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Detection and isolation of cell-derived microparticles are compromised by protein complexes due to shared biophysical parameters


György, B; Módos, K; Pállinger, E; Pálóczi, K; Pásztói, M; Misják, P; Deli, M A; Sipos, A; Szalai, A; Voszka, I; Polgár, A; Tóth, K; Csete, M; Nagy, G; Gay, S; Falus, A; Kittel, A; Buzás, E I (2011). Detection and isolation of cell-derived microparticles are compromised by protein complexes due to shared biophysical parameters. Blood, 117(4):e39.

Abstract

Numerous diseases, recently reported to associate with elevated microvesicle/microparticle (MP) counts, have also long been known to be characterized by accelerated immune complex (IC) formation. The goal of this study was to investigate the potential overlap between parameters of protein complexes (e.g. ICs or avidin-biotin complexes) and MPs, which might perturb detection and/or isolation of MPs. In this work, after comprehensive characterization of MPs by electron microscopy, atomic force microscopy, dynamic light scattering analysis and flow cytometry, for the first time we drive attention to the fact that protein complexes, especially insoluble ICs, overlap in biophysical properties (size, light scattering, sedimentation) with MPs. This, in turn, affects MP quantification by flow cytometry and purification by differential centrifugation, especially in diseases in which IC formation is common, including not only autoimmune diseases, but also hematological disorders, infections and cancer. These data may necessitate reevaluation of certain published data on patient-derived MPs, and contribute to correct the clinical laboratory assessment of the presence and biological functions of MPs in health and disease.

Abstract

Numerous diseases, recently reported to associate with elevated microvesicle/microparticle (MP) counts, have also long been known to be characterized by accelerated immune complex (IC) formation. The goal of this study was to investigate the potential overlap between parameters of protein complexes (e.g. ICs or avidin-biotin complexes) and MPs, which might perturb detection and/or isolation of MPs. In this work, after comprehensive characterization of MPs by electron microscopy, atomic force microscopy, dynamic light scattering analysis and flow cytometry, for the first time we drive attention to the fact that protein complexes, especially insoluble ICs, overlap in biophysical properties (size, light scattering, sedimentation) with MPs. This, in turn, affects MP quantification by flow cytometry and purification by differential centrifugation, especially in diseases in which IC formation is common, including not only autoimmune diseases, but also hematological disorders, infections and cancer. These data may necessitate reevaluation of certain published data on patient-derived MPs, and contribute to correct the clinical laboratory assessment of the presence and biological functions of MPs in health and disease.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Rheumatology Clinic and Institute of Physical Medicine
Dewey Decimal Classification:610 Medicine & health
Language:English
Date:2011
Deposited On:24 Nov 2010 16:18
Last Modified:21 Nov 2017 15:00
Publisher:American Society of Hematology
ISSN:0006-4971
Publisher DOI:https://doi.org/10.1182/blood-2010-09-307595
PubMed ID:21041717

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