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@ARTICLE{Bechet:119629,
author = {D. Bechet and G. G. H. Gielen and A. Korshunov$^*$ and S.
Pfister$^*$ and C. Rousso and D. Faury and P.-O. Fiset and
N. Benlimane and P. W. Lewis and C. Lu and C. David Allis
and M. W. Kieran and K. L. Ligon and T. Pietsch and B.
Ellezam and S. Albrecht and N. Jabado},
title = {{S}pecific detection of methionine 27 mutation in histone 3
variants ({H}3{K}27{M}) in fixed tissue from high-grade
astrocytomas.},
journal = {Acta neuropathologica},
volume = {128},
number = {5},
issn = {1432-0533},
address = {Berlin},
publisher = {Springer},
reportid = {DKFZ-2017-00260},
pages = {733 - 741},
year = {2014},
abstract = {Studies in pediatric high-grade astrocytomas (HGA) by our
group and others have uncovered recurrent somatic mutations
affecting highly conserved residues in histone 3 (H3)
variants. One of these mutations leads to analogous
p.Lys27Met (K27M) mutations in both H3.3 and H3.1 variants,
is associated with rapid fatal outcome, and occurs
specifically in HGA of the midline in children and young
adults. This includes diffuse intrinsic pontine gliomas
$(80 \%)$ and thalamic or spinal HGA $(>90 \%),$ which are
surgically challenging locations with often limited tumor
material available and critical need for specific
histopathological markers. Here, we analyzed formalin-fixed
paraffin-embedded tissues from 143 pediatric HGA and 297
other primary brain tumors or normal brain.
Immunohistochemical staining for H3K27M was compared to
tumor genotype, and also compared to H3 tri-methylated
lysine 27 (H3K27me3) staining, previously shown to be
drastically decreased in samples carrying this mutation.
There was a $100 \%$ concordance between genotype and
immunohistochemical analysis of H3K27M in tumor samples.
Mutant H3K27M was expressed in the majority of tumor cells,
indicating limited intra-tumor heterogeneity for this
specific mutation within the limits of our dataset. Both
H3.1 and H3.3K27M mutants were recognized by this antibody
while non-neoplastic elements, such as endothelial and
vascular smooth muscle cells or lymphocytes, did not stain.
H3K27me3 immunoreactivity was largely mutually exclusive
with H3K27M positivity. These results demonstrate that
mutant H3K27M can be specifically identified with high
specificity and sensitivity using an H3K27M antibody and
immunohistochemistry. Use of this antibody in the clinical
setting will prove very useful for diagnosis, especially in
the context of small biopsies in challenging midline tumors
and will help orient care in the context of the extremely
poor prognosis associated with this mutation.},
keywords = {Histones (NLM Chemicals) / Methionine (NLM Chemicals)},
cin = {G380 / B062},
ddc = {610},
cid = {I:(DE-He78)G380-20160331 / I:(DE-He78)B062-20160331},
pnm = {317 - Translational cancer research (POF3-317)},
pid = {G:(DE-HGF)POF3-317},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:25200321},
pmc = {pmc:PMC4201745},
doi = {10.1007/s00401-014-1337-4},
url = {https://inrepo02.dkfz.de/record/119629},
}