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Article ; Online: Higher levels of von Willebrand factor in hospitalised patient plasma provides an explanation for the association of ABO blood group and secretor status with COVID19 severity.

Mankelow, Tosti J / Blair, Allison / Arnold, David T / Hamilton, Fergus W / Gillespie, Kathleen M / Anstee, David J / Toye, Ashley M

Transfusion medicine (Oxford, England)

2022 Volume 32, Issue 3, Page(s) 261–262

MeSH term(s)	ABO Blood-Group System/genetics ; Blood Grouping and Crossmatching ; COVID-19 ; Factor VIII ; Humans ; von Willebrand Factor/genetics
Chemical Substances	ABO Blood-Group System ; von Willebrand Factor ; Factor VIII (9001-27-8)
Language	English
Publishing date	2022-03-24
Publishing country	England
Document type	Letter
ZDB-ID	1067989-3
ISSN	1365-3148 ; 0958-7578
ISSN (online)	1365-3148
ISSN	0958-7578
DOI	10.1111/tme.12860
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Article ; Online: Large red cell-derived membrane particles are major contributors to hypercoagulability in sickle cell disease.

Smith, Rachel A / Mankelow, Tosti J / Drizou, Despoina / Bullock, Thomas / Latham, Tom / Trompeter, Sara / Blair, Allison / Anstee, David J

Scientific reports

2021 Volume 11, Issue 1, Page(s) 11035

Abstract: Sickle cell disease (SCD) is one of the most common inherited single gene disorders. Polymerisation of sickle hemoglobin results in erythrocytes that are inflexible and adherent, leading to coagulation, vascular and cellular activation and resultant ... ...

Abstract	Sickle cell disease (SCD) is one of the most common inherited single gene disorders. Polymerisation of sickle hemoglobin results in erythrocytes that are inflexible and adherent, leading to coagulation, vascular and cellular activation and resultant blood vessel blockage. Previous studies have observed elevated numbers of red cell-derived particles (RCDP), also denoted extracellular vesicles, in SCD plasma. Here, imaging flow cytometry was used to quantify all RCDP in SCD plasma. A more heterogenous population of RCDP was observed than previously reported. Significantly, large right side-out red cell macrovesicles (MaV), 7 µm in diameter, were identified. Most RCDP were right side-out but a minor population of inside-out vesicles was also present. Electron micrographs confirmed the heterogenous nature of the RCDP detected. All MaV are decorated with prothrombotic phosphatidylserine (PS) and their removal from plasma lengthened clotting times by more than three-fold. Removal of all right side-out RCDP from SCD patient plasma samples resulted in a seven-fold increase in clotting time. These results indicate that MaV comprise a large area of prothrombotic membrane and are thus major contributors to hypercoagulation in SCD. Consequently, controlled removal of MaV and PS exposed RCDP from plasma could provide a novel therapy for managing this disease.
MeSH term(s)	Anemia, Sickle Cell ; Blood Coagulation ; Erythrocyte Membrane ; Phosphatidylserines/metabolism ; Thrombin/metabolism ; Thrombophilia
Chemical Substances	Phosphatidylserines ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2021-05-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-90477-z
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Article ; Online: Large red cell-derived membrane particles are major contributors to hypercoagulability in sickle cell disease

Rachel A. Smith / Tosti J. Mankelow / Despoina Drizou / Thomas Bullock / Tom Latham / Sara Trompeter / Allison Blair / David J. Anstee

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 9

Abstract: Abstract Sickle cell disease (SCD) is one of the most common inherited single gene disorders. Polymerisation of sickle hemoglobin results in erythrocytes that are inflexible and adherent, leading to coagulation, vascular and cellular activation and ... ...

