Breast and Prostate Cancer Diagnosis

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Thanks to a diagnostic imaging technique that should soon find its way to medical establishments, many patients will be spared the pain and risk of biopsies. The technique, which detects breast and prostate cancer, has recently received FDA clearance. Slated for use as early as next year, it will enable doctors to distinguish between malignant tumors and benign lumps by scanning instead of cutting.

 

 
Called 3TP (Three Time Point), the technique makes use of existing MRI machinery and a dye-like material (called a "contrast agent") that is injected near the examination site. The site is scanned by MRI three times over a period of several minutes, once before the contrast agent is injected and twice after. The software developed for the method then creates a colored image of the breast or prostate area. A preponderance of red in the image indicates malignancy, while mainly blue and green are signs of a benign growth.
 
The procedure was developed by Prof. Hadassa Degani of the Institute's Biological Regulation Department. Because 3TP is non-invasive and is based on existing MRI technology that has long been approved, the FDA clearing process was shorter than usual. Clearance is now being sought in Canada and Europe.
 
Prof. Degani's research was supported by the M.D. Moross Institute for Cancer Research; Sir David Alliance, CBE, UK; Mr. and Mrs. Lon Morton, Calabasas, CA; Mrs. Jackie Gee, Ms. Livia Meyer and Mr. Harry Woolf, UK; Ms. Lynne Mochon and Ms. Edith Degani, NY, USA; the Washington Square Health Foundation; the Willner Family Center for Vascular Biology; and the Estate of Mrs. Ilse Katz, Switzerland. She is the incumbent of the Fred and Andrea Fallek Professorial Chair in Breast Cancer Research.
Life Sciences
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A Matter of Taste

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De gustibus non est disputandum, as the saying goes, emphasizes the futility of arguing over personal taste. An Institute team headed by Prof. Doron Lancet of the Molecular Genetics Department has found why this is true. In our genome, around 1,000 genes code for the nose's odor-detecting receptors (responsible for our sense of smell and a great part of flavor perception). Of these, more than half have become totally inactive in humans, a fact that has been known for years. In a surprising discovery, published in Nature Genetics, the team showed that at least 50 genes are "optional"-  they can be active in some individuals and inactive in others. This high level of genetic variation accounts for the differences in our sense of taste and smell. The study also shows that the obliteration level of odor-detecting receptors varies among different ethnic groups. The findings could lead to fundamental changes in the cosmetics and foodstuff industries, which might be able to tailor their products to the tastes of their customers.

 

Prof. Lancet's research was supported by the Jean-Jacques Brunschwig Fund for the Molecular Genetics of Cancer; the Crown Human Genome Center; the Avraham and Judy Goldwasser Fund; the Philip M. Klutznick Research Fund; and the Alfried Krupp von Bohlen und Halbach Foundation. He is the incumbent of the Ralph and Lois Silver Professorial Chair in Human Genomics.

Life Sciences
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DNA Fuels Tiny Computing Machine

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Shapiro, Livneh, Paz-Elizur, Benenson and Adar. World's smallest computer

 
Fifty years after the discovery of the structure of DNA, a Weizmann team has found a new use for this celebrated molecule – as fuel for molecular computation systems. They have developed a device – an improvement upon a molecular computing device reported by the team around a year ago –  in which a single DNA molecule provides the computer with input data as well as all the necessary fuel. A spoonful (5 milliliters) of  solution can contain 15,000 trillion such computers. The new device was awarded the Guinness World Record for “smallest biological computing device.”
 
The study was carried out by Prof. Ehud Shapiro, Prof. Zvi Livneh, Yaakov Benenson, Dr. Rivka Adar and Dr. Tamar Paz-Elizur of the Institute’s Biological Chemistry Department and the Computer Science and Applied Mathematics Department. 
 
Prof. Ehud Shapiro’s research is supported by the Samuel R. Dweck Foundation; the Dolfi and Lola Ebner Center for Biomedical Research; the Benjamin and Seema Pulier Charitable Foundation; the Robert Rees Fund for Applied Research; and Yad Hanadiv.
 
