Intrauterine Growth Retardation Related to Maternal Erythrocyte Oxygen Transport

Mendoza, Glenn J.; Calem-Grunat, Jaclyn; Karmel, Bernard Z.; LeBlanc, Michael H.; Brown, Edwin G.; Chervenak, Frank A.; Krouskop, Richard W.; Winslow, Robert M.

doi:10.1007/978-1-4684-5643-1_42

Cited by 3 publications

(2 citation statements)

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“…Seven women whose blood P 50 of 27.3 ± 0.4 mm Hg was at the lower bound of the normal range had smaller babies than women with P 50 of 28.5 ± 0.3 torr 16 . Among 21 normal women with third‐trimester fetal growth retardation, hemoglobin‐O 2 affinity was linearly related to birth weight 17,18 …”

Section: Hemoglobin Variants P50 and Fetal Developmentmentioning

confidence: 97%

“…16 Among 21 normal women with third-trimester fetal growth retardation, hemoglobin-O 2 affinity was linearly related to birth weight. 17,18 Twenty-two women with 11%-100% HbF had 43 pregnancies with 33 live births. Four women, all with severe forms of β thalassemia and HbF of 70%-100%, had growth-restricted or small for gestational age fetuses; fetal growth was normal in 17 heterozygotes with different genotypes of β thalassemia who had HbF 11%-29%.…”

Section: Hemoglobin Variants P 5 0 and Fetal Developmentmentioning

confidence: 99%

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Fetal hemoglobin in β hemoglobinopathies: Is enough too much?

Steinberg

2022

American J Hematol

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Cell-based therapies inducing about 40% fetal hemoglobin (HbF), or a HbF-like hemoglobin in most erythrocytes, can-at least in the shortterm-effect a cure or near-cure of β hemoglobinopathies, which are humankind's most common Mendelian diseases. [1][2][3] In sickle cell disease, a point mutation in the normal β-globin gene (HBB) directs the synthesis of sickle hemoglobin (HbS), which polymerizes on deoxygenation, damaging the red cell and triggering a complex pathophysiology. HbF exerts a powerful anti-polymerization effect because the chances of both the HbF tetramer (α 2 γ 2 ) and the hybrid tetramer α 2 γβ S entering the polymer phase are nearly nil. 4 Hundreds of different HBB mutations cause β thalassemia where insufficient β-globin synthesis allows free unpaired α globin to accumulate, leading to ineffective erythropoiesis and severe anemia. γ-Globin pairs with α globin forming HbF and preventing, at its earliest stage, the pathophysiology of the β thalassemia phenotype.

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Section: Hemoglobin Variants P50 and Fetal Developmentmentioning

confidence: 97%