Diane Jelinek - Academia.edu (original) (raw)
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Papers by Diane Jelinek
Blood, 2008
Primary systemic amyloidosis (AL) is a rare monoclonal plasma cell (PC) disorder characterized by... more Primary systemic amyloidosis (AL) is a rare monoclonal plasma cell (PC) disorder characterized by the deposition of misfolded immunoglobulin (Ig) light chains (LC) in vital organs throughout the body. To our knowledge, no cell lines have ever been established from AL patients. Here we describe the establishment of the ALMC-1 and ALMC-2 cell lines from an AL patient. Both cell lines exhibit a PC phenotype and display cytokine-dependent growth. Using a comprehensive genetic approach, we established the genetic relationship between the cell lines and the primary patient cells, and we were also able to identify new genetic changes accompanying tumor progression that may explain the natural history of this patient's disease. Importantly, we demonstrate that free lambda LC secreted by both cell lines contained a beta structure and formed amyloid fibrils. Despite absolute Ig LC variable gene sequence identity, the proteins show differences in amyloid formation kinetics that are abolish...
Oncotarget, Jan 30, 2014
Multiple myeloma (MM) is characterized by the clonal expansion of malignant plasma cells within t... more Multiple myeloma (MM) is characterized by the clonal expansion of malignant plasma cells within the bone marrow. There is a growing literature that tumor cells release biologically active microvesicles (MVs) that modify both local and distant microenvironments. In this study, our goals were to determine if MM cells release MVs, and if so, begin to characterize their biologic activity. Herein we present clear evidence that not only do both patient MM cells and human MM cell lines (HMCLs) release MVs, but that these MVs stimulate MM cell growth. Of interest, MM-derived MVs were enriched with the biologically active form of CD147, a transmembrane molecule previously shown by us to be crucial for MM cell proliferation. Using MVs isolated from HMCLs stably transfected with a CD147-GFP fusion construct (CD147GFP), we observed binding and internalization of MV-derived CD147 with HMCLs. Cells with greater CD147GFP internalization proliferated at a higher rate than did cells with less CD147GFP association. Lastly, MVs obtained from CD147 downregulated HMCLs were attenuated in their ability to stimulate HMCL proliferation. In summary, this study demonstrates the significance of MV shedding and MV-mediated intercellular communication on malignant plasma cell proliferation, and identifies the role of MV-enriched CD147 in this process.
Journal of Proteome Research, 2015
Immunoglobulin light chain (LC) amyloidosis (AL) is caused by deposition of clonal LCs produced b... more Immunoglobulin light chain (LC) amyloidosis (AL) is caused by deposition of clonal LCs produced by an underlying plasma cell neoplasm. The clonotypic LC sequences are unique to each patient and they cannot be reliably detected by either immunoassays or standard proteomic workflows that target the constant regions of LCs. We addressed this issue by developing a novel sequence template-based workflow to detect LC variable (LCV) region peptides directly from AL amyloid deposits. The workflow was implemented in a CAP/CLIA compliant clinical laboratory dedicated to proteomic subtyping of amyloid deposits extracted from either formalin-fixed paraffin-embedded tissues or subcutaneous fat aspirates. We evaluated the performance of the workflow on a validation cohort of 30 AL patients, whose amyloidogenic clone was identified using a novel proteogenomics method, and 30 controls. The recall and negative predictive value of the workflow, when identifying the gene family of the AL clone, was 93% and 98%, respectively. Application of the workflow on a clinical cohort of 500 AL amyloidosis samples highlighted a bias in the LCV gene families used by the AL clones. We also detected similarity between AL clones deposited in multiple organs of systemic AL patients. In summary, AL proteomic data sets are rich in LCV region peptides of potential clinical significance that are recoverable with advanced bioinformatics.
