Neuroscience

Articles and news from the latest research reports.

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Research advances understanding of the human brain Advanced neuroimaging techniques are giving researchers new insight into how the human brain plans and controls limb movements. This advance could one day lead to new understanding of disease and dysfunction in the brain and has important implications for movement-impaired patient populations, like those who suffer from spinal cord injuries. Randy Flanagan (Psychology and Centre for Neuroscience Studies), working with colleagues at Western University, used functional magnetic resonance imaging (fMRI) to uncover what regions of the human brain are used to plan hand actions with the left and right arm. This study, spearheaded by Jason Gallivan, a Banting postdoctoral fellow at Queen’s found that by using the fMRI signals from several different brain regions, they could predict the limb to be used (left vs. right) and hand action to be performed (grasping vs. touching an object), moments before that movement is actually executed. “We are trying to understand how the brain plans actions,” says Dr. Gallivan. “By using highly sensitive analysis techniques that enable the detection of subtle changes in brain activity patterns, we can reveal which of a series of actions a volunteer is merely intending to do, seconds later. Mapping and characterizing these predictive signals across the human brain allows us to pinpoint the key brain structures involved in generating normal, everyday behaviours.” In another study, Dr. Flanagan and doctoral student Jonathan Diamond examined how the brain learns object mechanical properties, knowledge that is essential for skilled manipulation. They found that, through experience, humans use mismatches between predicted and actual fingertip forces and between predicted and actual object motions to build internal representations, or models, of the mechanical properties of the objects. “The goal of this work is to understand the representations underlying skilled manipulation,” explains Dr. Flanagan. “This is important because it will enable us to better characterize deficits in manipulation tasks that often result from stroke and neurological diseases.” Dr. Flanagan, Dr. Gallivan, and Ingrid Johnsrude (Psychology and Centre for Neuroscience Studies) have recently been awarded a CIHR operating grant to support ongoing neuroimaging work. Both research papers were published in the Journal of Neuroscience. Read Dr. Flanagan’s paper here and read the joint paper here. (Image: Getty Images)

Research advances understanding of the human brain

Advanced neuroimaging techniques are giving researchers new insight into how the human brain plans and controls limb movements. This advance could one day lead to new understanding of disease and dysfunction in the brain and has important implications for movement-impaired patient populations, like those who suffer from spinal cord injuries.

Randy Flanagan (Psychology and Centre for Neuroscience Studies), working with colleagues at Western University, used functional magnetic resonance imaging (fMRI) to uncover what regions of the human brain are used to plan hand actions with the left and right arm. This study, spearheaded by Jason Gallivan, a Banting postdoctoral fellow at Queen’s found that by using the fMRI signals from several different brain regions, they could predict the limb to be used (left vs. right) and hand action to be performed (grasping vs. touching an object), moments before that movement is actually executed.

“We are trying to understand how the brain plans actions,” says Dr. Gallivan. “By using highly sensitive analysis techniques that enable the detection of subtle changes in brain activity patterns, we can reveal which of a series of actions a volunteer is merely intending to do, seconds later. Mapping and characterizing these predictive signals across the human brain allows us to pinpoint the key brain structures involved in generating normal, everyday behaviours.”

In another study, Dr. Flanagan and doctoral student Jonathan Diamond examined how the brain learns object mechanical properties, knowledge that is essential for skilled manipulation. They found that, through experience, humans use mismatches between predicted and actual fingertip forces and between predicted and actual object motions to build internal representations, or models, of the mechanical properties of the objects.

“The goal of this work is to understand the representations underlying skilled manipulation,” explains Dr. Flanagan. “This is important because it will enable us to better characterize deficits in manipulation tasks that often result from stroke and neurological diseases.”

Dr. Flanagan, Dr. Gallivan, and Ingrid Johnsrude (Psychology and Centre for Neuroscience Studies) have recently been awarded a CIHR operating grant to support ongoing neuroimaging work.

Both research papers were published in the Journal of Neuroscience. Read Dr. Flanagan’s paper here and read the joint paper here.

