The Experts below are selected from a list of 153 Experts worldwide ranked by ideXlab platform
David L. Murray - One of the best experts on this subject based on the ideXlab platform.
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using matrix assisted laser desorption ionization time of flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid Communications in Mass Spectrometry, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
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Using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid communications in mass spectrometry : RCM, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
David R. Barnidge - One of the best experts on this subject based on the ideXlab platform.
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using matrix assisted laser desorption ionization time of flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid Communications in Mass Spectrometry, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
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Using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid communications in mass spectrometry : RCM, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
Michel Cogné - One of the best experts on this subject based on the ideXlab platform.
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Animal models of monoclonal Immunoglobulin-related renal diseases
Nature Reviews Nephrology, 2018Co-Authors: Christophe Sirac, Sebastien Bender, Maria Victoria Ayala, Jiamin Teng, Elba A. Turbat-herrera, Vecihi Batuman, Paul W Sanders, Vincent Javaugue, Guillermo A. Herrera, Michel CognéAbstract:Monoclonal Immunoglobulin deposition produces complex diseases with heterogeneous phenotypes, making it difficult to identify the underlying mechanisms of Immunoglobulin aggregation and deposition. In this Review, the authors discuss animal models of various human Immunoglobulin deposition diseases, and each model's drawbacks and contributions to our understanding of these diseases. The renal deposition of monoclonal Immunoglobulins can cause severe renal complications in patients with B cell and plasma cell lymphoproliferative disorders. The overproduction of a structurally unique Immunoglobulin can contribute to the abnormal propensity of monoclonal Immunoglobulins to aggregate and deposit in specific organs. A wide range of renal diseases can occur in multiple myeloma or monoclonal gammopathy of renal significance, including tubular and glomerular disorders with organized or unorganized Immunoglobulin deposits. The development of reliable experimental models is challenging owing to the inherent variability of Immunoglobulins and the heterogeneity of the pathologies they produce. However, although imperfect, animal models are invaluable tools to understand the molecular pathogenesis of these diseases, and advances in creating genetically modified animals might provide novel approaches to evaluate innovative therapeutic interventions. We discuss the strategies employed to reproduce human monoclonal Immunoglobulin-induced kidney lesions in animal models, and we highlight their advantages and shortcomings. We also discuss how these models have affected the management of these deposition diseases and might do so in the future. Finally, we discuss hypotheses that explain some limitations of the various models, and how these models might improve our understanding of other nephropathies without Immunoglobulin involvement that have similar pathogenic mechanisms. Numerous renal diseases occur owing to the deposition of a monoclonal Immunoglobulin, including multiple myeloma and monoclonal gammopathy of renal significance Understanding the molecular pathogenesis of human Immunoglobulin deposition diseases and testing new therapeutic strategies requires relevant animal models, which is a challenge owing to the heterogeneity of these diseases Models based on the injection of purified human Immunoglobulins and on tumour grafts that produce the monoclonal Immunoglobulin have revealed several early pathogenic events in Immunoglobulin deposition and demonstrated the efficacy of innovative therapeutic agents Advances in transgenic techniques have allowed the creation of mouse models that faithfully reproduce the human diseases and have aided in unravelling the pathogenic mechanisms of monoclonal Immunoglobulin deposition Animal models are invaluable tools to study the process of deposition and to explore the direct toxicity of monoclonal Immunoglobulins in tissues and Immunoglobulin-producing plasma cells
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animal models of monoclonal Immunoglobulin related renal diseases
Nature Reviews Nephrology, 2018Co-Authors: Christophe Sirac, Sebastien Bender, Maria Victoria Ayala, Jiamin Teng, Vecihi Batuman, Paul W Sanders, Vincent Javaugue, Guillermo A. Herrera, Elba A Turbatherrera, Michel CognéAbstract:The renal deposition of monoclonal Immunoglobulins can cause severe renal complications in patients with B cell and plasma cell lymphoproliferative disorders. The overproduction of a structurally unique Immunoglobulin can contribute to the abnormal propensity of monoclonal Immunoglobulins to aggregate and deposit in specific organs. A wide range of renal diseases can occur in multiple myeloma or monoclonal gammopathy of renal significance, including tubular and glomerular disorders with organized or unorganized Immunoglobulin deposits. The development of reliable experimental models is challenging owing to the inherent variability of Immunoglobulins and the heterogeneity of the pathologies they produce. However, although imperfect, animal models are invaluable tools to understand the molecular pathogenesis of these diseases, and advances in creating genetically modified animals might provide novel approaches to evaluate innovative therapeutic interventions. We discuss the strategies employed to reproduce human monoclonal Immunoglobulin-induced kidney lesions in animal models, and we highlight their advantages and shortcomings. We also discuss how these models have affected the management of these deposition diseases and might do so in the future. Finally, we discuss hypotheses that explain some limitations of the various models, and how these models might improve our understanding of other nephropathies without Immunoglobulin involvement that have similar pathogenic mechanisms.
Thomas P. Krick - One of the best experts on this subject based on the ideXlab platform.
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using matrix assisted laser desorption ionization time of flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid Communications in Mass Spectrometry, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
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Using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid communications in mass spectrometry : RCM, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
Timothy J. Griffin - One of the best experts on this subject based on the ideXlab platform.
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using matrix assisted laser desorption ionization time of flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid Communications in Mass Spectrometry, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
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Using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry to detect monoclonal Immunoglobulin light chains in serum and urine
Rapid communications in mass spectrometry : RCM, 2015Co-Authors: David R. Barnidge, Thomas P. Krick, Timothy J. Griffin, David L. MurrayAbstract:Rationale Use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) to monitor serum and urine samples for endogenous monoclonal Immunoglobulins. MALDI-TOFMS is faster, fully automatable, and provides superior specificity compared to protein gel electrophoresis (PEL). Methods Samples were enriched for Immunoglobulins in 5 min using Melon Gel™ followed by reduction with dithiothreitol for 15 min to separate Immunoglobulin light chains and heavy chains. Samples were then desalted using C4 ZipTips, mixed with sinapinic acid matrix, and analyzed on a Bruker Biflex III MALDI-TOF mass spectrometer. Results Monoclonal Immunoglobulin light chains were identified in serum and urine samples from patients with a known monoclonal gammopathy using MALDI-TOFMS with minimal sample preparation. Conclusions MALDI-TOFMS can identify a monoclonal Immunoglobulin in serum and urine samples. The molecular mass of the monoclonal Immunoglobulin light chain is obtained providing unprecedented specificity compared to PEL. In addition, the methodology can be automated, making it a practical alternative to PEL. Copyright © 2015 John Wiley & Sons, Ltd.
