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RATIONALE: Vaccines may make the body build an immune response to kill tumor cells.
OBJECTIVES: I. Determine whether active specific immunization comprising tyrosinase and gp100:209-217 (gp100) peptides fused with OVA BiP peptide and heat shock protein 70 (HSP70) induces immunity against tyrosinase and gp100 in HLA-A2 positive patients with stage III or IV melanoma. II. Determine the lowest optimally immunogenic dose of tyrosinase and gp100 in these patients. III. Determine the tolerability of this regimen in these patients.
OUTLINE: This is a dose escalation study of tyrosinase and gp100:209-217 antigen (gp100). Patients receive vaccination comprising tyrosinase and gp100 fused with OVA BiP peptide and heat shock protein 70 (HSP70) subcutaneously on weeks 0, 1, 2, 6, and 18 for a total of 5 vaccinations in the absence of disease progression or unacceptable toxicity. Cohorts of 9 patients receive escalating doses of tyrosinase and gp100 until the lowest optimally immunogenic dose is determined. The lowest optimally immunogenic dose is defined as the dose at which 4 or more of 9 patients demonstrate T-cell responses.
PROJECTED ACCRUAL: A total of 27 patients will be accrued for this study.
Primary Purpose: Treatment
OVA BiP peptide, gp209-2M antigen, recombinant 70-kD heat-shock protein, tyrosinase peptide
Memorial Sloan-Kettering Cancer Center
National Cancer Institute (NCI)
Published on BioPortfolio: 2014-08-27T03:57:44-0400
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Rice bran albumin (RBAlb), which showed higher tyrosinase inhibitory activity than other protein fractions, was hydrolyzed with papain to improve the bioactivity. The obtained RBAlb hydrolysate (RBAlb...
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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A vaccine is a biological preparation that improves immunity to a particular disease. A vaccine typically contains an agent that resembles a disease-causing microorganism, and is often made from weakened or killed forms of the microbe, its toxins or one ...
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