Grape Seed Extract Eliminates Cancer Cell

Did You Know…

… grape seed oil can cure seemingly hopeless cases of cancer?

Discovering a chemotherapy treatment capable of selectively eliminating cancer cells would be a cancer researcher’s equivalent of finding the Holy Grail.  Continue reading

Learning Faster with Neurodegenerative Disease

Huntington’s gene mutation carriers: Severity of the genetic mutation related to learning efficiency

People who bear the genetic mutation for Huntington’s disease learn faster than healthy people. The more pronounced the mutation was, the more quickly they learned. This is reported by researchers from the Ruhr-Universität Bochum and from Dortmund in the journal Current Biology. Continue reading

Cell Phone Alert: Fertility Issues Discovered

Unfortunately, cell phones do emit electromagnetic radiation. There has been much debate recently in health news circles about the effects of this radiation on human health.

The problem with radiation is that it is made up of subatomic particles. These particles move at a very high speeds, sometimes as much as 100,000 miles per second! Because of these tremendous speeds, radiation can penetrate deep inside your body, damaging your cells.

When a radiation particle collides violently with atoms or molecules in your cells, these cells may die. If the cells survive the impact, they may begin to grow in a mutated form.

And in fact, this is just what a recent study has found when it comes to sperm cells. Researchers conducted an animal trial involving rats exposed to cell phone radiation. Continue reading

Specialized Regulatory T Cell Stifles Antibody Production Centers

Discovery has potential implications for cancer, autoimmune disease

A regulatory T cell that expresses three specific genes shuts down the mass production of antibodies launched by the immune system to attack invaders, a team led by scientists at The University of Texas MD Anderson Cancer Center reported online in the journal Nature Medicine.

“Regulatory T cells prevent unwanted or exaggerated immune system responses, but the mechanism by which they accomplish this has been unclear,” said paper senior author Chen Dong, Ph.D., professor in MD Anderson’s Department of Immunology and director of the Center for Inflammation and Cancer.

“We’ve identified a molecular pathway that creates a specialized regulatory T cell, which suppresses the reaction of structures called germinal centers. This is where immune system T cells and B cells interact to swiftly produce large quantities of antibodies,” Dong said. Continue reading

How Disordered Proteins Spread From Cell To Cell, Potentially Spreading Disease

One bad apple is all it takes to spoil the barrel. And one misfolded protein may be all that’s necessary to corrupt other proteins, forming large aggregations linked to several incurable neurodegenerative diseases such as Huntington’s, Parkinson’s and Alzheimer’s.

Stanford biology Professor Ron Kopito has shown that the mutant, misfolded protein responsible for Huntington’s disease can move from cell to cell, recruiting normal proteins and forming aggregations in each cell it visits.

Knowing that this protein spends part of its time outside cells “opens up the possibility for therapeutics,” he said. Kopito studies how such misfolded proteins get across a cell’s membrane and into its cytoplasm, where they can interact with normal proteins. He is also investigating how these proteins move between neuronal cells.

The ability of these proteins to move from one cell to another could explain the way Huntington’s disease spreads through the brain after starting in a specific region. Similar mechanisms may be involved in the progress of Parkinson’s and Alzheimer’s through the brain.

Kopito discussed his research at the annual meeting of the American Association for the Advancement of Science in Washington, D.C.

Not all bad

Not all misfolded proteins are bad. The dogma used to be that all our proteins formed neat, well-folded structures, packed together in complexes with a large number of other proteins, Kopito said. But over the past 20 years, researchers have found that as much as 30 percent of our proteins never fold into stable structures. And even ordered proteins appear to have some disordered parts.

Disordered proteins are important for normal cellular functions. Unlike regular proteins, they only interact with one partner at a time. But they are much more dynamic, capable of several quick interactions with many different proteins. This makes them ideal for a lot of the standard communication that happens within a cell for its normal functioning, Kopito said.

But if some of our proteins are always disordered, how do our cells tell which proteins need to be properly folded, and which don’t? “It’s a big mystery,” said Kopito, and one that he’s studying. This question has implications for how people develop neurodegenerative diseases, all of which appear to be age-related.

Huntington’s disease is caused by a specific mutated protein. But the body makes this mutant protein all your life, so why do you get the disease in later adulthood? Kopito said it’s because the body’s protective mechanisms stop doing their job as we get older. He said his lab hopes to determine what these mechanisms are.

A bad influence

But it’s clear what happens when these mechanisms stop working – misfolded proteins start recruiting normal versions of the same protein and form large aggregations. The presence of these aggregations in neurons has been closely linked with several neurodegenerative diseases.

Kopito found that the mutant protein associated with Huntington’s disease can leave one cell and enter another one, stirring up trouble in each new cell as it progresses down the line. The spread of the misfolded protein may explain how Huntington’s progresses through the brain.

