Demonstrate Potential of High-Throughput Screening in Academia
Boston, MA -- October 25, 1999 -- Nine months after the Harvard Medical School Institute for Chemistry and Cell Biology (ICCB) opened its doors, its researchers are reporting their first success. In the October 29 Science, they describe how they used a series of screens to fish out of a library of chemical compounds the first known small-molecule inhibitor to a motor protein involved in cell division.
The scientists describe a molecule that perturbs the normally bipolar mitotic spindle apparatus in such a way that cells arrest midway through mitosis with a characteristically malformed spindle that looks a bit like an exploding star.
Moreover, the scientists, led by Tim Mitchison and Stuart Schrieber, pinpointed the protein through which this chemical exerts its peculiar effect: it is a member of the kinesin family of motor proteins. That makes monastrol the first in a new class of mitosis inhibitors. All others -- ranging from colchicine, a medicine used since ancient Egyptian times, to modern cancer drugs including taxol -- affect microtubules, the long, thin protein tubes that are the main structural element of the mitotic spindle.
The paper demonstrates that it is feasible and efficient for academic scientists to perform high-throughput screening, most of which occurs in industrial research. "We are very pleased with this paper," says Mitchison, professor of cell biology. "For this to come out of an academic lab is unusual, if not unique, at this point."
The project was designed primarily to yield tools for basic research.
Indeed, the ICCB scientists are already using monastrol to study the molecular
dynamics of the mitotic spindle, a finely tuned structure that separates the two
sets of chromosomes during cell division. At the same time, any mitotic
inhibitor represents a potential starting point for developing better
Contact: Peta Gillyatt
Harvard Medical School