First Domino Falls in Touch Research

Clinical Trials:
Trials Open at HMS to Test HIV Vaccine
Circadian Rhythms May Distinguish Alzheimer's Disease
Kirschner Wins Gairdner International Award

Genetically Transferred Angiogenesis Inhibitors Being Put to the Test

New Protein May Link Functions of Breast Cancer Molecule

Identity of Calcium-release Channel Unveiled

Proceedings of the HMS Faculty Council

Black Surgeons' Group Meets at HMS, Probes Residency Training Issues

Urban Institute Head to Speak at Inaugural Seidman Health Policy Lecture

Free Oral Cancer Screening Dates Set

Osher Foundation Gives $10 Million to HMS Division for Complementary Medical Therapies

HMS Tops Medical Schools in U.S. News Rankings

Medical Dean Martin Made Honorary Professor at Chinese Medical School

Alpert Winners to Discuss Their Research at Scientific Symposium

On Dissection and Healing

Call for Writers

Student Research Gets Limelight at Soma Weiss Day

Letter to the Editor

Front Page


Kirschner Wins Gairdner International Award

The Gairdner Foundation of Toronto has named Marc Kirschner, the Carl W. Walter professor and head of the HMS Department of Cell Biology, as one of four recipients of the 2001 Gairdner International Awards. Established by Toronto businessman James Gairdner in 1957 and carrying a $30,000 cash prize, they are among the most prestigious international awards in medical research. Of the past 251 recipients, 54 have gone on to win a Nobel Prize. The award recognizes outstanding contributions by medical scientists whose work will significantly improve the quality of life.

Marc Kirschner
Photo by Stu Rosner

This year's other winners are Clay Armstrong of the University of Pennsylvania, Bertil Hille of the University of Washington, and Roderick Mac-Kinnon of Rockefeller University and a Howard Hughes investigator. They share an award for elucidating the mechanism of action and molecular structure of ion channels.

Kirschner, who also directs the Armenise–Harvard Center for Integrative Biology and Physiology, was chosen for his pioneering work in the understanding of the structure, function, and dynamics of microtubules.

"The Gairdner International award represents a great and richly deserved honor for Marc Kirschner," said HMS dean Joseph Martin. "Dr. Kirschner has made important contributions in several distinct areas of cell biology. As the founding chair of our Department of Cell Biology, he has played a key role in ensuring Harvard Medical School's continued excellence and leadership in research and bringing us into the modern era of molecular biology."

In the 1970s, Kirschner began investigating the mechanism of microtubule assembly using biophysical means. He and his colleagues identified in 1975 the novel protein tau, which was later shown by others to be the major component of neurofibrillary tangles in Alzheimer's disease. In 1984, Kirschner and his group showed that microtubules polymerize by a completely novel process, which they called "dynamic instability." The process has a significant impact on the morphogenesis of cells and, in particular, that of the mitotic spindle. Using biotin-labeled tubulin in 1986, Kirschner and his group demonstrated dynamic instability of microtubules in the mammalian spindle, provided evidence that tubulin subunits were added at the kinetochore of chromosomes during mitosis, and showed that there was a steady flux of tubulin subunits to the pole. These discoveries form the basis of much current work on spindle morphogenesis.

The Kirschner group was the first to study interactions of microtubules with kinetochores in purified systems in vitro, establishing in 1985 certain activities of microtubule interaction with chromosomes. In 1988, the Kirschner laboratory showed that depolymerization alone could do work and move chromosomes, a result that verified earlier theoretical studies. And many earlier discoveries have been followed up by former Kirschner trainees. Kirschner's recent work has focused on the role of microtubules in axonogenesis and the biochemical regulation of actin assembly.