This disease, like Parkinson’s and Alzheimer’s, starts in one area of the brain and spreads to the rest of it. This is also similar to the spread of prions, the self-replicating proteins implicated in mad cow disease and, in humans, Creutzfeldt-Jakob disease. As the misfolded protein reaches more parts of the brain, it could be responsible for the progressive worsening of these diseases.

Now that we know that these misfolded proteins spend part of their time outside of cells, traveling from one cell to another, new drugs could target them there, Kopito said. This could help prevent or at least block the progression of these diseases.

Kopito is currently working to figure out how misfolded proteins get past cell membranes into cells in the first place. It is only once in the cell’s cytoplasm that these proteins can recruit others. So these studies could help find ways to keep these mischief-makers away from the normal proteins.

He is also collaborating with biology professor Liqun Luo to track these proteins between cells in the well-mapped fruit fly nervous system. In the future, Kopito said he hopes to link his cell biology work to disease pathology in order to understand the role misfolded proteins play in human disease.

Scientist Discover Cell of Origin for Childhood Muscle Cancer

Researchers at Oregon Health & Science University Doernbecher Children’s Hospital have defined the cell of origin for a kind of cancer called sarcoma. In a study published as the Featured Article in the journal Cancer Cell, they report that childhood and adult sarcomas are linked in their biology, mutations and the cells from which these tumors first start. These findings may lead to non-chemotherapy medicines that can inhibit “molecular targets” such as growth factor receptors, thereby stopping or eradicating the disease.

Childhood muscle cancer, or rhabdomyo sarcoma, is a condition that when spread throughout the body has a low survival rate – just 20 percent to 40 percent. In adults with soft tissue sarcomas, survival can be even lower. Now, for the first time, the researchers have shown from where these tumors arise and what drives them to grow and spread.

“A commonly held belief is that cancers should be cut out, burned out or killed. There is a fourth option – to have cancer cells choose to become normal cells, in this case muscle cells,” said Charles Keller, M.D., principal investigator of the study, leader of Pediatric Cancer Biology Program in the Papé Family Pediatric Research Institute at OHSU Doernbecher Children’s Hospital, and a member of the OHSU Knight Cancer Institute and the Oregon Stem Cell Center at OHSU.

“At least for a subset of patients, possibly the ones with hereditary cancer, one approach suggested by our research might be to administer drugs that muscle cancers to convert into non-cancerous muscle fibers. This is a minority opinion, but one held by a small group of careful scientists throughout the United States and abroad,” said Keller.

The survival rate for childhood muscle cancer that has spread has remained unchanged for more than 40 years. It has reached the point that increasing the intensity of chemotherapy, radiation or surgery is no longer having any improved effect, Keller explained. He and colleagues have taken a novel approach in the laboratory as well as in new clinical trials, using non-chemotherapy medicines to inhibit “molecular targets” such as growth factor receptors.

Suman Malempati, M.D., assistant professor of pediatrics (hematology/oncology) and director of the Oncology Developmental Therapeutics Program at OHSU Doernbecher Children’s Hospital, is the lead on a national clinical trial of one such growth factor inhibitor. This is the Children’s Oncology Group’s first trial incorporating a molecularly targeted drug into a clinical trial for childhood muscle cancer and was funded by CureSearch for Children’s Cancer, a nationwide network of hospitals, doctors and leading scientists that develop new treatments for childhood cancer.

This type of therapy tailored to a cancer’s mutation was first pioneered at OHSU by Brian J. Druker, M.D., director of the OHSU Knight Cancer Institute and recipient of the 2009 Lasker~DeBakey Clinical Medical Research Award, commonly referred to as America’s Nobel Prize. Druker and colleagues developed Gleevec, the first genetically targeted, non-chemotherapy pill for chronic myeloid leukemia (CML) that left healthy cells unharmed and converted this fatal cancer into a manageable chronic condition.

Onset of Genetic Diseases Identified

BARCELONA – Scientists from Universitat Autonoma de Barcelona (UAB) have identified a mechanism that could trigger onset of various genetic diseases.

They have found a process by which proteins with a tendency to cause conformational diseases such as amyotrophic lateral sclerosis, familial amyloidotic polyneuropathy, familial amyloidotic cardiomyopathy, etc. finally end up causing them.

The answer can be found in the separation of the proteins.

According to the researchers Salvador Ventura and Virgmnia Castillo, every day cells produce thousands of new proteins, which renew themselves every second and which, by obeying the orders prescribed in our genetic code, work towards the proper functioning of our body.

However, these proteins occasionally suffer genetic mutations, which can cause changes in their composition, thus preventing them from carrying out their functions and the activities they are assigned.

In many cases this gives way to the formation of toxic macromolecular aggregates – amyloid fibrils – which block our body’s protein quality control system and finally provoke cell death.

Protein aggregation and the misfolding of proteins can be linked to the origin of many conformational diseases, which can be either genetic or spontaneous.

As possible strategies to prevent the dissociation of proteins, the authors propose introducing genetic mutations into the proteins to strengthen their association and developing specific molecules to block the risk regions of already dissociated proteins.

The study appears in journal PLoS Computational Biology.