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Vaccine Therapy in Treating Women With Triple-Negative Breast Cancer

2014-08-27 03:18:58 | BioPortfolio

Summary

RATIONALE:

Vaccines made from peptides may help the body build an effective immune response to kill tumor cells. Giving booster vaccinations may make a stronger immune response and prevent or delay the recurrence of cancer.

PURPOSE:

This clinical trial is studying the side effects and how well vaccine therapy works in treating women with triple-negative breast cancer.

Description

PRIMARY OBJECTIVES:

I. To evaluate the efficacy of MUC1 peptide-poly-ICLC adjuvant vaccine in boosting systemic immunity to MUC1 in women who have completed therapy for AJCC stage I-III 'triple-negative' [i.e., ER(-) PR(-) HER2/neu(-)] breast cancer.

SECONDARY OBJECTIVES:

I. To evaluate the safety and toxicity of the MUC1 peptide and poly-ICLC vaccine in this cohort of patients.

OUTLINE:

Patients receive MUC-1 peptide vaccine subcutaneously and poly-ICLC vaccine intramuscularly in weeks 0, 4, 8, 12, 52, and 56 in the absence of disease progression or unacceptable toxicity. Patients may receive additional vaccines in weeks 34 and 38 if anti-MUC1 immunity falls below the two-fold enhancement from baseline.

Study Design

Endpoint Classification: Safety/Efficacy Study, Intervention Model: Single Group Assignment, Masking: Open Label, Primary Purpose: Treatment

Conditions

Breast Cancer

Intervention

MUC-1 peptide vaccine, poly ICLC, MUC1 peptide-poly-ICLC adjuvant vaccine, laboratory biomarker analysis, enzyme-linked immunosorbent assay, flow cytometry

Location

Ireland Cancer Center at University Hospitals Case Medical Center, Case Comprehensive Cancer Center
Cleveland
Ohio
United States
44106

Status

Recruiting

Source

Case Comprehensive Cancer Center

Results (where available)

View Results

Links

Published on BioPortfolio: 2014-08-27T03:18:58-0400

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Medical and Biotech [MESH] Definitions

A poly(A) binding protein that is involved in promoting the extension of the poly A tails of MRNA. The protein requires a minimum of ten ADENOSINE nucleotides in order for binding to mRNA. Once bound it works in conjunction with CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR to stimulate the rate of poly A synthesis by POLY A POLYMERASE. Once poly-A tails reach around 250 nucleotides in length poly(A) binding protein II no longer stimulates POLYADENYLATION. Mutations within a GCG repeat region in the gene for poly(A) binding protein II have been shown to cause the disease MUSCULAR DYSTROPHY, OCULOPHARYNGEAL.

A poly(ADP-ribose) polymerase that contains two ZINC FINGERS in its N-terminal DNA-binding region. It modifies NUCLEAR PROTEINS involved in chromatin architecture and BASE EXCISION REPAIR with POLY ADENOSINE DIPHOSPHATE RIBOSE.

A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.

Post-translational modification of proteins with POLY ADENOSINE DIPHOSPHATE RIBOSE.

The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.

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