F1000 - Post-publication peer review of the biomedical literature, 2000
The Molecular Basis of B-Cell Differentiation and Function, 1986
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
Blood, 2008
Primary systemic amyloidosis (AL) is a rare monoclonal plasma cell (PC) disorder characterized by... more Primary systemic amyloidosis (AL) is a rare monoclonal plasma cell (PC) disorder characterized by the deposition of misfolded immunoglobulin (Ig) light chains (LC) in vital organs throughout the body. To our knowledge, no cell lines have ever been established from AL patients. Here we describe the establishment of the ALMC-1 and ALMC-2 cell lines from an AL patient. Both cell lines exhibit a PC phenotype and display cytokine-dependent growth. Using a comprehensive genetic approach, we established the genetic relationship between the cell lines and the primary patient cells, and we were also able to identify new genetic changes accompanying tumor progression that may explain the natural history of this patient's disease. Importantly, we demonstrate that free lambda LC secreted by both cell lines contained a beta structure and formed amyloid fibrils. Despite absolute Ig LC variable gene sequence identity, the proteins show differences in amyloid formation kinetics that are abolish...
Oncotarget, Jan 30, 2014
Multiple myeloma (MM) is characterized by the clonal expansion of malignant plasma cells within t... more Multiple myeloma (MM) is characterized by the clonal expansion of malignant plasma cells within the bone marrow. There is a growing literature that tumor cells release biologically active microvesicles (MVs) that modify both local and distant microenvironments. In this study, our goals were to determine if MM cells release MVs, and if so, begin to characterize their biologic activity. Herein we present clear evidence that not only do both patient MM cells and human MM cell lines (HMCLs) release MVs, but that these MVs stimulate MM cell growth. Of interest, MM-derived MVs were enriched with the biologically active form of CD147, a transmembrane molecule previously shown by us to be crucial for MM cell proliferation. Using MVs isolated from HMCLs stably transfected with a CD147-GFP fusion construct (CD147GFP), we observed binding and internalization of MV-derived CD147 with HMCLs. Cells with greater CD147GFP internalization proliferated at a higher rate than did cells with less CD147GFP association. Lastly, MVs obtained from CD147 downregulated HMCLs were attenuated in their ability to stimulate HMCL proliferation. In summary, this study demonstrates the significance of MV shedding and MV-mediated intercellular communication on malignant plasma cell proliferation, and identifies the role of MV-enriched CD147 in this process.
Journal of Proteome Research, 2015
Immunoglobulin light chain (LC) amyloidosis (AL) is caused by deposition of clonal LCs produced b... more Immunoglobulin light chain (LC) amyloidosis (AL) is caused by deposition of clonal LCs produced by an underlying plasma cell neoplasm. The clonotypic LC sequences are unique to each patient and they cannot be reliably detected by either immunoassays or standard proteomic workflows that target the constant regions of LCs. We addressed this issue by developing a novel sequence template-based workflow to detect LC variable (LCV) region peptides directly from AL amyloid deposits. The workflow was implemented in a CAP/CLIA compliant clinical laboratory dedicated to proteomic subtyping of amyloid deposits extracted from either formalin-fixed paraffin-embedded tissues or subcutaneous fat aspirates. We evaluated the performance of the workflow on a validation cohort of 30 AL patients, whose amyloidogenic clone was identified using a novel proteogenomics method, and 30 controls. The recall and negative predictive value of the workflow, when identifying the gene family of the AL clone, was 93% and 98%, respectively. Application of the workflow on a clinical cohort of 500 AL amyloidosis samples highlighted a bias in the LCV gene families used by the AL clones. We also detected similarity between AL clones deposited in multiple organs of systemic AL patients. In summary, AL proteomic data sets are rich in LCV region peptides of potential clinical significance that are recoverable with advanced bioinformatics.
F1000 - Post-publication peer review of the biomedical literature, 2000
The Molecular Basis of B-Cell Differentiation and Function, 1986
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000
F1000 - Post-publication peer review of the biomedical literature, 2000