Abstract	Abstract Sickle cell disease (SCD) is one of the most common inherited single gene disorders. Polymerisation of sickle hemoglobin results in erythrocytes that are inflexible and adherent, leading to coagulation, vascular and cellular activation and resultant blood vessel blockage. Previous studies have observed elevated numbers of red cell-derived particles (RCDP), also denoted extracellular vesicles, in SCD plasma. Here, imaging flow cytometry was used to quantify all RCDP in SCD plasma. A more heterogenous population of RCDP was observed than previously reported. Significantly, large right side-out red cell macrovesicles (MaV), 7 µm in diameter, were identified. Most RCDP were right side-out but a minor population of inside-out vesicles was also present. Electron micrographs confirmed the heterogenous nature of the RCDP detected. All MaV are decorated with prothrombotic phosphatidylserine (PS) and their removal from plasma lengthened clotting times by more than three-fold. Removal of all right side-out RCDP from SCD patient plasma samples resulted in a seven-fold increase in clotting time. These results indicate that MaV comprise a large area of prothrombotic membrane and are thus major contributors to hypercoagulation in SCD. Consequently, controlled removal of MaV and PS exposed RCDP from plasma could provide a novel therapy for managing this disease.
Keywords	Medicine ; R ; Science ; Q
Subject code	610
Language	English
Publishing date	2021-05-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Blood group type A secretors are associated with a higher risk of COVID-19 cardiovascular disease complications.

EJHaem

2021 Volume 2, Issue 2, Page(s) 175–187

Abstract: The SARS-CoV-2 virus causes COVID-19, an infection capable of causing severe disease and death but which can also be asymptomatic or oligosymptomatic. We investigated whether ABO blood group or secretor status was associated with COVID-19 severity. We ... ...

Abstract	The SARS-CoV-2 virus causes COVID-19, an infection capable of causing severe disease and death but which can also be asymptomatic or oligosymptomatic. We investigated whether ABO blood group or secretor status was associated with COVID-19 severity. We investigated secretor status because expression of ABO glycans on secreted proteins and non-erythroid cells are controlled by a fucosyltransferase (FUT2), and inactivating FUT2 mutations result in a non-secretor phenotype which protects against some viral infections. Data combined from healthcare records and our own laboratory tests (
Language	English
Publishing date	2021-04-02
Publishing country	United States
Document type	Journal Article
ISSN	2688-6146
ISSN (online)	2688-6146
DOI	10.1002/jha2.180
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Article ; Online: The ins and outs of reticulocyte maturation revisited: The role of autophagy in sickle cell disease.

Mankelow, Tosti J / Griffiths, Rebecca E / Trompeter, Sara / Flatt, Joanna F / Cogan, Nicola M / Massey, Edwin J / Anstee, David J

Autophagy

2016 Volume 12, Issue 3, Page(s) 590–591

Abstract: Autophagy plays an important role in the removal of membrane bound organelles during the last stage of erythropoiesis as the enucleate reticulocyte matures into the erythrocyte. Autophagic vesicles are expelled from the reticulocyte as intact, inside-out, ...

Abstract	Autophagy plays an important role in the removal of membrane bound organelles during the last stage of erythropoiesis as the enucleate reticulocyte matures into the erythrocyte. Autophagic vesicles are expelled from the reticulocyte as intact, inside-out, phosphatidylserine (PS) decorated vesicles and are subsequently removed during splenic passage. Failure to remove these vesicles causes the elevation in PS exposed red cells in Sickle Cell Disease.
MeSH term(s)	Anemia, Sickle Cell/pathology ; Autophagy ; Cell Differentiation ; Cytoplasmic Vesicles/metabolism ; Humans ; Models, Biological ; Reticulocytes/cytology
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2015.1125072
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Article ; Online: Non-muscle myosin II drives vesicle loss during human reticulocyte maturation.

Moura, Pedro L / Hawley, Bethan R / Mankelow, Tosti J / Griffiths, Rebecca E / Dobbe, Johannes G G / Streekstra, Geert J / Anstee, David J / Satchwell, Timothy J / Toye, Ashley M

Haematologica

2018 Volume 103, Issue 12, Page(s) 1997–2007

Abstract: The process of maturation of reticulocytes into fully mature erythrocytes that occurs in the circulation is known to be characterized by a complex interplay between loss of cell surface area and volume, removal of remnant cell organelles and redundant ... ...

