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

doi:10.1080/03630269.2020.1776322

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

Laboratory Medicine and Pathology

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	174-178
Number of pages	5
Journal	Hemoglobin
Volume	44
Issue number	3
DOIs	https://doi.org/10.1080/03630269.2020.1776322
State	Published - May 3 2020

Keywords

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

ASJC Scopus subject areas

Genetics(clinical)
Biochemistry, medical
Hematology
Clinical Biochemistry

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10.1080/03630269.2020.1776322

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

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).",

keywords = "Hb Bronovo, microcytic anemia, thalassemia, α hemoglobin (Hb) stabilizing protein (AHSP), α-Globin",

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

note = "Publisher Copyright: {\textcopyright} 2020 Informa UK Limited, trading as Taylor & Francis Group.",

year = "2020",

month = may,

day = "3",

doi = "10.1080/03630269.2020.1776322",

language = "English (US)",

volume = "44",

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T1 - Further Characterization of Hb Bronovo [α103(G10)His→Leu; HBA2

T2 - c.311A>T] and First Report of the Homozygous State

AU - Mehta, Nikita

AU - Johnston, J. Martin

AU - Hein, Molly

AU - Kipp, Benjamin R.

AU - Coon, Lea

AU - Savedra, Michelle E.

AU - Hoyer, James D.

AU - He, Rong

AU - Rangan, Aruna

AU - Shi, Min

AU - Oliveira, Jennifer L.

PY - 2020/5/3

Y1 - 2020/5/3

N2 - 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).

AB - 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).

KW - Hb Bronovo

KW - microcytic anemia

KW - thalassemia

KW - α hemoglobin (Hb) stabilizing protein (AHSP)

KW - α-Globin

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DO - 10.1080/03630269.2020.1776322

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JO - Hemoglobin

JF - Hemoglobin

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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