Prof. Zvi Livneh is the incumbent of the Maxwell Ellis Professorial Chair in Biomedical Research. His research is supported by the Dolfi and Lola Ebner Center for Biomedical Research; the Levine Institute of Applied Science; the Dr. Josef Cohn Minerva Center for Biomembrane Research; and the M.D. Moross Institute for Cancer Research.
Clockwise: Prof. Ehud Shapiro, Prof. Zvi Livneh, Dr. Tamar Paz-Elizur, Ph. D. student Yaakov Benenson and Dr. Rivka Adar. Guinness World Record
Math & Computer Science
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Newly Uncovered Genes

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Melanoma, Colon Cancer

 
Scientists at the Weizmann Institute have identified a gene involved in the progression of human melanoma and colon cancer. The new marker for these killer diseases has important implications because it could eventually lead to the screening of large populations and early diagnosis. The gene, called Nr-CAM, was found by by the team of Prof. Avri Ben-Ze’ev of the Molecular Cell Biology Department. It is highly expressed in human melanoma cells and colon cancer tissue. Further research will be done to learn more about the gene’s role in the development of these cancers.
 
Prof. Avri Ben-Ze’ev is the incumbent of the Samuel Lunenfeld-Reuben Kunin Chair of Genetics. His research is supported by the M.D. Moross Institute for Cancer Research; the Yad Abraham Center for Cancer Diagnostics and Therapy; and the late Maria Zondek.
 

Anemia (Type CDA-1)

 
A combined effort by scientists at the Schneider Children’s Medical Center and the Weizmann Institute of Science has led to the discovery of a gene responsible for congenital dyserythropoietic anemia-1 (CDA-1), found mainly in Bedouin families.
 
The findings could lead to effective detection and eventually to treatment of the disease. In addition, understanding the role of this gene’s protein product could provide important clues to other types of anemia as well as to the general mechanisms of blood cell formation. Leading the Weizmann team was Prof. Doron Lancet of the Molecular Genetics Department. Prof. Hannah Tamary headed the Schneider team.
 
Prof. Doron Lancet is the incumbent of the Ralph and Lois Silver Professorial Chair in Human Genomics. His research is supported by the Jean-Jacques Brunschwig Fund for the Molecular Genetics of Cancer; the Crown Human Genome Center; the Avraham and Judy Goldwasser Fund; and the Alfried Krupp von Bohlen und Halbach Foundation.
Life Sciences
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X-Rays Yield Mechanism of Alzheimer’s Drug

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Profs. Israel Silman and Joel Sussman. Drug snapshots

 

A team of Weizmann scientists has gained new insight into a recently approved Alzheimer’s drug called rivastigmine (currently sold as Exelon (TM)), revealing its molecular mechanism.
“The results were surprising,” says Prof. Joel Sussman of the Structural Biology Department. “They show that we can safely treat Alzheimer’s disease with much lower quantities of rivastigmine, thus minimizing adverse effects.”
 
Rivastigmine, like other Alzheimer’s drugs, works by blocking the action of an enzyme involved in Alzheimer’s disease called acetylcholinesterase (AChE). The scientists – Sussman, Prof. Israel Silman of the Neurobiology Department and Ph.D. student Pazit Bar-On – took complex “snapshots” of rivastigmine bound to AChE.
 
They then built a molecular map showing the spatial arrangement of all the atoms of AChE and rivastigmine. Using this map, they found that after binding to AChE the rivastigmine molecule breaks in two and moves some of AChE’s atoms, making it difficult for AChE to return to an active state. It thus prolongs the drug’s effect.
 
Prof. Israel Silman is the incumbent of the Bernstein-Mason Professorial Chair of Neurochemistry. His research is supported by the Nella and Leon Benoziyo Center for Neurosciences; the Charles A. Dana Foundation; the Carl and Micaela Einhorn-Dominic Brain Research Institute; and the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly.
 
