Thursday February 27, 2014
Researchers in the UK have genetically engineered a tomato to produce anthocyanins--the compounds that give some berries and a handful of other fruits and vegetables their purple-red colors. However, anthocyanin aren't just about pretty colors. They are thought to provide significant health benefits. In fact, when the tomatoes were developed several years ago, testing showed that the provided some protection against tumors in cancer-prone mice.
As a result, a company has formed to begin medical trials to evaluate if juice from the genetic engineered anthocyanin tomatoes has measurable benefits for humans.
You can read more details on these tomatoes at the Animate Discovery blog.
Wednesday February 19, 2014
You may have heard about the sensational study a couple weeks ago which showed that certain type of stress can turn normal adult cells into stem cells. Many news stories fixated particularly on the finding that simple acid was enough to generate pluripotent stem cells from regular mouse blood cells. Such an easy way to produce stem cells would be a phenomenal achievement. In the last several days, however, concerns about the integrity of these novel findings have begun to replace much of the initial excitement.
The study, published in the journal Nature, was carried out at the prestigious RIKEN Center for Developmental Biology in Japan.
Within days of the publication, however, peers noticed problems with figures in the paper. A photograph was duplicated and artifacts on gel images appeared to have been retouched. In response to these reported discoveries, the RIKEN Research Institute opened an investigation to look into the "irregularities" in the publication last week.
Adding to the concern, last week UC Davis stem-cell researcher Paul Knoepfler also blogged about the difficulty many labs are having in repeating the work. It appears that at least 9 other labs have been unable to produce stem cells using the reported approach. Even more disturbing, one of the publication's own authors reports that he cannot get the method to work in the new lab that he founded when he left RIKEN just before publication.
You can read more about the developing concerns with the publication in Nature and Science. While it is not clear yet whether there is any implication of fraud in with this research, there are certainly a number of reasons to be skeptical of the results are this point.
Monday February 17, 2014
It's been known for over 100 years that dark sticky deposits known as plaques form in the brains of Alzheimer's patients. These are caused by fragments of a protein known as amyloid. For some reason, normal amyloid sometimes folds up incorrectly and the misfolded molecule then clumps together to form these plaques between nerve cells. Alzheimer's seems to start as soon as the amyloid clumps begin to accumulate and disrupt brain cell function. The large visible plaques occur late in the process.
Several recent drug failures indicate that just reducing the amount of amyloid to try to slow the formation of the plaques doesn't seem to really affect Alzheimer's progression. As a result, a lot of recent research has focused on why cells have trouble getting rid of misfolded forms of the amyloid protein appears necessary, which causes it to accumulate with age.
Since there is always some misfolding of the millions of proteins produced constantly by organisms, cells have a sophisticated way to dispose of this potentially damaging debris. When misfolded protein accumulate, cells activate the unfolded protein response which captures the proteins in specialized cell vesicles called lysozomes which contain enzymes to degrade them.
Essentially, then, cells have a way to digest and eliminate misfolded proteins. First, though, they have to realize these trashed proteins are around and locate where they are in the cell. For this purpose, there are receptors on the surfaces of the lysosomes that help identify and capture misfolded proteins.
Just a few days ago, researchers published a study that showed that SORLA, a receptor found on lysosomes, is critical for proper processing of the amyloid precursor protein. Genetically engineered mice with increased SORLA cleared the amyloid-plaque forming peptides more quickly. The researcher also noted that mutations in the gene for SORLA have been linked to early onset of Alzheimer's.
This recent study identifying a protein involved in managing the processing of misfolded amyloid complements a different discovery last fall that showed how regulating another part of the unfolded protein response could protect mice from dementia. Slowly there seems to be real progress uncovering the biological causes for Alzheimer's and related neurodegenerative diseases, and these discovery offer new approaches for treating these diseases.
You can read more about the recent work unraveling how SORLA regulates amyloid process at the Alzforum.
Monday February 10, 2014
There are heart transplants and artificial hearts but they are poor substitutes for the one you are born with. While the heart has been a symbol of love and desire since ancient times, it's pumping actions does truly sustain our lives from minute to minute. In fact, keeping your cardiovascular system fit may be the most important thing you can do for your personal health.
It is tradition to focus on your heart's desires for Valentine's Day. It seems this holiday would also be a good time to consider your own heart health. Take some time on Valentine's Day to tend to both the romantic and physical dimensions of the heart. You'll find that their needs are not so different.
Take a look at Have a Care for Your Heart on Valentine's Day.