This webcast is packed with information on the makeup and function of eukaryotic cells, which are the type of cells found in animals. It is part of a interesting series of science webcasts by Crash Course. The webcast style might be a bit too hyperactive and flippant for some but the content is quite interesting and the videos they are are of similar style and quality so if you like this one you can subscribe to their channel. They offer quite a few webcasts on science but they also offer webcasts on history.
A disease-fighting protein in our teardrops has been tethered to a tiny transistor, enabling UC Irvine scientists to discover exactly how it destroys dangerous bacteria. The research could prove critical to long-term work aimed at diagnosing cancers and other illnesses in their very early stages.
Ever since Nobel laureate Alexander Fleming found that human tears contain antiseptic proteins called lysozymes about a century ago, scientists have tried to solve the mystery of how they could relentlessly wipe out far larger bacteria. It turns out that lysozymes have jaws that latch on and chomp through rows of cell walls like someone hungrily devouring an ear of corn.
“Those jaws chew apart the walls of the bacteria that are trying to get into your eyes and infect them,” said molecular biologist and chemistry professor Gregory Weiss, who co-led the project with associate professor of physics & astronomy Philip Collins.
The researchers decoded the protein’s behavior by building one of the world’s smallest transistors – 25 times smaller than similar circuitry in laptop computers or smartphones. Individual lysozymes were glued to the live wire, and their eating activities were monitored.
“Our circuits are molecule-sized microphones,” Collins said. “It’s just like a stethoscope listening to your heart, except we’re listening to a single molecule of protein.”
It took years for the UCI scientists to assemble the transistor and attach single-molecule teardrop proteins. The scientists hope the same novel technology can be used to detect cancerous molecules. It could take a decade to figure out but would be well worth it, said Weiss, who lost his father to lung cancer.
“If we can detect single molecules associated with cancer, then that means we’d be able to detect it very, very early,” Weiss said. “That would be very exciting, because we know that if we treat cancer early, it will be much more successful, patients will be cured much faster, and costs will be much less.”
The project was sponsored by the National Cancer Institute and the National Science Foundation. Co-authors of the Science paper are Yongki Choi, Issa Moody, Patrick Sims, Steven Hunt, Brad Corso and Israel Perez.
Living and eating healthily is tricky but not entirely confusing. The whole area of eating healthy food and what is a healthy weight is one where the scientific inquiry process and the complexity of scientific research on what is healthy for us is clear. Scientists study various issues and learn things but creating simple rules has proven difficult. Different studies seem to show benefits of contradictory advice, advice once seen as wise is now seen as wrong…
This is an area I am far from knowledgable about. Still I try to pay some attention as I like being healthy. Being sick is the quickest way to appreciate how great it is to be healthy. From various things I have skimmed it seems there is more evidence from several studies about how difficult it is to lose weight. Our bodies seem to work against our efforts.
It seems to me the most important thing to take from this, is the importance of maintaining a healthy weight: since you can’t just easily make up for a bad year of weight gain. I am not sure why I haven’t seen this note in most of what I have read – I suspect it is our reluctance to make value judgements about what is healthy. The problem I see with that is, the best advice we have is confusing enough without people with more knowledge being reluctant to state their best advice given the current knowledge. That doesn’t mean the suggestions are right, but at least they are educated guesses.
I try to eat relatively healthily. Which for me means taking steps to increase the amount of vegetables I eat (especially greens and some fiber) and decrease the amount of sweets and heavily processed food I eat (I still eat way too much heavily processed food). And I try to exercise as it seems to have many benefits including helping make up for some weaknesses in your diet (like eating too many calories and too many “empty calories). In my opinion (which on this topic may well not be worth much) eating a bit more stuff that really isn’t so good for you and exercising more is an easier tradeoff than trying to eat perfectly and do the minimum amount of exercise needed to stay healthy.
I also eat yogurt – I like it and the beneficial benefits of some bacteria seems likely. I heard recently something that surprised me which is that the beneficial bacteria remain for close to 2 weeks. I figured they would be gone in a couple days. I only heard that from one source (I can’t remember now but some seemingly knowledgable source – scientist researching the area), so it might not be accurate but it was interesting.
