Now, there’s a new hope for those dealing withleukaemia. As per a new study, a
mechanism that improves functioning ofproteins impaired in patients with acute
forms of leukaemia has beenunveiled by researchers at the Memorial
Sloan-Kettering Cancer Center(MSKCC) in New York.
The protein, called AML1, plays a crucialrole in the development of the blood
system and in the production ofplatelets and immune cells.
Investigators identified themethyltransferase enzyme that controls the activity
of normal AML1protein - also called RUNX1. They demonstrated its ability to
regulatethe function of proteins that control cell fate by turning genes on
oroff.
The researchers found that cellular pathways that regulate activityof normal
AML1 protein through a process called arginine methylationcannot similarly
regulate the activity of AML1-ETO, a proteinassociated with causing acute
leukaemia.
Methylation is theprocess by which methyltransferases catalyze the attachment
of a methylgroup to DNA or protein in order to regulate gene expression or
proteinfunction. Demethylase enzymes that remove methyl groups from
proteinshave only recently been discovered.
By manipulating theactivity of these enzymes, it may be possible to promote the
activityof the normal protein, and thereby lessen the impact of the proteinthat
promotes leukaemia," said the study's co-author Stephen D. Nimer,of Hematology
Service at MSKCC.
There are currently no availabledrugs that target protein methylation, although
two drugs that targetDNA methylation are FDA approved for treating patients
withmyelodysplastic syndromes.
The findings are published in the March 1 issue of Genes and Development.
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