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  1. Article ; Online: Single-site, five-year experience with human eosinophil isolation by density gradient centrifugation and CD16 immunomagnetic negative separation

    Yun Cao / Sooncheon Shin / Daniela J. Carroll / Jeremy A. O’Sullivan / Bruce S. Bochner

    BMC Research Notes, Vol 13, Iss 1, Pp 1-

    2020  Volume 5

    Abstract: Abstract Objective Little has been reported regarding the reliability of methods for the purification of human blood eosinophils. We retrospectively reviewed our experience with 350 consecutive eosinophil isolations. Results Between January 2014 and ... ...

    Abstract Abstract Objective Little has been reported regarding the reliability of methods for the purification of human blood eosinophils. We retrospectively reviewed our experience with 350 consecutive eosinophil isolations. Results Between January 2014 and December 2018, we conducted 350 eosinophil purifications from 83 donors. Absolute eosinophil count (AEC), calculated from hospital complete blood counts when available (n = 289), ranged from 32 to 1352 eosinophils/µL ( $$\bar{x} \pm {\text{SD}}$$ x ¯ ± SD : 179 ± 136/µL). Eosinophil yields ranged from 0.4 to 24.4 million cells per 20 mL of blood drawn ( $$\bar{x} \pm {\text{SD}}$$ x ¯ ± SD : 3.1 ± 1.9 million eosinophils) with > 98% purity. Comparing AEC to actual yield, recovery was 87% ± 29% ( $$\bar{x} \pm {\text{SD}}$$ x ¯ ± SD ) and AEC strongly correlated with yield. To explore the reproducibility of yield, a subsequent analysis was limited to those donors drawn ≥ 3 times (N = 35), and there was no difference in the average coefficient of variation for yield between allergic and non-allergic donors. Viability of isolated eosinophils was consistently > 95% and after 24 h of culture did not differ between allergic and non-allergic donors. We conclude that this immunomagnetic separation method for human eosinophil isolation from whole blood is a reliable, reproducible technique for obtaining an average of 87% yield with high purity and viability.
    Keywords Human eosinophil purification ; Blood ; Methods ; Purity ; Yield ; Immunomagnetic separation ; Medicine ; R ; Biology (General) ; QH301-705.5 ; Science (General) ; Q1-390
    Subject code 610
    Language English
    Publishing date 2020-04-01T00:00:00Z
    Publisher BMC
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Glycobiology of Eosinophilic Inflammation

    Jeremy A. O’Sullivan / Daniela J. Carroll / Bruce S. Bochner

    Frontiers in Medicine, Vol

    Contributions of Siglecs, Glycans, and Other Glycan-Binding Proteins

    2017  Volume 4

    Abstract: The historical focus on protein–protein interactions in biological systems, at the expense of attention given to interactions between other classes of molecules, has overlooked important and clinically relevant processes and points of potential clinical ... ...

    Abstract The historical focus on protein–protein interactions in biological systems, at the expense of attention given to interactions between other classes of molecules, has overlooked important and clinically relevant processes and points of potential clinical intervention. For example, the significance of protein–carbohydrate interactions, especially in the regulation of immune responses, has recently received greater recognition and appreciation. This review discusses several ways by which cell-surface lectin–glycan interactions can modulate eosinophil function, particularly at the levels of eosinophil recruitment and survival, and how such interactions can be exploited therapeutically. A primary focus is on discoveries concerning Siglec-8, a glycan-binding protein selectively expressed on human eosinophils, and its closest functional paralog in the mouse, Siglec-F. Recent advances in the synthesis of polymeric ligands, the identification of physiological ligands for Siglec-8 and Siglec-F in the airway, and the determination of the basis of glycan ligand discrimination of Siglec-8 are discussed. Important similarities and differences between these siglecs are outlined. Eosinophil expression of additional glycan-binding proteins or their glycan ligands, including interactions involving members of the selectin, galectin, and siglec families, is summarized. The roles of these molecules in eosinophil recruitment, survival, and inflammation are described. Finally, the modulation of these interactions and potential therapeutic exploitation of glycan-binding proteins and their ligands to ameliorate eosinophil-associated diseases are considered.
    Keywords eosinophils ; Siglec-8 ; Siglec-F ; selectins ; galectins ; glycans ; Medicine (General) ; R5-920
    Language English
    Publishing date 2017-08-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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