A study has suggested that new “Nanobody” agents can help physicians identify patients most likely to benefit from breast cancer drug therapies.
If the compound, called “Nanobody”, proves effective in clinical trials, it would represent a significant advance for breast cancer drug therapy because some drugs are effective only in some people.
In addition, some drugs have side effects that may cause damage to vital organs, making it more crucial for physicians to get the right treatment to the right patient the first time around.
“What makes Nanobodies so promising is that they are robust, small enough for rapid elimination from the body, and easy to produce at a relatively low cost,” Ilse Vaneycken, M.Sc., a researcher involved in the work, said.
Breast cancer
To make this discovery, Vaneycken and her colleagues started with the target of the therapeutic drugs (HER2) and immunized a dromedary camel to raise special antibodies unique to this species.
Next, all unnecessary parts of the camel’s antibodies were removed and cloned in bacteria.
Of 100 million bacterial clones, the team selected those that produced the 40 Nanobodies that recognized or bound to the same site targeted by therapeutic drugs.
Of this group, the team screened for compounds that picked out breast cancer cells bearing the genetic tag HER2. Their lead compound did just that, and without blocking access to cancer-killing drugs now in use.
Other properties of Nanobodies, such as good expression, stability, and visibility enabled breast cancer tumours to be stained and seen rapidly were also exploited.
“The scientists went over the hump to get to the lump so to speak,” Gerald Weissmann, M.D., the Editor-in-Chief, said.
“This technique not only promises to help doctors target cancer cells with effective drugs today, but to pick out other discrete cancer targets in the future,” he added.
The new discovery has been published online in The FASEB Journal.
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Scientists have found that an enzyme essential for DNA replication and repair in humans works in a way that might be exploited as an anti-cancer therapy.
Researchers at The Scripps Research Institute and Lawrence Berkeley National Laboratory focused on a member of a group of enzymes called flap endonucleases, which are essential to the life of a cell.
The findings showed new, clearly defined crystal structures of the enzyme FEN1 in action-demonstrating it functions in a way opposite to accepted dogma.
“The research produced very accurate structures showing DNA before and after being cut by FEN1 activity, providing a basis for understanding a whole superfamily of enzymes that must cut specific DNA structures in order for DNA to be replicated and repaired,” said team leader John Tainer.
This superfamily includes important targets for the development of new cancer interventions, Tainer added.
Many cancers show high levels of FEN1 expression, which in some cases is correlated to tumor aggression. For these cases, FEN1-specific inhibitors may have chemotherapeutic potential.
To determine what FEN1 looked like in action, co-author Andy Arvai led the difficult but ultimately successful effort to grow crystals of the human FEN1 protein bound to DNA.
The end result was a highly detailed and accurate model showing the structures of DNA before and after being cut by FEN1.
Researchers know that mutations in FEN1 can predispose humans to cancer growth because errors in flap removal can create unstable DNA that promotes cell growth and division.
And studies in mice have shown that when one of two inherited FEN1 genes are knocked out, the mice are predisposed to cancer development if their DNA is damaged.
The study has been published in the April 15, 2011 issue of the journal Cell.