Abstract	The process of maturation of reticulocytes into fully mature erythrocytes that occurs in the circulation is known to be characterized by a complex interplay between loss of cell surface area and volume, removal of remnant cell organelles and redundant proteins, and highly selective membrane and cytoskeletal remodeling. However, the mechanisms that underlie and drive these maturational processes
MeSH term(s)	Cell Differentiation ; Cells, Cultured ; Cytoplasmic Vesicles/metabolism ; Cytoskeletal Proteins/metabolism ; Erythrocytes/cytology ; Erythrocytes/metabolism ; Erythropoiesis ; Humans ; Molecular Motor Proteins/metabolism ; Myosin Heavy Chains/metabolism ; Myosin Type II/metabolism ; Phosphorylation ; Proteomics/methods ; Reticulocytes/cytology ; Reticulocytes/metabolism
Chemical Substances	Cytoskeletal Proteins ; MYH9 protein, human ; Molecular Motor Proteins ; Myosin Type II (EC 3.6.1.-) ; Myosin Heavy Chains (EC 3.6.4.1)
Language	English
Publishing date	2018-08-03
Publishing country	Italy
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2333-4
ISSN	1592-8721 ; 0017-6567 ; 0390-6078
ISSN (online)	1592-8721
ISSN	0017-6567 ; 0390-6078
DOI	10.3324/haematol.2018.199083
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Article ; Online: Autophagic vesicles on mature human reticulocytes explain phosphatidylserine-positive red cells in sickle cell disease.

Mankelow, Tosti J / Griffiths, Rebecca E / Trompeter, Sara / Flatt, Joanna F / Cogan, Nicola M / Massey, Edwin J / Anstee, David J

Blood

2015 Volume 126, Issue 15, Page(s) 1831–1834

Abstract: During maturation to an erythrocyte, a reticulocyte must eliminate any residual organelles and reduce its surface area and volume. Here we show this involves a novel process whereby large, intact, inside-out phosphatidylserine (PS)-exposed autophagic ... ...

Abstract	During maturation to an erythrocyte, a reticulocyte must eliminate any residual organelles and reduce its surface area and volume. Here we show this involves a novel process whereby large, intact, inside-out phosphatidylserine (PS)-exposed autophagic vesicles are extruded. Cell surface PS is a well-characterized apoptotic signal initiating phagocytosis. In peripheral blood from patients after splenectomy or in patients with sickle cell disease (SCD), the number of circulating red cells exposing PS on their surface is elevated. We show that in these patients PS is present on the cell surface of red cells in large (∼1.4 µm) discrete areas corresponding to autophagic vesicles. The autophagic vesicles found on reticulocytes are identical to those observed on red cells from splenectomized individuals and patients with SCD. Our data suggest the increased thrombotic risk associated with splenectomy, and patients with hemoglobinopathies is a possible consequence of increased levels of circulating mature reticulocytes expressing inside-out PS-exposed autophagic vesicles because of asplenia.
MeSH term(s)	Anemia, Sickle Cell/blood ; Anemia, Sickle Cell/pathology ; Autophagy ; Blotting, Western ; Case-Control Studies ; Cell Proliferation ; Cells, Cultured ; Erythrocytes/metabolism ; Erythrocytes/pathology ; Flow Cytometry ; Glycophorins/metabolism ; Humans ; Image Processing, Computer-Assisted ; Phagocytosis ; Phosphatidylserines/chemistry ; Phosphatidylserines/metabolism ; Reticulocytes/metabolism ; Reticulocytes/pathology ; Splenectomy
Chemical Substances	Glycophorins ; Phosphatidylserines
Language	English
Publishing date	2015-08-14
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2015-04-637702
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Article ; Online: Tetraspanins CD81 and CD82 facilitate α4β1-mediated adhesion of human erythroblasts to vascular cell adhesion molecule-1.

