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“NASA intends to shift its human spaceflight program out to the Moon and cis-lunar region, evaluating new habitat technologies, surface transportation systems, fuel generation, and storage solutions, as well as additional technologies that need to be developed prior to traveling to the surface of the Moon and deeper into space.”
My view, having worked DOD programs with NASA, and serving with Charlie Bolden in the USMC, ( Obama’s NASA Director) and several former astronauts that I served with (I was not in thier club but I had several of them back in the day take squadron patches and other such to orbit for me) that were basically at odds with Charlie’s direction.
NASA started to lose its way 30 years ago when it started putting school teachers in Space. This was about the time Charlie joined NASA.They went from risk takers stretching the limits of aviation technology and space to overly cautious globalists.
The practical effect was that in DOD, we had to do our own thing for hypersonics, power source technology, imagery and satellites. You see this in the rise of commercial enterprises as well. but I’d prefer the risk taking leading edge technology attitude [Reply]
Originally Posted by Coyote:
“NASA intends to shift its human spaceflight program out to the Moon and cis-lunar region, evaluating new habitat technologies, surface transportation systems, fuel generation, and storage solutions, as well as additional technologies that need to be developed prior to traveling to the surface of the Moon and deeper into space.”
My view, having worked DOD programs with NASA, and serving with Charlie Bolden in the USMC, ( Obama’s NASA Director) and several former astronauts that I served with (I was not in thier club but I had several of them back in the day take squadron patches and other such to orbit for me) that were basically at odds with Charlie’s direction.
NASA started to lose its way 30 years ago when it started putting school teachers in Space. This was about the time Charlie joined NASA.They went from risk takers stretching the limits of aviation technology and space to overly cautious globalists.
The practical effect was that in DOD, we had to do our own thing for hypersonics, power source technology, imagery and satellites. You see this in the rise of commercial enterprises as well. but I’d prefer the risk taking leading edge technology attitude
Thats all fine and dandy man. Now, lets get to the nuts and bolts. Have we been visited by aliens? [Reply]
Originally Posted by BigRedChief:
Why bother with anything in space until a different President is in place? Whatever the idea or project is in space, its going to take years to pull off. He could flip flop at any time based on someone he talked too the night before and say he's canceling the project.
All Presidents could do that. Waiting for that reason makes no sense. [Reply]
Originally Posted by tooge:
The "fact" is that any sitting president "could" flip flop based on new information they receive from lobbyists, etc. So, to even post this opinion in the science is cool thread makes it a political post in a non political thread. Because you mentioned that something should or shouldn't be done until a "different president" is in office, makes it a political post. That is a fact.
Originally Posted by BigRedChief:
Why bother with anything in space until a different President is in place? Whatever the idea or project is in space, its going to take years to pull off. He could flip flop at any time based on someone he talked too the night before and say he's canceling the project.
Originally Posted by tooge:
And just like that, a thread about science and some of the coolest new science around, and BOOM, it becomes political. Sad
Not only that, but it's congress that said no to the plan - not the president. :-) [Reply]
Alzheimer’s disease is a progressive memory disorder that affects nearly one in three seniors and is on the rise, currently affecting 43 million people worldwide.
Behind the memory impairments, there is a perfect storm of destruction in the brain, stemming in part from accumulations of a protein called tau. Normally a stabilizing structure inside of neurons, tau can accumulate in long tangles that disrupt the ability of neurons to communicate with one another.
University of New Mexico researchers have developed a vaccine that could prevent the formation of the tau tangles and potentially prevent the cognitive decline typically seen in Alzheimer’s patients.
In a paper published last week in NPJ Vaccines, the team reported it had engineered a vaccine using virus-like particles (VLPs, for short) that eliminated the tau tangles in mice that had been bred to develop symptoms like those affecting human Alzheimer’s patients.
“We’re excited by these findings, because they seem to suggest that we can use the body’s own immune system to make antibodies against these tangles, and that these antibodies actually bind and clear these tau tangles,” said Nicole Maphis, a PhD candidate in UNM’s Biomedical Sciences Graduate Program.
Maphis, working in the lab of Kiran Bhaskar, PhD, an associate professor in UNM’s Department of Molecular Genetics & Microbiology, found that when the vaccine was given to mice, they developed antibodies that cleared the tau protein from their brains – and the response lasted for months.
Then, she tested the animals in a battery of maze-like tests. Mice receiving the vaccination performed remarkably better than those that hadn’t. MRI scans showed that the vaccinated animals had less brain shrinkage, suggesting that the vaccine prevented neurons from dying.
Maphis also found significantly fewer tangles in both the cortex and the hippocampus – areas in the brain that are important for learning and memory, and which are destroyed in Alzheimer’s.
