Collecting Samples From Patients With Primary Systemic Amyloidosis
RATIONALE: Collecting and storing samples of blood, urine, and tissue from patients with primary systemic amyloidosis to test in the laboratory may help the study of this disease in the future.
PURPOSE: This research study is collecting samples from patients with primary systemic amyloidosis.
|Multiple Myeloma||Genetic: clonality analysis Genetic: polymerase chain reaction Genetic: protein analysis Other: biologic sample preservation procedure Other: laboratory biomarker analysis Procedure: fluorescence spectroscopy Procedure: quality-of-life assessment|
|Study Design:||Observational Model: Other
Time Perspective: Prospective
|Official Title:||Data, Tissue, Blood, and Urine Repository for Amyloid Diseases|
- Establish a repository to promote biochemical research [ Time Frame: life of study ]
- Collection of clinical material and information [ Time Frame: life of study ]
Biospecimen Retention: Samples With DNA
|Study Start Date:||January 2000|
|Estimated Study Completion Date:||February 2037|
|Estimated Primary Completion Date:||January 2018 (Final data collection date for primary outcome measure)|
Genetic: clonality analysis
- To establish and maintain a database of clinical material (i.e., blood, urine, and tissue) and information on patients with primary systemic amyloidosis.
OUTLINE: Blood, urine, tissue, and bone marrow samples are collected during standard laboratory evaluations to maintain a repository of biospecimens in the Gerry Amyloid Research Laboratory, to permit the correlation of clinical results with measured biological events, and for future research studies. Bone marrow RNA samples are examined for immunoglobulin light-chain gene sequences and amino acids by PCR and positional cloning. Blood serum and urine samples are evaluated for amyloid protein stability by high-resolution calorimetry, isothermal-titration calorimetry, and far- and near-UV circular dichroism and fluorescence spectroscopy. Urine samples are also examined for post-translational modifications (e.g., glycosylation, sulfation, and cross-linking) to identify common features unique to amyloid proteins. Tissue samples are analyzed for biochemical and biophysical properties and for post-translational modifications in light chains.
Quality of life is assessed by the SF36 questionnaire.
Please refer to this study by its ClinicalTrials.gov identifier: NCT00898235
|Contact: Salli Fennesseyfirstname.lastname@example.org|
|United States, Massachusetts|
|Boston University Cancer Research Center||Recruiting|
|Boston, Massachusetts, United States, 02118|
|Contact: Clinical Trials Office - Boston University Cancer Research Cen 617-638-8265|
|Principal Investigator:||Vaishali Sanchorawala, MD||Boston Medical Center|