Spring, Frances A / Griffiths, Rebecca E / Mankelow, Tosti J / Agnew, Christopher / Parsons, Stephen F / Chasis, Joel A / Anstee, David J

PloS one

2013 Volume 8, Issue 5, Page(s) e62654

Abstract: The proliferation and terminal differentiation of erythroid progenitors occurs in human bone marrow within erythroblastic islands, specialised structures consisting of a central macrophage surrounded by developing erythroid cells. Many cell-cell and cell- ...

Abstract	The proliferation and terminal differentiation of erythroid progenitors occurs in human bone marrow within erythroblastic islands, specialised structures consisting of a central macrophage surrounded by developing erythroid cells. Many cell-cell and cell-matrix adhesive interactions maintain and regulate the co-ordinated daily production of reticulocytes. Erythroid cells express only one integrin, α4β1, throughout differentiation, and its interactions with both macrophage Vascular Cell Adhesion Molecule-1 and with extracellular matrix fibronectin are critical for erythropoiesis. We observed that proerythroblasts expressed a broad tetraspanin phenotype, and investigated whether any tetraspanin could modulate integrin function. A specific association between α4β1 and CD81, CD82 and CD151 was demonstrated by confocal microscopy and co-immune precipitation. We observed that antibodies to CD81 and CD82 augmented adhesion of proerythroblasts to Vascular Cell Adhesion Molecule-1 but not to the fibronectin spliceoforms FnIII12-IIICS-15 and FnIII12-15. In contrast, different anti-CD151 antibodies augmented or inhibited adhesion of proerythroblasts to Vascular Cell Adhesion Molecule-1 and the fibronectin spliceoform FnIII12-IIICS-15 but not to FnIII12-15. These results strongly suggest that tetraspanins have a functional role in terminal erythropoiesis by modulating interactions of erythroblast α4β1 with both macrophages and extracellular matrix.
MeSH term(s)	Antibodies/pharmacology ; Basophils/cytology ; Cell Adhesion/drug effects ; Cell Differentiation/drug effects ; Cell Line ; Epitopes/immunology ; Erythroblasts/cytology ; Erythroblasts/metabolism ; Erythropoiesis/drug effects ; Fibronectins/metabolism ; Flow Cytometry ; Humans ; Immunoprecipitation ; Integrin alpha4beta1/metabolism ; Kangai-1 Protein/metabolism ; Ligands ; Microscopy, Confocal ; Platelet Glycoprotein GPIIb-IIIa Complex/metabolism ; Protein Transport/drug effects ; Reticulocytes/cytology ; Reticulocytes/drug effects ; Reticulocytes/metabolism ; Tetraspanin 24/metabolism ; Tetraspanin 28/metabolism ; Vascular Cell Adhesion Molecule-1/metabolism
Chemical Substances	Antibodies ; CD151 protein, human ; CD81 protein, human ; CD82 protein, human ; Epitopes ; Fibronectins ; Integrin alpha4beta1 ; Kangai-1 Protein ; Ligands ; Platelet Glycoprotein GPIIb-IIIa Complex ; Tetraspanin 24 ; Tetraspanin 28 ; Vascular Cell Adhesion Molecule-1
Language	English
Publishing date	2013-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0062654
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Article ; Online: Tetraspanins CD81 and CD82 facilitate α4β1-mediated adhesion of human erythroblasts to vascular cell adhesion molecule-1.