(Image: Getty Images)

Filed under brain spinal cord injuries neuroimaging brain activity limb movements neuroscience science

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A proposed link between aging, autism, and oxidation Like any fac­tory, the body burns oxygen to get energy for its var­ious needs. As a result, detri­mental byprod­ucts are released and our cells try to clean up shop with antiox­i­dants. But as we age, this process becomes a losing battle. “Oxi­da­tion inex­orably moves us along toward an oxi­dized state,” said phar­ma­ceu­tical sci­ences pro­fessor Richard Deth. “You have to deal with it progressively.” One option is to slow down the syn­thesis of new pro­teins, a process that requires energy. Indeed, as we age, we pro­duce fewer new pro­teins, which explains why our capacity for learning and healing suffer as we grow old. Since every pro­tein orig­i­nates from instruc­tions in the DNA, pro­tein syn­thesis can be slowed down by turning off par­tic­ular genes. A process called epi­ge­netic reg­u­la­tion accom­plishes the task by adding mol­e­c­ular tags on top of the genome. The pro­tein methio­nine syn­thase reg­u­lates this process. But what reg­u­lates methio­nine syn­thase? Oxidation. “This enzyme is the most easily oxi­dized mol­e­cule in the body,” said Deth, whose research on the sub­ject was recently pub­lished in the journal PLOS ONE. The senior author for the study, Christina Mura­tore, received her doc­torate in phar­ma­ceu­tical sci­ences from North­eastern in 2010. When­ever the body is under oxida­tive stress, Deth explained, methio­nine syn­thase, or MS, stops working. He and his team hypoth­e­sized that MS plays an impor­tant reg­u­la­tory role in aging and that it might be impaired in autism, which Deth has con­nected to unchecked oxida­tive stress in pre­vious research. To examine their hypoth­esis, the researchers looked at post­mortem human brain sam­ples across the lifespan, with sub­jects as young as 28 weeks of fetal devel­op­ment to as old as 84 years. They mea­sured the levels of a mol­e­cule called MS mRNA, which tran­scribes the genetic code for methio­nine syn­thase into actual protein. As the sub­jects aged, their brain tissue showed lower levels of MS mRNA. But, sur­pris­ingly, the levels of the pro­tein itself remained con­stant across the lifespan. Deth and his col­leagues sus­pect that this observed decrease in MS mRNA over our lives may act as a check in the system to save energy that we no longer have in plen­tiful supply and to slow down oxida­tive stress. “One way that the system can guard against too much pro­tein syn­thesis is to restrict the amount of mRNA,” Deth said. The team also com­pared MS pro­tein and mRNA levels between brain tissue sam­ples from autistic and nor­mally devel­oping sub­jects. Autistic brains had markedly less MS mRNA than the con­trol sam­ples but sim­ilar pro­tein levels. Addi­tion­ally, the age-​​dependent trend seen in nor­mally devel­oping brains was not mim­icked among the autistic sample. If decreased MS mRNA does mean decreased pro­tein pro­duc­tion, it’s no big deal for adults who don’t need to make new pro­teins as often. But for the devel­oping brain, new pro­teins are crit­ical. “Your capacity for learning might be pre­ma­turely reduced because meta­bol­i­cally you can’t afford it,” Deth suggested. While the results are pre­lim­i­nary and will ben­efit from repeated studies and more inves­ti­ga­tion, Deth’s find­ings add to a growing body of evi­dence linking both aging and autism to oxida­tive stress.

A proposed link between aging, autism, and oxidation

Like any fac­tory, the body burns oxygen to get energy for its var­ious needs. As a result, detri­mental byprod­ucts are released and our cells try to clean up shop with antiox­i­dants. But as we age, this process becomes a losing battle.

“Oxi­da­tion inex­orably moves us along toward an oxi­dized state,” said phar­ma­ceu­tical sci­ences pro­fessor Richard Deth. “You have to deal with it progressively.”

One option is to slow down the syn­thesis of new pro­teins, a process that requires energy. Indeed, as we age, we pro­duce fewer new pro­teins, which explains why our capacity for learning and healing suffer as we grow old.

Since every pro­tein orig­i­nates from instruc­tions in the DNA, pro­tein syn­thesis can be slowed down by turning off par­tic­ular genes. A process called epi­ge­netic reg­u­la­tion accom­plishes the task by adding mol­e­c­ular tags on top of the genome. The pro­tein methio­nine syn­thase reg­u­lates this process. But what reg­u­lates methio­nine syn­thase? Oxidation.

“This enzyme is the most easily oxi­dized mol­e­cule in the body,” said Deth, whose research on the sub­ject was recently pub­lished in the journal PLOS ONE. The senior author for the study, Christina Mura­tore, received her doc­torate in phar­ma­ceu­tical sci­ences from North­eastern in 2010.

When­ever the body is under oxida­tive stress, Deth explained, methio­nine syn­thase, or MS, stops working. He and his team hypoth­e­sized that MS plays an impor­tant reg­u­la­tory role in aging and that it might be impaired in autism, which Deth has con­nected to unchecked oxida­tive stress in pre­vious research.