Prof. Joel Sussman is the incumbent of the Morton and Gladys Pickman Chair in Structural Biology. His research is supported by the Charles A. Dana Foundation; the Jean and Jula Goldwurm Memorial Foundation; the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly; the Joseph and Ceil Mazer Center for Structural Biology; and the late Sally Schnitzer.
 
Life Sciences
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First Glimpses of Folding Proteins

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Proteins, it appears, have taken Frank Sinatra’s “I Did It My Way” to heart. A new study published in the Proceedings of the National Academy of Sciences (PNAS) reveals how single proteins, each a few nanometers (billionths of a meter) long, fold to assume their final shape. It shows that even proteins that end up with the same final shape take different routes to reach it.
 
Using a novel technology developed in their lab, Weizmann scientists headed by Dr. Gilad Haran of the Chemical Physics Department took the first glimpses ever of single proteins in the process of folding. Proteins, the fundamental components of all living cells, start out as randomly shaped chains and twist into a well-defined structure that determines their function. In some cases this process goes awry and can result in a wide variety of disorders.
 
For decades scientists have pondered how proteins go through this folding process, yet they were unable to follow individual folding proteins for more than a few milliseconds – the proteins were just too small and constantly on the go. Haran’s technology, which makes following single proteins possible, has provided an answer to a central question, showing that they differ in the routes taken to the same folded shape. The new technology might help clarify the reasons for protein misfolding and ensuing disease.
 
Dr. Gilad Haran is the incumbent of the  Benjamin H. Swig and Jack D. Weiler Career Development Chair. His research is supported by the Clore Center for Biological Physics; the Fritz Haber Center for Physical Chemistry; and the Avron-Wilstaetter Minerva Center for Research in Photosynthesis.
Space & Physics
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Protein Teamwork Do or Die

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Woody Allen once said, "It's not that I'm afraid to die. I just don't want to be there when it happens!"


Perhaps he was unaware of it, but if we're lucky, we all actually "die" a little every day. A growing body of scientific evidence is proving what philosophers and artists have preached for millennia -- that a healthful life is dependent on, driven forward, by death.

Cells contain built-in suicide mechanisms. Known as apoptosis, or programmed cell death, this process is vital to normal embryonic development and tissue maintenance. It is the body's means of ridding itself of damaged or surplus cells.

Apoptosis failure can be deadly. Cell mutation occurs regularly due to environmental factors such as ultraviolet radiation and chemical toxins, as well as natural cell processes. If left unchecked, the damaged cells continue to proliferate, often leading to life-threatening diseases, such as cancer.

Prof. Yosef Shaul of the Weizmann Institute's Molecular Genetics Department has deciphered part of the cellular events underlying this pivotal defense mechanism. Published in Nature, his findings provide important insights into cancer pathologies and their potential cures.

"The emergency pathway is designed to reverse or mitigate mutation-induced damage," explains Shaul. "It's an intricate check-and-balance system controlled by a tightly orchestrated team of genes and their respective proteins. Interacting within a rigid, cascading 'If, Then, Else' environment characteristic of computer programming, the proteins initially attempt to repair the DNA. But if unsuccessful, they command the cell to self-destruct. In the third and worst-case scenario, both DNA repair and apoptosis fail, and disease usually ensues.

Who are these protein players and, most importantly, how do they interact? This is what Shaul and colleagues, Prof. Moshe Oren and Drs. Reuven Agami and Giovanni Blandino, set out to understand.

They began with c-Abl -- a major regulator of cell growth that, when mutated, can act as an oncogene, a gene that causes cancer. For instance, more than 90 percent of patients with chronic myeloid leukemia have a unique abnormality known as the Philadelphia chromosome, characterized by c-Abl mutations. Shaul decided to examine why c-Abl breakdown results in cancer. Specifically, what is its role in safeguarding the cell?