Here is an example of one of these health studies. They find that a low protein diet resulted in a loss of “lean weight” (muscle…) and more fat than a comparable diet with more protein. The same weight with a higher percentage of fat is not a good thing for human health. Thus the message is that a lower protein diet has this risk that must be considered (and therefor higher protein diets may well be wise). Of course things get much more complicated than that when we actually try to live by a diet.
A reader commented on a previous post (MIT Engineers Design New Type of Nanoparticle for Vacines) asking about how vaccines can fight cancer. Preventative vaccines can build up immune response to viruses which cause cancer. So the vaccine actually works against the virus which prevents the virus from causing cancer.
The U.S. Food and Drug Administration (FDA) has approved two vaccines, Gardasil® and Cervarix®, that protect against infection by the two types of human papillomavirus (HPV) – types 16 and 18 – that cause approximately 70% of all cases of cervical cancer worldwide. At least 17 other types of HPV are responsible for the remaining 30% of cervical cancer cases. HPV types 16 and/or 18 also cause some vaginal, vulvar, anal, penile, and oropharyngeal cancers.
Many scientists believe that microbes cause or contribute to between 15% and 25% of all cancers diagnosed worldwide each year, with the percentages being lower in developed than developing countries.
Vaccines can also help stimulate the immune system to fight cancers.
B cells make antibodies, which are large secreted proteins that bind to, inactivate, and help destroy foreign invaders or abnormal cells. Most preventive vaccines, including those aimed at hepatitis B virus (HBV) and human papillomavirus (HPV), stimulate the production of antibodies that bind to specific, targeted microbes and block their ability to cause infection. Cytotoxic T cells, which are also known as killer T cells, kill infected or abnormal cells by releasing toxic chemicals or by prompting the cells to self-destruct (a process known as apoptosis).
Other types of lymphocytes and leukocytes play supporting roles to ensure that B cells and killer T cells do their jobs effectively. These supporting cells include helper T cells and dendritic cells, which help activate killer T cells and enable them to recognize specific threats.
Cancer treatment vaccines are designed to work by activating B cells and killer T cells and directing them to recognize and act against specific types of cancer. They do this by introducing one or more molecules known as antigens into the body, usually by injection. An antigen is a substance that stimulates a specific immune response. An antigen can be a protein or another type of molecule found on the surface of or inside a cell.
McMaster University researchers have developed a vaccine which successfully treats people with an allergy to cats. Traditionally, frequent allergy shots have been considered the most effective way to bring relief — other than getting rid of the family pet — for the 8 to 10% of the population allergic to cats.
The researchers took one protein (molecule) that cats secrete on their fur which causes the majority of allergic problems. Using blood samples from 100 patient volunteers allergic to cats, they deconstructed the molecule and identified short regions within the protein which activate T-cells (helper cells that fight infection) in the immune system.
The development of a vaccine to treat people allergic to cats is the first in a line of vaccines developed with Adiga Life Sciences, a company established at McMaster in 2008. It is a joint venture between McMaster University Circassia Ltd., a UK-based biotech company.
Adiga and McMaster are now collaborating on research into the use of peptide immunotherapy for house dust mite, ragweed, grass, birch tree and moulds
All life on Earth shares a single common ancestor, a new statistical analysis confirms.
…
Because microorganisms of different species often swap genes, some scientists have proposed that multiple primordial life forms could have tossed their genetic material into life’s mix, creating a web, rather than a tree of life.
…
A universal common ancestor is at least 102,860 times more probable than having multiple ancestors, Theobald calculates.
…
For his analysis, Theobald selected 23 proteins that are found across the taxonomic spectrum but have structures that differ from one species to another. He looked at those proteins in 12 species – four each from the bacterial, archaeal and eukaryotic domains of life.
Then he performed computer simulations to evaluate how likely various evolutionary scenarios were to produce the observed array of proteins. Theobald found that scenarios featuring a universal common ancestor won hands down against even the best-performing multi-ancestor models.