To examine their hypoth­esis, the researchers looked at post­mortem human brain sam­ples across the lifespan, with sub­jects as young as 28 weeks of fetal devel­op­ment to as old as 84 years. They mea­sured the levels of a mol­e­cule called MS mRNA, which tran­scribes the genetic code for methio­nine syn­thase into actual protein.

As the sub­jects aged, their brain tissue showed lower levels of MS mRNA. But, sur­pris­ingly, the levels of the pro­tein itself remained con­stant across the lifespan.

Deth and his col­leagues sus­pect that this observed decrease in MS mRNA over our lives may act as a check in the system to save energy that we no longer have in plen­tiful supply and to slow down oxida­tive stress. “One way that the system can guard against too much pro­tein syn­thesis is to restrict the amount of mRNA,” Deth said.

The team also com­pared MS pro­tein and mRNA levels between brain tissue sam­ples from autistic and nor­mally devel­oping sub­jects. Autistic brains had markedly less MS mRNA than the con­trol sam­ples but sim­ilar pro­tein levels. Addi­tion­ally, the age-​​dependent trend seen in nor­mally devel­oping brains was not mim­icked among the autistic sample.

If decreased MS mRNA does mean decreased pro­tein pro­duc­tion, it’s no big deal for adults who don’t need to make new pro­teins as often. But for the devel­oping brain, new pro­teins are crit­ical. “Your capacity for learning might be pre­ma­turely reduced because meta­bol­i­cally you can’t afford it,” Deth suggested.

While the results are pre­lim­i­nary and will ben­efit from repeated studies and more inves­ti­ga­tion, Deth’s find­ings add to a growing body of evi­dence linking both aging and autism to oxida­tive stress.

Filed under brain oxidation autism brain tissue lifespan antioxidants protein synthesis aging medicine science

80 notes

Adding to the list of disease-causing proteins in brain disorders A multi-institution group of researchers has found new candidate disease proteins for neurodegenerative disorders. James Shorter, Ph.D., assistant professor of Biochemistry and Biophysics at the Perelman School of Medicine, University of Pennsylvania, Paul Taylor, M.D., PhD, St. Jude Children’s Research Hospital, and colleagues describe in an advanced online publication of Nature that mutations in prion-like segments of two RNA-binding proteins are associated with a rare inherited degeneration disorder affecting muscle, brain, motor neurons and bone (called multisystem proteinopathy) and one case of the familial form of amyotrophic lateral sclerosis (ALS). "This study uses a variety of scientific approaches to provide powerful evidence that unregulated polymerization of proteins involved in RNA metabolism may contribute to ALS and related diseases," said Amelie Gubitz, Ph.D., a program director at the National Institute of Neurological Disorders and Stroke (NINDS). ALS, or Lou Gehrig’s disease, is a universally fatal neurodegenerative disease. Previous studies found that mutations in two related RNA-binding proteins, TDP-43 and FUS, cause some forms of ALS, but more proteins were suspected of causing other forms of the disease. TDP-43 and FUS regulate how the genetic code is translated for the assembly of proteins. There are over 200 human RNA-binding proteins, including FUS and TDP-43, raising the possibility that additional RNA-binding proteins might contribute to ALS pathology. Computer algorithms, based on protein sequences, designed to identify yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with neurodegenerative disease, harbor a distinctive prion-like segment. These segments are essential for the assembly of certain protein complexes. But, the interplay between human prion-like segments and disease is not well understood. Using yeast as a model organism, co-author Aaron Gitler, while at Penn in 2011, surveyed 133 of 200-plus candidate human RNA-binding proteins to predict new ALS disease genes, other than TDP-43 and FUS. They further winnowed the candidates to about 10 proteins with prion-like segments, and selected two candidates, TAF15 and EWSR1, for further study. Both TAF15 and EWSR1 aggregated in the test tube and were toxic in yeast. Remarkably, they also uncovered TAF15 and EWSR1 mutations in ALS patients that were not found in healthy individuals. Based on these findings, they proposed that RNA-binding proteins with prion-like segments might contribute very broadly to the pathology of ALS and related brain disorders. Characterizing the Top-Ten Taylor, Gitler, Shorter, and others continued to characterize the top-ten human RNA-binding proteins with prion-like segments. The Nature study describes that two more of the top-ten candidates, called hnRNPA1 and hnRNPA2B1, are mutated and cause familial cases of brain disease. The mutations in hnRNPA1 and hnRNPA2B1 were present in two families with an extremely rare inherited degeneration affecting muscle, brain, motor neuron, and bone and another from a person with familial ALS. Mutations in these two proteins fell in the prion-like segments and coincided with “sticky” regions in the proteins, making these regions more prone to assemble into self-organizing fibrils. The normal form of the proteins shows a natural tendency to assemble into fibrils, which is exacerbated by the disease mutations. "The mutations accelerate the formation of the fibrils that recruit normal protein to form more fibrils," noted co-first author Emily Scarborough, from Penn. This dysregulated assembly likely contributes to disease. Indeed, the disease mutations also promote excess incorporation of the proteins into stress granules within a cell and the formation of clumps in the cells of animal models of human neurodegenerative disease. "Neurodegenerative disease could ensue from unregulated fibril formation initiated spontaneously by environmental stress or another factor that regulates a protein’s assembly," says Scarborough. "This paper reflects an amazing collaborative effort and provides a great example of how understanding the underlying pure protein biochemistry can help explain how genetic mutations might cause pathology and disease," says Shorter. "The findings confirm a strong prediction that the disease-causing mutations make the prion-like segment ‘stickier’ and more prone to clump," added co-first author Zamia Diaz, also from Penn. Diseases associated with fibrils forming from prion-like domains in proteins frequently show “spreading” pathology, in which cellular degeneration via inclusions starts in one center of the brain and “spreads” to neighboring tissue. Although not directly addressed in the Nature study, the findings suggest that cell-to-cell transmission of a self-templating protein could contribute to the spreading pathology that is characteristic of these diseases. "Related proteins with prion-like domains must be considered candidates for initiating and perhaps propagating similar pathologies in muscle, brain, motor neurons, and bone," concluded Shorter.

