TY - JOUR
T1 - A recurring mutation in the respiratory complex 1 protein NDUFB11 is responsible for a novel form of X-linked sideroblastic anemia
AU - Lichtenstein, Daniel A.
AU - Crispin, Andrew W.
AU - Sendamarai, Anoop K.
AU - Campagna, Dean R.
AU - Schmitz-Abe, Klaus
AU - Sousa, Cristovao M.
AU - Kafina, Martin D.
AU - Schmidt, Paul J.
AU - Niemeyer, Charlotte M.
AU - Porter, John
AU - May, Alison
AU - Patnaik, Mrinal M.
AU - Heeney, Matthew M.
AU - Kimmelman, Alec
AU - Bottomley, Sylvia S.
AU - Paw, Barry H.
AU - Markianos, Kyriacos
AU - Fleming, Mark D.
N1 - Funding Information:
This work was supported by National Institutes of Health National Institute of Diabetes and Digestive and Kidney Diseases DK087992 (M.D.F.) and R01 DK070838 and National Heart, Lung, and Blood Institute P01 HL03226 2 (B.H.P.).
Publisher Copyright:
© 2016 by The American Society of Hematology.
PY - 2016/10/13
Y1 - 2016/10/13
N2 - The congenital sideroblastic anemias (CSAs) are a heterogeneous group of inherited blood disorders characterized by pathological mitochondrial iron deposition in erythroid precursors. Each known cause has been attributed to a mutation in a protein associated with heme biosynthesis, iron-sulfur cluster biogenesis, mitochondrial translation, or a component of the mitochondrial respiratory chain. Here, we describe a recurring mutation, c.276_278del, p.F93del, in NDUFB11, a mitochondrial respiratory complex I-associated protein encoded on the X chromosome, in 5 males with a variably syndromic, normocytic CSA. The p.F93del mutation results in respiratory insufficiency and loss of complex I stability and activity in patient-derived fibroblasts. Targeted introduction of this allele into K562 erythroleukemia cells results in a proliferation defect with minimal effect on erythroid differentiation potential, suggesting the mechanism of anemia in this disorder.
AB - The congenital sideroblastic anemias (CSAs) are a heterogeneous group of inherited blood disorders characterized by pathological mitochondrial iron deposition in erythroid precursors. Each known cause has been attributed to a mutation in a protein associated with heme biosynthesis, iron-sulfur cluster biogenesis, mitochondrial translation, or a component of the mitochondrial respiratory chain. Here, we describe a recurring mutation, c.276_278del, p.F93del, in NDUFB11, a mitochondrial respiratory complex I-associated protein encoded on the X chromosome, in 5 males with a variably syndromic, normocytic CSA. The p.F93del mutation results in respiratory insufficiency and loss of complex I stability and activity in patient-derived fibroblasts. Targeted introduction of this allele into K562 erythroleukemia cells results in a proliferation defect with minimal effect on erythroid differentiation potential, suggesting the mechanism of anemia in this disorder.
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U2 - 10.1182/blood-2016-05-719062
DO - 10.1182/blood-2016-05-719062
M3 - Article
C2 - 27488349
AN - SCOPUS:84991582039
SN - 0006-4971
VL - 128
SP - 913
EP - 917
JO - Blood
JF - Blood
IS - 15
ER -