Further Characterization of Hb Bronovo [α103(G10)His→Leu; HBA2: c.311A>T] and First Report of the Homozygous State

Nikita Mehta, J. Martin Johnston, Molly Hein, Benjamin R. Kipp, Lea Coon, Michelle E. Savedra, James D. Hoyer, Rong He, Aruna Rangan, Min Shi, Jennifer L. Oliveira

Research output: Contribution to journalArticle

Abstract

Hb Bronovo [α103(G10)His→Leu, HBA2: c.311A>T] is an α-globin variant that interferes with and decreases binding efficiency to α hemoglobin (Hb) stabilizing protein (AHSP), a chaperone molecule. The histidine residue at position 103 is integral to the AHSP hydrogen bond formation where disruption results in an increased quantity of cytotoxic free α-globin chains, thereby creating a similar pathophysiology as β-thalassemia (β-thal). We report a family with Hb Bronovo, including a homozygous proband, which resulted from maternal uniparental disomy (UPD). Although not detected by routine studies in previous reports, the variant protein is visible by intact mass spectrometry (MS).

Original languageEnglish (US)
Pages (from-to)174-178
Number of pages5
JournalHemoglobin
Volume44
Issue number3
DOIs
StatePublished - May 3 2020

Keywords

  • Hb Bronovo
  • microcytic anemia
  • thalassemia
  • α hemoglobin (Hb) stabilizing protein (AHSP)
  • α-Globin

ASJC Scopus subject areas

  • Hematology
  • Clinical Biochemistry
  • Genetics(clinical)
  • Biochemistry, medical

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