.
- T-cell activation protocols (PMA, TCR cross-linking) caused hsp70 repositioning into the aggregate.
Conclusions:
- hsp70 is an active component of lymphocyte aggregates.
- hsp70 may play a functional role in the interactions within this activation-associated organelle.