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PURPOSE: Phase I trial to study the effectiveness of vaccine therapy in treating patients who have chronic myelogenous leukemia.
- Determine the feasibility of vaccination with autologous heat shock protein 70 in patients with chronic phase chronic myelogenous leukemia.
- Determine the toxicity of this vaccination in these patients.
OUTLINE: Patients undergo leukapheresis to obtain peripheral mononuclear cells (PMNCs). Heat shock protein 70 (HSP70) is derived from the autologous PMNCs. Patients receive HSP70 intradermally once weekly for 8 weeks.
Patients are followed for 2 weeks.
PROJECTED ACCRUAL: A total of 10 patients will be accrued for this study.
Primary Purpose: Treatment
recombinant 70-kD heat-shock protein
University of Connecticut Health Center
Active, not recruiting
National Cancer Institute (NCI)
Published on BioPortfolio: 2014-08-27T03:56:21-0400
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Aging in Caenorhabditis elegans is controlled, in part, by the insulin-like signaling and heat shock response pathways. Following thermal stress, expression levels of small heat shock protein-16.2 sho...
To study the mechanism of heat shock protein 27 (HSP27) phosphorylation in the visfatin-induced proliferation and its protective effect against high-glucose induced apoptosis in HUVECs.
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Heat shock protein A9 (HSPA9), a member of the heat shock protein family, is a putative receptor for tembusu virus (TMUV). Using Western blot and co-immunoprecipitation assay, E protein domains I and ...
A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.
A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.
Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.
A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.
Heat and cold stress-inducible, transcription factors that bind to inverted 5'-NGAAN-3' pentamer DNA sequences and are regulated by poly(ADP) ribosylation. They play essential roles as transcriptional activators of the HEAT-SHOCK RESPONSE by inducing expression of large classes of MOLECULAR CHAPERONES and heat-shock proteins. They also function in DNA REPAIR; transcriptional reactivation of latent HIV-1; and pre-mRNA processing and nuclear export of HSP70 HEAT-SHOCK PROTEINS during heat stress.
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