A human anti-matriptase-2 antibody limits iron overload, α-globin aggregates, and splenomegaly in β-thalassemic mice Article Swipe
Matthew Wake
,
Anaïs Palin
,
Audrey Belot
,
Mathieu Berger
,
Megane Lorgouilloux
,
Margot Bichon
,
Jonathan Papworth
,
Luke Bayliss
,
Benjamin Grimshaw
,
Natalie K. Rynkiewicz
,
Jemima Paterson
,
Alicia Poindron
,
Erin Spearing
,
Emily Carter
,
Robyne Hudson
,
Millie Campbell
,
Verena Petzer
,
Céline Besson‐Fournier
,
Chloé Latour
,
Amélie Largounez
,
Ophélie Gourbeyre
,
Alexis Fay
,
Hélène Coppin
,
Marie‐Paule Roth
,
Igor Theurl
,
Volker Germaschewski
,
Delphine Meynard
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1182/bloodadvances.2023012010
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1182/bloodadvances.2023012010
Iron plays a major role in the deterioration of β-thalassemia. Indeed, the high levels of transferrin saturation and iron delivered to erythroid progenitors are associated with production of α-globin precipitates that negatively affect erythropoiesis. Matriptase-2/TMPRSS6, a membrane-bound serine protease expressed in hepatocytes, negatively modulates hepcidin production and thus is a key target to prevent iron overload in β-thalassemia. To address safety concerns raised by the suppression of Tmprss6 by antisense oligonucleotides or small interfering RNA, we tested a fully human anti-matriptase-2 antibody, RLYB331, which blocks the protease activity of matriptase-2. When administered weekly to Hbbth3/+ mice, RLYB331 induced hepcidin expression, reduced iron loading, prevented the formation of toxic α-chain/heme aggregates, reduced ros oxygen species formation, and improved reticulocytosis and splenomegaly. To increase the effectiveness of RLYB331 in β-thalassemia treatment even further, we administered RLYB331 in combination with RAP-536L, a ligand-trapping protein that contains the extracellular domain of activin receptor type IIB and alleviates anemia by promoting differentiation of late-stage erythroid precursors. RAP-536L alone did not prevent iron overload but significantly reduced apoptosis in the erythroid populations of the bone marrow, normalized red blood cell counts, and improved hemoglobin and hematocrit levels. Interestingly, the association of RLYB331 with RAP-536L entirely reversed the β-thalassemia phenotype in Hbbth3/+ mice and simultaneously corrected iron overload, ineffective erythropoiesis, splenomegaly, and hematological parameters, suggesting that a multifunctional molecule consisting of the fusion of RLYB331 with luspatercept (human version of RAP-536L) would allow administration of a single medication addressing simultaneously the different pathophysiological aspects of β-thalassemia.
Related Topics
Concepts
Hepcidin
Ineffective erythropoiesis
Erythropoiesis
Transferrin receptor
TMPRSS6
Internal medicine
Hemoglobin
Anemia
Endocrinology
Beta thalassemia
Chemistry
Cell biology
Biology
Thalassemia
Serine protease
Transferrin
Biochemistry
Protease
Medicine
Enzyme
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1182/bloodadvances.2023012010
- https://ashpublications.org/bloodadvances/article-pdf/doi/10.1182/bloodadvances.2023012010/2210658/bloodadvances.2023012010.pdf
- OA Status
- gold
- Cited By
- 6
- References
- 35
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4391017468
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W4391017468Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1182/bloodadvances.2023012010Digital Object Identifier
- Title
-
A human anti-matriptase-2 antibody limits iron overload, α-globin aggregates, and splenomegaly in β-thalassemic miceWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-01-19Full publication date if available
- Authors
-
Matthew Wake, Anaïs Palin, Audrey Belot, Mathieu Berger, Megane Lorgouilloux, Margot Bichon, Jonathan Papworth, Luke Bayliss, Benjamin Grimshaw, Natalie K. Rynkiewicz, Jemima Paterson, Alicia Poindron, Erin Spearing, Emily Carter, Robyne Hudson, Millie Campbell, Verena Petzer, Céline Besson‐Fournier, Chloé Latour, Amélie Largounez, Ophélie Gourbeyre, Alexis Fay, Hélène Coppin, Marie‐Paule Roth, Igor Theurl, Volker Germaschewski, Delphine MeynardList of authors in order
- Landing page
-
https://doi.org/10.1182/bloodadvances.2023012010Publisher landing page
- PDF URL
-