The Weizmann Institute team found that irradiation-induced DNA damage activates c-Abl, which subsequently recruits p73, another key regulating protein. If earlier attempts at cell repair fail, the interplay between these proteins leads to cell death. "The likelihood of tumor formation increases significantly if the function of either protein is flawed," Shaul explains. "Likewise, most cancer therapies depend on this cell repair mechanism. The object of chemotherapy and radiation is to activate the protein teamwork that causes damaged, cancerous cells to self-destruct."

Being able to pin down the precise point of damage along the pathway leading to DNA repair, cell death, or tumor formation could enhance future cancer therapies. Understanding the origin of disease in each patient may prove vital to determining the most effective form of therapy, tailored to individual pathologies.
Life Sciences
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Fill It Up... With Hydrogen

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Hydrogen, the lightest and most prevalent element in the universe, may prove to be the car fuel of choice in the future.

Tests on experimental vehicles have already shown hydrogen to be an efficient and pollution-free fuel; now Institute researchers are working on reducing the prohibitive cost involved in its production. They are developing technology that will use solar energy to extract hydrogen from its most readily available source, water.

Water molecules, which contain two atoms of hydrogen and one of oxygen, break apart when heated to very high temperatures under low pressure. But until now the hydrogen could not be exploited because the elements quickly recombine once they cool down.

Now a method to keep the elements separate has been developed by Prof. Avraham Kogan, working at the Institute's Solar Research Facilities Unit. In collaboration with the Israel Ceramic and Silicate Institute, he designed a special ceramic membrane that withstands temperatures of more than 2,000°C and allows hydrogen atoms to pass through while leaving the larger oxygen atoms behind. Kogan says the method is feasible, but the membrane has to work at even higher temperatures for it to be economically viable.
Environment
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Cellular "Suicide Weapon" Discovered

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An enzyme that acts as the "weapon" with which cells "commit suicide" has been discovered by an Institute team led by Prof. David Wallach of the Membrane Research and Biophysics Department. The finding may lead to treatments for autoimmune disorders caused by abnormal cellular self-destruction, such as juvenile diabetes or multiple sclerosis.

"We've identified a crucial step in the self-annihilation of cells and may now be able to control this process," Wallach says.

All cells have a normal ability to "commit suicide" when they become redundant, but in certain diseases the immune system erroneously commands healthy cells to do so. In these disorders, a cell receives the suicide message through receptor molecules known as Fas/Apo-1 and through tumor necrosis factor receptors.

Wallach's team has now discovered the "weapon" that translates this message into action: an enzyme they call MACH. This enzyme cuts up vital proteins inside a cell, disrupting the cell's normal functions and killing it. The team has also found that the suicide message is transmitted with surprising directness. Unlike many other cellular processes that involve multiple stages, this one goes directly from the receptor to the enzyme.

The new understanding may make it possible to block the suicide mechanism when it causes disease.
Life Sciences
English

How the Mongoose Beats the Snake

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The mongoose, as anyone who has read Rudyard Kipling's Jungle Book knows, has but one purpose in life: "to fight and eat snakes." Now a team of Weizmann Institute researchers, led by Prof. Sara Fuchs of the Immunology Department, has revealed how this small mammal manages to survive the effects of deadly snake venom.

When a poisonous snake bites, venom attaches itself to a protein message receiver on the victim's muscle cells, blocking the normal flow of signals sent from the central nervous system to the cell, thus paralyzing and ultimately killing the victim.

The Institute team has found that in mongooses -- and in snakes themselves -- the structure of the receiver, the acetylcholine receptor, is slightly different from that in other animals. The difference is small -- only four out of several hundred amino acids that make up the receptor differ -- but it is enough to prevent venom from attaching itself to the cells. So mongooses like Kipling's Rikki-tikki-tavi, and snakes themselves, are protected from otherwise deadly snake attacks.

Fuchs has spent more than two decades studying the acetylcholine receptor, a protein that plays a key role in muscle function and is also involved in the autoimmune neuromuscular disorder myasthenia gravis. Part of the research was done in collaboration with Tel Aviv University's Zoology Department .
Space & Physics
English

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