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Pathology Research

Research Overview

Sarah Ducamp’s research is focused on identifying new genes responsible for Congenital Sideroblastic Anemias (CSAs) and on developing new models of these diseases using different approaches such as genome editing. CSAs’ genes are involved in different mitochondrial pathways, including heme biosynthesis, iron-sulfur cluster assembly, oxidative phosphorylation and translation. Sarah aims to understand why iron accumulates inside the mitochondria of CSAs patients’ erythroid cells and to develop new strategies to cure those diseases.

Research Background

Sarah Ducamp earned her PhD in 2011 at the Pierre and Marie Curie University in Paris, France. Her thesis was conducted in the Beaumont Lab and notably allowed the identification of new genes responsible for erythropoietic protoporphyria (EPP). After her defense, she joined the Mayeux Lab at the Cochin Institute in Paris and focused her research on human normal and pathological erythropoiesis. In 2016, she joined the Fleming Lab to continue her work on rare inherited and erythroid diseases at Boston Children’s Hospital. Meanwhile, Sarah also joined the BCH Postdoctoral Association. She served as co-chair of the Career Development Committee for 18 months, and she is currently co-chair of the Public Affair Committee.

Publications

  1. Engineered bacterial lipoate protein ligase A (lplA) restores lipoylation in cell models of lipoylation deficiency. J Biol Chem. 2024 Nov 14; 300(12):107995. View Abstract
  2. Murine models of erythroid 5ALA synthesis disorders and their conditional synthetic lethal dependency on pyridoxine. Blood. 2024 09 26; 144(13):1418-1432. View Abstract
  3. Comprehensive Genomic Analysis Identifies a Diverse Landscape of Sideroblastic and Nonsideroblastic Iron-Related Anemias with Novel and Pathogenic Variants in an Iron-Deficient Endemic Setting. J Mol Diagn. 2024 05; 26(5):430-444. View Abstract
  4. Folate depletion induces erythroid differentiation through perturbation of de novo purine synthesis. Sci Adv. 2024 Feb 02; 10(5):eadj9479. View Abstract
  5. Physiology of Red Cell Lineage: From Erythroblast Progenitors to Mature Red Blood Cell. Int J Mol Sci. 2023 Jun 03; 24(11). View Abstract
  6. Prospective observational pilot study of quantitative light dosimetry in erythropoietic protoporphyria. J Am Acad Dermatol. 2023 05; 88(5):1148-1151. View Abstract
  7. A mutation in the iron-responsive element of ALAS2 is a modifier of disease severity in a patient suffering from CLPX associated erythropoietic protoporphyria. Haematologica. 2021 07 01; 106(7):2030-2033. View Abstract
  8. p53 activation during ribosome biogenesis regulates normal erythroid differentiation. Blood. 2021 01 07; 137(1):89-102. View Abstract
  9. Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia. J Clin Invest. 2020 10 01; 130(10):5245-5256. View Abstract
  10. Evidence in the UK Biobank for the underdiagnosis of erythropoietic protoporphyria. Genet Med. 2021 01; 23(1):140-148. View Abstract
  11. XPO1 regulates erythroid differentiation and is a new target for the treatment of ß-thalassemia. Haematologica. 2020 09 01; 105(9):2240-2249. View Abstract
  12. XPO1 regulates erythroid differentiation and is a new target for the treatment of ß-thalassemia. Haematologica. 2019 Nov 21. View Abstract
  13. The molecular genetics of sideroblastic anemia. Blood. 2019 01 03; 133(1):59-69. View Abstract
  14. Finely-tuned regulation of AMP-activated protein kinase is crucial for human adult erythropoiesis. Haematologica. 2019 05; 104(5):907-918. View Abstract
  15. Dyserythropoiesis evaluated by the RED score and hepcidin:ferritin ratio predicts response to erythropoietin in lower-risk myelodysplastic syndromes. Haematologica. 2019 03; 104(3):497-504. View Abstract
  16. Mutation in human CLPX elevates levels of d-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria. Proc Natl Acad Sci U S A. 2017 09 19; 114(38):E8045-E8052. View Abstract
  17. Comprehensive Proteomic Analysis of Human Erythropoiesis. Cell Rep. 2016 08 02; 16(5):1470-1484. View Abstract
  18. Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release. Biochemistry. 2015 Sep 15; 54(36):5617-31. View Abstract
  19. Antisense oligonucleotide-based therapy in human erythropoietic protoporphyria. Am J Hum Genet. 2014 Apr 03; 94(4):611-7. View Abstract
  20. Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP). Hum Mol Genet. 2013 Apr 01; 22(7):1280-8. View Abstract
  21. Late-onset X-linked dominant protoporphyria: an etiology of photosensitivity in the elderly. J Invest Dermatol. 2013 Jun; 133(6):1688-90. View Abstract
  22. ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria. Blood. 2011 Aug 11; 118(6):1443-51. View Abstract
  23. Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations. Hum Mutat. 2011 Jun; 32(6):590-7. View Abstract
  24. [Inheritance in erythropoietic protoporphyria]. Pathol Biol (Paris). 2010 Oct; 58(5):372-80. View Abstract
  25. Excessive erythrocyte PPIX influences the hematologic status and iron metabolism in patients with dominant erythropoietic protoporphyria. Cell Mol Biol (Noisy-le-grand). 2009 Feb 16; 55(1):45-52. View Abstract
  26. C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. Am J Hum Genet. 2008 Sep; 83(3):408-14. View Abstract
  27. Similarity of the 5' and 3'-TAR secondary structures in HIV-1. Biochem Biophys Res Commun. 1993 Sep 15; 195(2):565-73. View Abstract
  28. [Computer-assisted diet therapy in pediatric kidney diseases]. Pediatrie. 1989; 44(3):197-202. View Abstract

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