Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/87031
Title: Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation
Authors: Chu, Trang T. T.
Sinha, Ameya
Malleret, Benoit
Suwanarusk, Rossarin
Park, Jung Eun
Naidu, Renugah
Das, Rupambika
Dutta, Bamaprasad
Ong, Seow Theng
Verma, Navin Kumar
Chan, Jerry K.
Nosten, François
Rénia, Laurent
Sze, Siu Kwan
Russell, Bruce
Chandramohanadas, Rajesh
Keywords: Red Blood Cells
Reticulocytes
Issue Date: 2017
Source: Chu, T. T. T., Sinha, A., Malleret, B., Suwanarusk, R., Park, J. E., Naidu, R., et al. (2018). Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. British Journal of Haematology, 180(1), 118-133.
Series/Report no.: British Journal of Haematology
Abstract: Erythropoiesis is marked by progressive changes in morphological, biochemical and mechanical properties of erythroid precursors to generate red blood cells (RBC). The earliest enucleated forms derived in this process, known as reticulocytes, are multi-lobular and spherical. As reticulocytes mature, they undergo a series of dynamic cytoskeletal re-arrangements and the expulsion of residual organelles, resulting in highly deformable biconcave RBCs (normocytes). To understand the significant, yet neglected proteome-wide changes associated with reticulocyte maturation, we undertook a quantitative proteomics approach. Immature reticulocytes (marked by the presence of surface transferrin receptor, CD71) and mature RBCs (devoid of CD71) were isolated from human cord blood using a magnetic separation procedure. After sub-fractionation into triton-extracted membrane proteins and luminal samples (isobaric tags for relative and absolute quantitation), quantitative mass spectrometry was conducted to identify more than 1800 proteins with good confidence and coverage. While most structural proteins (such as Spectrins, Ankyrin and Band 3) as well as surface glycoproteins were conserved, proteins associated with microtubule structures, such as Talin-1/2 and ß-Tubulin, were detected only in immature reticulocytes. Atomic force microscopy (AFM)-based imaging revealed an extended network of spectrin filaments in reticulocytes (with an average length of 48 nm), which shortened during reticulocyte maturation (average spectrin length of 41 nm in normocytes). The extended nature of cytoskeletal network may partly account for increased deformability and shape changes, as reticulocytes transform to normocytes.
URI: https://hdl.handle.net/10356/87031
http://hdl.handle.net/10220/44297
ISSN: 0007-1048
DOI: http://dx.doi.org/10.1111/bjh.14976
Rights: © 2017 John Wiley & Sons Ltd. This is the author created version of a work that has been peer reviewed and accepted for publication by British Journal of Haematology, John Wiley & Sons Ltd. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1111/bjh.14976].
Fulltext Permission: open
Fulltext Availability: With Fulltext
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