Understanding the role of the protein H3.3 may lead to new treatment options.
A team at the University of Nottingham, led by Professor Richard Grundy, hope that studying the protein histone H3.3, which has been linked to the formation of DIPG, will lead to much-needed new treatments for for the tumour type.
DIPG tumours develop within the brainstem and so cannot be surgically removed. New drugs which specifically target the tumour cells without damaging the surrounding brain are urgently needed.
The researchers will be 'tagging' both mutant and normal histone H3.3 with a fluorescent marker to compare where the proteins are found within the brain during normal development and tumour growth. They will also investigate which genes are being controlled by mutant histone H3.3 and whether these genes are linked to tumour formation.
Histones are spherical proteins that help to package DNA within each cell. They also have a role in sending messages to the DNA to control which genes are switched on and off - mutations to histone H3.3 will lead to changes in gene activity which may cause a cell to become cancerous.
A greater understanding of histone H3.3 may enable researchers to develop new drugs which target the proteins, ensuring that these aberrant changes to gene activity do not occur.
Formal title: Molecular insights into histone H3.3 mutations in Diffuse Intrinsic Pontine Gliomas and Paediatric Glioblastoma
Key Researcher: Professor Richard Grundy, Professor of Paediatric Neuro-Oncolcogy University of Nottingham
Timing: Granted in 2012 for 3 years.
Tumour type: Diffuse Intrinsic Pontine Glioma (DIPG)
Research type: Tumour biology