“These results confirm that targeting tau tangles using a vaccine intervention could rescue memory impairments and prevent neurons from dying,” Maphis said.
The vaccine was created with help from UNM scientists David Peabody and Bryce Chackerian. The pair helped pioneer the use of VLPs to create vaccines targeting dengue virus, hepatitis B, human papillomavirus and amyloid beta protein (which is also present in the brains of Alzheimer’s patients).
VLPs are derived from viruses that have their genomes removed, leaving only their outer protein shell. Lacking a genome, they’re unable to reproduce, but the body’s immune system still recognizes them as foreign invaders and manufactures antibodies to neutralize the proteins attached to their surface. In this case, a portion of tau protein on the surface of the VLP triggers an immune response, leading to the elimination of the tau tangles.
Going forward, Bhaskar hopes to obtain funding to commercialize this vaccine in order to create an injection that could potentially be tested in human patients. However, moving a drug from bench to bedside can cost millions of dollars and take decades. [Reply]
Alzheimer’s disease is a progressive memory disorder that affects nearly one in three seniors and is on the rise, currently affecting 43 million people worldwide.
Behind the memory impairments, there is a perfect storm of destruction in the brain, stemming in part from accumulations of a protein called tau. Normally a stabilizing structure inside of neurons, tau can accumulate in long tangles that disrupt the ability of neurons to communicate with one another.
University of New Mexico researchers have developed a vaccine that could prevent the formation of the tau tangles and potentially prevent the cognitive decline typically seen in Alzheimer’s patients.
In a paper published last week in NPJ Vaccines, the team reported it had engineered a vaccine using virus-like particles (VLPs, for short) that eliminated the tau tangles in mice that had been bred to develop symptoms like those affecting human Alzheimer’s patients.
“We’re excited by these findings, because they seem to suggest that we can use the body’s own immune system to make antibodies against these tangles, and that these antibodies actually bind and clear these tau tangles,” said Nicole Maphis, a PhD candidate in UNM’s Biomedical Sciences Graduate Program.
Maphis, working in the lab of Kiran Bhaskar, PhD, an associate professor in UNM’s Department of Molecular Genetics & Microbiology, found that when the vaccine was given to mice, they developed antibodies that cleared the tau protein from their brains – and the response lasted for months.
Then, she tested the animals in a battery of maze-like tests. Mice receiving the vaccination performed remarkably better than those that hadn’t. MRI scans showed that the vaccinated animals had less brain shrinkage, suggesting that the vaccine prevented neurons from dying.
Maphis also found significantly fewer tangles in both the cortex and the hippocampus – areas in the brain that are important for learning and memory, and which are destroyed in Alzheimer’s.
“These results confirm that targeting tau tangles using a vaccine intervention could rescue memory impairments and prevent neurons from dying,” Maphis said.
The vaccine was created with help from UNM scientists David Peabody and Bryce Chackerian. The pair helped pioneer the use of VLPs to create vaccines targeting dengue virus, hepatitis B, human papillomavirus and amyloid beta protein (which is also present in the brains of Alzheimer’s patients).
VLPs are derived from viruses that have their genomes removed, leaving only their outer protein shell. Lacking a genome, they’re unable to reproduce, but the body’s immune system still recognizes them as foreign invaders and manufactures antibodies to neutralize the proteins attached to their surface. In this case, a portion of tau protein on the surface of the VLP triggers an immune response, leading to the elimination of the tau tangles.
Going forward, Bhaskar hopes to obtain funding to commercialize this vaccine in order to create an injection that could potentially be tested in human patients. However, moving a drug from bench to bedside can cost millions of dollars and take decades.
I just read this and was coming to post it in here. This is really something that should get way more attention. Alzheimer's is such a devastating disease with how it puts such a burden on families and just how much it costs to take care of someone with Alzheimer's. According to ALZ.org, Alzheimer's will cost the US $290 bil this year. There really should be better awareness. [Reply]
I hope it all proves to be true, Alzheimer's has been what I have always assumed I would die from, I guess since my great grandmother passed away from it 20some years ago. If they are on to something not sure if it can have immediate applications, but I'd love to know that progress is being made in this area. [Reply]
Originally Posted by allen_kcCard:
I hope it all proves to be true, Alzheimer's has been what I have always assumed I would die from, I guess since my great grandmother passed away from it 20some years ago. If they are on to something not sure if it can have immediate applications, but I'd love to know that progress is being made in this area.
We just filled you in yesterday. Don't tell me you forgot. [Reply]
Blood transfusion is an indispensable part of the health care system, saving many thousands of lives annually. The blood used must be carefully matched since transfusion with mismatched blood types can lead to fatal consequences. However, this can be problematic in emergency situations, where there is no time for blood matching: in that case the use of universal donor blood (Type O) is essential, but supply of O Type blood is often short.
