Biological Fingerprint Identifies Leiomyomatosis and Renal Cell Cancer
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By LabMedica International staff writers Posted on 31 May 2011 |
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A diagnostic test involves screening tumor samples for a particular molecular fingerprint unique to leiomyomatosis and renal cell cancer (HLRCC).
A protein modification induced by FH deficiency (due to an over-abundance of fumarate) was identified by scientists at the Henry Wellcome Building for Molecular Physiology, University of Oxford (United Kingdom). This alteration is unique to HLRCC and can be used as a biomarker–a biological 'fingerprint' to identify tumors caused by this mechanism.
The disorder is caused by mutations, which may be inherited, in a gene responsible for the production of an enzyme known as fumarate hydratase (FH). This leads to an accumulation within cells of fumarate, which promotes the development of cancer cells.
Screening cases of papillary renal cell cancer using the new test allows scientists to identify undiagnosed cases of HLRCC for genetic testing. The team that developed the test believes that it should be applied to all cases of papillary renal cell cancer to identify those with FH mutations, allowing advice to be provided to their families on their own relative risks of developing the disorder and associated kidney cancer.
Hereditary leiomyomatosis and renal cell cancer (HLRCC) is a disorder which causes the development of benign but often painful tumors in the skin and, in females, in the uterus. Between one in six and one in ten people affected by the disorder will go on to develop an aggressive form of kidney cancer called papillary renal cell cancer. The condition often strikes people in their twenties.
Dr. Lesley Walker, director of cancer information at Cancer Research UK (London, United Kingdom), said: "Tests like this can also help us to identify other patients with the same mutation, paving the way for the development of targeted treatments for specific groups of patients. This approach is called stratified medicine and many scientists now believe it could revolutionize cancer treatment in the future."
Related Links:
Cancer Research UK
Henry Wellcome Building for Molecular Physiology, University of Oxford
A protein modification induced by FH deficiency (due to an over-abundance of fumarate) was identified by scientists at the Henry Wellcome Building for Molecular Physiology, University of Oxford (United Kingdom). This alteration is unique to HLRCC and can be used as a biomarker–a biological 'fingerprint' to identify tumors caused by this mechanism.
The disorder is caused by mutations, which may be inherited, in a gene responsible for the production of an enzyme known as fumarate hydratase (FH). This leads to an accumulation within cells of fumarate, which promotes the development of cancer cells.
Screening cases of papillary renal cell cancer using the new test allows scientists to identify undiagnosed cases of HLRCC for genetic testing. The team that developed the test believes that it should be applied to all cases of papillary renal cell cancer to identify those with FH mutations, allowing advice to be provided to their families on their own relative risks of developing the disorder and associated kidney cancer.
Hereditary leiomyomatosis and renal cell cancer (HLRCC) is a disorder which causes the development of benign but often painful tumors in the skin and, in females, in the uterus. Between one in six and one in ten people affected by the disorder will go on to develop an aggressive form of kidney cancer called papillary renal cell cancer. The condition often strikes people in their twenties.
Dr. Lesley Walker, director of cancer information at Cancer Research UK (London, United Kingdom), said: "Tests like this can also help us to identify other patients with the same mutation, paving the way for the development of targeted treatments for specific groups of patients. This approach is called stratified medicine and many scientists now believe it could revolutionize cancer treatment in the future."
Related Links:
Cancer Research UK
Henry Wellcome Building for Molecular Physiology, University of Oxford
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