Very interesting. Surprising too. As the article points out this doesn’t mean all life ever on Earth evolved from the single ancestor – life that has gone extinct could be from outside this single “tree.”
Non-infectious prion proteins found in the brain may contribute to Alzheimer’s disease, researchers have found.
…
normal prion proteins produced naturally in the brain interact with the amyloid-β peptides that are hallmarks of Alzheimer’s disease. Blocking this interaction in preparations made from mouse brains halted some neurological defects caused by the accumulation of amyloid-β peptide. It was previously thought that only infectious prion proteins, rather than their normal, non-infectious counterparts, played a role in brain degeneration.
…
Alzheimer’s disease has long been linked to the build-up of amyloid-β peptides, first into relatively short chains known as oligomers, and then eventually into the long, sticky fibrils that form plaques in the brain. The oligomeric form of the peptide is thought to be toxic, but exactly how it acts in the brain is unknown.
Researchers discovered of a specific protein called disabled-2 (Dab2) that switches on the process that releases cancer cells from the original tumor and allows the cells to spread and develop into new tumors in other parts of the body.
The process called epithelial-mesenchymal transdifferientiation (EMT) has been known to play a role in releasing cells (epithelial cells) on the surface of the solid tumor and transforming them into transient mesenchymal cell: cells with the ability to start to grow a new tumor.
This is often the fatal process in breast, ovarian, pancreatic and colon-rectal cancers.
Searching to understand how the EMT process begins, Ge Jin, who has joint appointments at the Case Western Reserve University School of Dental Medicine and the Lerner Research Institute at the Cleveland Clinic, began by working backwards from EMT to find its trigger. The researchers found that a compound called transforming growth factor-ß (TGF-ß) triggers the formation of the Dab2 protein. It was this protein, Dab2, that activated the EMT process.
He discovered that when the researchers knocked out Dab2, EMT was not triggered. “This is the major piece in cancer research that has been missing,” Jin said. Most tumors are epithelial in origin and have epithelial markers on their surface. The EMT process takes place when some of those cells dislodge from the surface and undergo a transformation into a fibrous mesenchymal cell maker with the ability to migrate.
“EMT is the most important step in this process,” said Jin. He was part of a six-member research team, led by Philip Howe from the Department of Cancer Biology at the Lerner Research Institute in a National Institute of Cancer-funded study. The research group studied the biological processes that initiated the cancer spread by using cancer cells in animal models.
“If we can understand the signaling pathway for modulating EMT, then we can design drugs to delay or halt EMT cells and control tumor progression,” Jin said. Beyond cancer, Jin said. “The process we discovered may lead to understanding how other diseases progress.”
scientists transferred prion populations from brain cells to other cells in culture and observed the prions that adapted to the new cellular environment out-competed their brain-adapted counterparts. When returned to the brain cells, the brain-adapted prions again took over the population.
Charles Weissmann, head of Scripps Florida’s department of infectology who led the study, said: “On the face of it, you have exactly the same process of mutation and adaptive change in prions as you see in viruses.
“This means that this pattern of Darwinian evolution appears to be universally active. “In viruses, mutation is linked to changes in nucleic acid sequence that leads to resistance.
“Now, this adaptability has moved one level down- to prions and protein folding – and it’s clear that you do not need nucleic acid (DNA or RNA) for the process of evolution.”
…
He said: “The prion protein is not a clone, it is a quasi-species that can create different protein strains even in the same animal. “The abnormal prion proteins multiply by converting normal prion proteins.
“The implication of Charles Weissmann’s work is that it would be better to cut off that supply of normal prion proteins rather than risk the abnormal prion adapting to a drug and evolving into a new more virulent form.
The above webcast shows protein synthesis, from a 1971 Stanford University video with Paul Berg (Nobel Laureate – 1980 Nobel Prize for Chemistry and National Medal of Science in 1983). The film does not exactly present the traditional scientist stereotype. It does pretty much present the typical California 1970’s hippie stereotype though.