Enzymes can be used to convert A and B type red blood cells (RBC) into O type, broadening the supply. However the enzymes available to date have not worked well on whole blood, thus new enzymes are needed. We in the Withers Laboratories asked: Where do we find those enzymes?
Interestingly the answer to this question was, within us! In recent years the research community has started to realize the importance of the human microbiome in the context of human health. However, it may prove to be even more important since the microorganisms within us also harbor enzyme activities we do not even known about, yet. The human gut is covered with mucins, large glycoproteins presenting a variety of glycan structures on their surface, including those of the blood group antigens. Bacteria within the gut derive some of their energy by foraging these glycans, so must produce enzymes to cut them off. We investigated this community by use of functional metagenomics - a technique that allows the screening of enzyme activity without culture bias. By screening a library of gut microbiome enzymes using fluorogenic substrates that mimic the blood antigen carbohydrates, we identified a set of enzymes expressed by a particular bacterium, Flavonifractor plautii, that are able to cleave the A antigen very efficiently.
An important factor in the efficient cleavage of substrates bound to cell surfaces, such as the A antigens on the RBCs, is the ability of the enzyme to associate with the cell surface. Some enzymes do this by acquiring a net charge that is complementary to that of the cell surface. In our case the enzymes carry carbohydrate binding modules (CBMs) that interact with other cell surface glycans allowing them to rapidly cleave the nearby A antigens. The combination of high substrate activity and affinity for the RBC surface makes our enzymes very efficient in the removal of A antigens from RBCs in whole blood samples.
In the future we hope these enzymes will be widely deployed for the production of enzymatically converted universal donor blood (ECO O Type RBCs) directly after blood donation. In addition to their use in RBC conversion we plan to test the use of these and related enzymes in the removal of antigens from other important cell surfaces and tissues. Such approaches could widen the availability of good “matches” in organ and stem cell transplantation's.
For me it was very interesting to see what our gut microbiome had to offer and I am keen to see what kind of other activities will be discovered within the human gut microbiome in the future. [Reply]
Blood transfusion is an indispensable part of the health care system, saving many thousands of lives annually. The blood used must be carefully matched since transfusion with mismatched blood types can lead to fatal consequences. However, this can be problematic in emergency situations, where there is no time for blood matching: in that case the use of universal donor blood (Type O) is essential, but supply of O Type blood is often short.
Enzymes can be used to convert A and B type red blood cells (RBC) into O type, broadening the supply. However the enzymes available to date have not worked well on whole blood, thus new enzymes are needed. We in the Withers Laboratories asked: Where do we find those enzymes?
Interestingly the answer to this question was, within us! In recent years the research community has started to realize the importance of the human microbiome in the context of human health. However, it may prove to be even more important since the microorganisms within us also harbor enzyme activities we do not even known about, yet. The human gut is covered with mucins, large glycoproteins presenting a variety of glycan structures on their surface, including those of the blood group antigens. Bacteria within the gut derive some of their energy by foraging these glycans, so must produce enzymes to cut them off. We investigated this community by use of functional metagenomics - a technique that allows the screening of enzyme activity without culture bias. By screening a library of gut microbiome enzymes using fluorogenic substrates that mimic the blood antigen carbohydrates, we identified a set of enzymes expressed by a particular bacterium, Flavonifractor plautii, that are able to cleave the A antigen very efficiently.
An important factor in the efficient cleavage of substrates bound to cell surfaces, such as the A antigens on the RBCs, is the ability of the enzyme to associate with the cell surface. Some enzymes do this by acquiring a net charge that is complementary to that of the cell surface. In our case the enzymes carry carbohydrate binding modules (CBMs) that interact with other cell surface glycans allowing them to rapidly cleave the nearby A antigens. The combination of high substrate activity and affinity for the RBC surface makes our enzymes very efficient in the removal of A antigens from RBCs in whole blood samples.
In the future we hope these enzymes will be widely deployed for the production of enzymatically converted universal donor blood (ECO O Type RBCs) directly after blood donation. In addition to their use in RBC conversion we plan to test the use of these and related enzymes in the removal of antigens from other important cell surfaces and tissues. Such approaches could widen the availability of good “matches” in organ and stem cell transplantation's.
For me it was very interesting to see what our gut microbiome had to offer and I am keen to see what kind of other activities will be discovered within the human gut microbiome in the future.
As an O- blood type myself, it'd be nice if the blood donation centers would care about me a little less. They're knocking down my door every 8 weeks on the dot. [Reply]