https://ashpublications.org/bloodadvances/article-pdf/doi/10.1182/bloodadvances.2023012010/2210658/bloodadvances.2023012010.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://ashpublications.org/bloodadvances/article-pdf/doi/10.1182/bloodadvances.2023012010/2210658/bloodadvances.2023012010.pdfDirect OA link when available
- Concepts
-
Hepcidin, Ineffective erythropoiesis, Erythropoiesis, Transferrin receptor, TMPRSS6, Internal medicine, Hemoglobin, Anemia, Endocrinology, Beta thalassemia, Chemistry, Cell biology, Biology, Thalassemia, Serine protease, Transferrin, Biochemistry, Protease, Medicine, EnzymeTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
6Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 1, 2024: 5Per-year citation counts (last 5 years)
- References (count)
-
35Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.antisense | 70 |
| abstract_inverted_index.apoptosis | 172 |
| abstract_inverted_index.corrected | 209 |
| abstract_inverted_index.delivered | 20 |
| abstract_inverted_index.different | 245 |
| abstract_inverted_index.erythroid | 22, 160, 175 |
| abstract_inverted_index.expressed | 40 |
| abstract_inverted_index.formation | 106 |
| abstract_inverted_index.modulates | 44 |
| abstract_inverted_index.overload, | 211 |
| abstract_inverted_index.phenotype | 203 |
| abstract_inverted_index.prevented | 104 |
| abstract_inverted_index.promoting | 156 |
| abstract_inverted_index.treatment | 129 |
| abstract_inverted_index.α-globin | 29 |
| abstract_inverted_index.addressing | 242 |
| abstract_inverted_index.alleviates | 153 |
| abstract_inverted_index.associated | 25 |
| abstract_inverted_index.consisting | 223 |
| abstract_inverted_index.formation, | 115 |
| abstract_inverted_index.hematocrit | 190 |
| abstract_inverted_index.hemoglobin | 188 |
| abstract_inverted_index.late-stage | 159 |
| abstract_inverted_index.medication | 241 |
| abstract_inverted_index.negatively | 32, 43 |
| abstract_inverted_index.normalized | 181 |
| abstract_inverted_index.production | 27, 46 |
| abstract_inverted_index.saturation | 17 |
| abstract_inverted_index.suggesting | 218 |
| abstract_inverted_index.aggregates, | 110 |
| abstract_inverted_index.association | 194 |
| abstract_inverted_index.combination | 136 |
| abstract_inverted_index.expression, | 100 |
| abstract_inverted_index.ineffective | 212 |
| abstract_inverted_index.interfering | 74 |
| abstract_inverted_index.parameters, | 217 |
| abstract_inverted_index.populations | 176 |
| abstract_inverted_index.precursors. | 161 |
| abstract_inverted_index.progenitors | 23 |
| abstract_inverted_index.suppression | 66 |
| abstract_inverted_index.transferrin | 16 |
| abstract_inverted_index.administered | 92, 133 |
| abstract_inverted_index.hepatocytes, | 42 |
| abstract_inverted_index.luspatercept | 230 |
| abstract_inverted_index.precipitates | 30 |
| abstract_inverted_index.deterioration | 8 |
| abstract_inverted_index.effectiveness | 124 |
| abstract_inverted_index.extracellular | 145 |
| abstract_inverted_index.hematological | 216 |
| abstract_inverted_index.matriptase-2. | 90 |
| abstract_inverted_index.significantly | 170 |
| abstract_inverted_index.splenomegaly, | 214 |
| abstract_inverted_index.splenomegaly. | 120 |
| abstract_inverted_index.α-chain/heme | 109 |
| abstract_inverted_index.Interestingly, | 192 |
| abstract_inverted_index.administration | 237 |
| abstract_inverted_index.membrane-bound | 37 |
| abstract_inverted_index.simultaneously | 208, 243 |
| abstract_inverted_index.β-thalassemia | 128, 202 |
| abstract_inverted_index.differentiation | 157 |
| abstract_inverted_index.erythropoiesis, | 213 |
| abstract_inverted_index.erythropoiesis. | 34 |
| abstract_inverted_index.ligand-trapping | 140 |
| abstract_inverted_index.multifunctional | 221 |
| abstract_inverted_index.reticulocytosis | 118 |
| abstract_inverted_index.β-thalassemia. | 10, 58, 249 |
| abstract_inverted_index.oligonucleotides | 71 |
| abstract_inverted_index.anti-matriptase-2 | 81 |
| abstract_inverted_index.pathophysiological | 246 |
| abstract_inverted_index.Matriptase-2/TMPRSS6, | 35 |
| cited_by_percentile_year.max | 98 |
| cited_by_percentile_year.min | 91 |
| countries_distinct_count | 3 |
| institutions_distinct_count | 27 |
| sustainable_development_goals[0].id | https://metadata.un.org/sdg/3 |
| sustainable_development_goals[0].score | 0.5899999737739563 |
| sustainable_development_goals[0].display_name | Good health and well-being |
| citation_normalized_percentile.value | 0.92094166 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | True |