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Writer Panagene     (Date : 2016-07-13 10:03:48)
Subject [Scientific publications] [2015]IDH Mutation Analysis in Ewing Sarcoma Family Tumors.

J Pathol Transl Med. 2015 May;49(3):257-61. doi: 10.4132/jptm.2015.04.14. Epub 2015 May 15.

IDH Mutation Analysis in Ewing Sarcoma Family Tumors.

Na KY1Noh BJ2Sung JY3Kim YW3Santini Araujo E4Park YK3.

Author information



Isocitrate dehydrogenase (IDH) catalyzes the oxidative decarboxylation of isocitrate to yield α-ketoglutarate (α-KG) with production of reduced nicotinamide adenine dinucleotide (NADH). Dysfunctional IDH leads to reduced production of α-KG and NADH and increased production of 2-hydroxyglutarate, an oncometabolite. This results in increased oxidative damage and stabilization of hypoxia-inducible factor α, causing cells to be prone to tumorigenesis.


This study investigated IDH mutations in 61 Ewing sarcoma family tumors (ESFTs), using a pentose nucleic acid clamping method and direct sequencing.


We identified four cases of ESFTs harboring IDH mutations. The number of IDH1 and IDH2 mutations was equal and the subtype of IDH mutations was variable. Clinicopathologic analysis according to IDH mutation status did not reveal significant results.


This study is the first to report IDH mutations in ESFTs. The results indicate that ESFTs can harbor IDH mutations in previously known hot-spot regions, although their incidence is rare. Further validation with a larger case-based study would establish more reliable and significant data on prevalence rate and the biological significance of IDH mutations in ESFTs.


Isocitrate dehydrogenase; PNA clamping; Sarcoma, Ewing


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