Frances A Spring / Rebecca E Griffiths / Tosti J Mankelow / Christopher Agnew / Stephen F Parsons / Joel A Chasis / David J Anstee

PLoS ONE, Vol 8, Iss 5, p e

2013 Volume 62654

Abstract	The proliferation and terminal differentiation of erythroid progenitors occurs in human bone marrow within erythroblastic islands, specialised structures consisting of a central macrophage surrounded by developing erythroid cells. Many cell-cell and cell-matrix adhesive interactions maintain and regulate the co-ordinated daily production of reticulocytes. Erythroid cells express only one integrin, α4β1, throughout differentiation, and its interactions with both macrophage Vascular Cell Adhesion Molecule-1 and with extracellular matrix fibronectin are critical for erythropoiesis. We observed that proerythroblasts expressed a broad tetraspanin phenotype, and investigated whether any tetraspanin could modulate integrin function. A specific association between α4β1 and CD81, CD82 and CD151 was demonstrated by confocal microscopy and co-immune precipitation. We observed that antibodies to CD81 and CD82 augmented adhesion of proerythroblasts to Vascular Cell Adhesion Molecule-1 but not to the fibronectin spliceoforms FnIII12-IIICS-15 and FnIII12-15. In contrast, different anti-CD151 antibodies augmented or inhibited adhesion of proerythroblasts to Vascular Cell Adhesion Molecule-1 and the fibronectin spliceoform FnIII12-IIICS-15 but not to FnIII12-15. These results strongly suggest that tetraspanins have a functional role in terminal erythropoiesis by modulating interactions of erythroblast α4β1 with both macrophages and extracellular matrix.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article: Investigation of the contribution of histidine 119 to the conduction of protons through human Nox2.

Mankelow, Tosti J / Hu, X Wen / Adams, Kate / Henderson, Lydia M

European journal of biochemistry

2004 Volume 271, Issue 20, Page(s) 4026–4033

Abstract: The conduction of protons through human Nox2 has previously been shown to be dependent upon His115. Alignment of sequences for both animal and plant Nox proteins indicated that histidines 115 and 119 are both highly conserved, while His111 was conserved ... ...

Abstract	The conduction of protons through human Nox2 has previously been shown to be dependent upon His115. Alignment of sequences for both animal and plant Nox proteins indicated that histidines 115 and 119 are both highly conserved, while His111 was conserved among animal homologues of Nox1-4. To investigate the possible role that these histidine residues might play in the conduction of protons through Nox2, we have introduced both paired and single mutations into these histidine residues. Each construct was used to generate a CHO cell line in which the expression of the mutated Nox2 was assessed. Nox2 was expressed in each of the CHO cell lines generated, however, the level of expression of H111/115L in CHO cells was lower and that of H111L very much reduced, compared to that of wild-type Nox2. The arachidonic acid activated proton flux was absent in the CHO cell lines expressing the mutations of H111/115L, H111/119L or H115/119L, compared to that observed for wild-type Nox2. Similarly only a small efflux of protons was observed from CHO cells expressing either H119L or H111L. In all cases the expected proton flux was elicited through the addition of the protonophore, carbonyl cyanide m-chlorophenylhydrazone. Conclusions regarding the role of His111 in the conduction of protons cannot be drawn due to the reduced expression. We can, however, conclude that His119, in addition to His115, is required for the conduction of protons through Nox2. His119 has been identified as a highly conserved residue for which no function has previously been proposed.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Arachidonic Acid/pharmacology ; CHO Cells ; Cattle ; Cricetinae ; Cricetulus ; Histidine/genetics ; Histidine/metabolism ; Humans ; Membrane Glycoproteins/drug effects ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Membrane Potentials/drug effects ; Membrane Potentials/physiology ; Membrane Proteins/genetics ; Mice ; Molecular Sequence Data ; Mutagenesis ; NADPH Oxidase 2 ; NADPH Oxidases/drug effects ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Protein Structure, Tertiary ; Proton Pumps/drug effects ; Proton Pumps/genetics ; Proton Pumps/metabolism ; Rabbits ; Rats ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Structure-Activity Relationship
Chemical Substances	Membrane Glycoproteins ; Membrane Proteins ; Proton Pumps ; Recombinant Proteins ; Arachidonic Acid (27YG812J1I) ; Histidine (4QD397987E) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2004-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1111/j.1432-1033.2004.04340.x
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