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Mutant fetal hemoglobin causing cyanosis in a newborn
J R Priest1, J Watterson, R T Jones
1Department of Pediatric Hematology/Oncology, Children's Hospital of St Paul, MN 55102.
Pediatrics
|May 1, 1989
Summary
A novel mutant gamma-globin chain caused abnormal fetal hemoglobin in cyanotic newborns. Symptoms resolved as beta-globin synthesis replaced gamma-globin, indicating a potential therapeutic window for hemoglobinopathies.
Area of Science:
- Hematology
- Molecular Biology
- Genetics
Background:
- Fetal hemoglobin (HbF) is crucial for oxygen transport in newborns.
- Mutations in globin chains can lead to dysfunctional hemoglobin and associated clinical conditions.
- Hemoglobin M (HbM) diseases are a group of rare inherited disorders characterized by cyanosis.
Observation:
- A cyanotic newborn presented with a functionally abnormal fetal hemoglobin.
- Genetic analysis revealed a single amino acid substitution in the gamma-globin chain.
- This mutation occurred at a site consistent with known adult Hemoglobin M variants.
Findings:
- The abnormal fetal hemoglobin led to cyanosis in the newborn.
- Clinical cyanosis resolved by 5 weeks of age, coinciding with the switch to beta-globin synthesis.
- A sibling exhibited similar cyanosis and the same mutant hemoglobin, confirming a genetic basis.
Implications:
- This case highlights a specific gamma-globin mutation affecting fetal hemoglobin function.
- The findings suggest that the transition from gamma- to beta-globin synthesis can compensate for certain globin chain abnormalities.
- Understanding such mutations is vital for diagnosing and potentially managing inherited hemoglobin disorders.