IN THIS ISSUE .
. .
November 21, 2007
- Revealing How Cancer Spreads
- Fur Finding Could Shed New Insights on Health
- Click Chemistry Comes to Life
- Scientists Unveil Structure of Molecular Target of Many Drugs
- Tackling Resistance to Cancer Drugs
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Revealing How Cancer Spreads
Courtesy of pathologist Richard Klemke of the University of California, San Diego.
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Zebrafish are showing scientists how cancer spreads to other parts of the body. By injecting the tiny, transparent fish with human breast cancer cells, researchers can watch blood vessels (green) grow toward a tumor (red)—a key step in cancer metastasis. The technique has helped them identify two proteins needed for cancer cells to invade the bloodstream and may aid the search for medicines that slow or stop the spread of the disease.
This work also was supported by NIH’s National Cancer Institute.
Full story
Klemke lab home page
Article abstract (from the October 30, 2007, issue of PNAS)
Fur Finding Could Shed New Insights on Health
Swabbing dogs’ inner cheeks for DNA helped researchers identify a coat color gene. Courtesy of Chris Kaelin.
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After swabbing DNA from dogs’ inner cheeks, geneticist Greg Barsh of the Stanford University School of Medicine identified the gene responsible for canine coat color. Variations in the gene produce coats of yellow, black, or shades in between. But the gene may play a bigger role in health: It makes a protein involved in a pathway that determines skin and hair color and regulates weight and response to stress. The coat color gene belongs to a family of genes thought to be involved mainly in the immune system, and its various functions raise new questions about what the gene family actually does.
This work also was supported by NIH’s National Institute of Diabetes and Digestive and Kidney Diseases.
Full story
Barsh home page
Article abstract (from the October 18, 2007, online issue of Science)
Click Chemistry Comes to Life
Looking inside living cells and watching their working parts can unlock secrets of human biology. But researchers have been able to do this only for a limited number of biological parts—mostly proteins. Now, chemist Carolyn Bertozzi of the Lawrence Berkeley National Laboratory has found a way to view other molecules that also play vital roles in cell health. She tweaked a well-known method called “click” chemistry, which snaps together molecules in a test tube, by attaching non-toxic chemical tags to sugars and fats. The tags let her not just see the molecules and, more importantly, study their movement in real time.
Full
story
Bertozzi lab home page
Article abstract (from the October 23, 2007, issue of PNAS)
Scientists Unveil Structure of Molecular Target of Many Drugs
Crystal structure of the beta2-adrenergic receptor protein. Courtesy of the Stevens laboratory.
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More than 40 years after beta blockers were first used clinically, scientists finally have a detailed, three-dimensional look at the drugs’ molecular target—the beta2-adrenergic receptor. This receptor hails from a family of proteins called G protein-coupled receptors (GPCRs) that control critical bodily functions and the action of about half of today’s pharmaceuticals. Brian Kobilka of Stanford University and Ray Stevens of The Scripps Research Institute used innovative techniques in protein engineering and structure determination to generate the first known structure of a human GPCR. The work could speed drug discovery and broaden our understanding of human health and disease.
This work also was supported by NIH’s Roadmap for Medical Research and National Institute of Neurological Disorders and Stroke.
Full
story
Kobilka lab home page
Stevens lab home page
Article abstracts 1, 2, 3 (from the October 25, 2007, online issue of Science and the November 15, 2007, issue of Nature)
Tackling Resistance to Cancer Drugs
Dictyostelium discoideum, a commonly used model organism in biomedical research. Courtesy of Stephen Alexander.
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When tumors become resistant to the drugs designed to defeat them, cancer patients have fewer treatment options. A team of researchers, including University of Missouri-Columbia biologist Stephen Alexander, set out to understand how tumors become insensitive to the commonly used anticancer drug cisplatin. They turned to Dictyosteleum discoideum, a soil-living amoeba that shares many genes with us. They found that cisplatin alters the activity of roughly 400 genes and that mutations in some of them lead to drug resistance. Targeting pathways governed by the resistance genes may help scientists boost cisplatin’s effectiveness and improve treatment outcomes.
This work also was supported by NIH’s National Institute of Child Health and Human Development and National Cancer Institute.
Full story
Alexander lab home page
Article abstract (from the September 25, 2007, issue of PNAS)