Adding to the list of disease-causing proteins in brain disorders

A multi-institution group of researchers has found new candidate disease proteins for neurodegenerative disorders. James Shorter, Ph.D., assistant professor of Biochemistry and Biophysics at the Perelman School of Medicine, University of Pennsylvania, Paul Taylor, M.D., PhD, St. Jude Children’s Research Hospital, and colleagues describe in an advanced online publication of Nature that mutations in prion-like segments of two RNA-binding proteins are associated with a rare inherited degeneration disorder affecting muscle, brain, motor neurons and bone (called multisystem proteinopathy) and one case of the familial form of amyotrophic lateral sclerosis (ALS).

"This study uses a variety of scientific approaches to provide powerful evidence that unregulated polymerization of proteins involved in RNA metabolism may contribute to ALS and related diseases," said Amelie Gubitz, Ph.D., a program director at the National Institute of Neurological Disorders and Stroke (NINDS).

ALS, or Lou Gehrig’s disease, is a universally fatal neurodegenerative disease. Previous studies found that mutations in two related RNA-binding proteins, TDP-43 and FUS, cause some forms of ALS, but more proteins were suspected of causing other forms of the disease. TDP-43 and FUS regulate how the genetic code is translated for the assembly of proteins.

There are over 200 human RNA-binding proteins, including FUS and TDP-43, raising the possibility that additional RNA-binding proteins might contribute to ALS pathology. Computer algorithms, based on protein sequences, designed to identify yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with neurodegenerative disease, harbor a distinctive prion-like segment. These segments are essential for the assembly of certain protein complexes. But, the interplay between human prion-like segments and disease is not well understood.

Using yeast as a model organism, co-author Aaron Gitler, while at Penn in 2011, surveyed 133 of 200-plus candidate human RNA-binding proteins to predict new ALS disease genes, other than TDP-43 and FUS. They further winnowed the candidates to about 10 proteins with prion-like segments, and selected two candidates, TAF15 and EWSR1, for further study. Both TAF15 and EWSR1 aggregated in the test tube and were toxic in yeast.

Remarkably, they also uncovered TAF15 and EWSR1 mutations in ALS patients that were not found in healthy individuals. Based on these findings, they proposed that RNA-binding proteins with prion-like segments might contribute very broadly to the pathology of ALS and related brain disorders.

Characterizing the Top-Ten

Taylor, Gitler, Shorter, and others continued to characterize the top-ten human RNA-binding proteins with prion-like segments. The Nature study describes that two more of the top-ten candidates, called hnRNPA1 and hnRNPA2B1, are mutated and cause familial cases of brain disease. The mutations in hnRNPA1 and hnRNPA2B1 were present in two families with an extremely rare inherited degeneration affecting muscle, brain, motor neuron, and bone and another from a person with familial ALS.

Mutations in these two proteins fell in the prion-like segments and coincided with “sticky” regions in the proteins, making these regions more prone to assemble into self-organizing fibrils. The normal form of the proteins shows a natural tendency to assemble into fibrils, which is exacerbated by the disease mutations.

"The mutations accelerate the formation of the fibrils that recruit normal protein to form more fibrils," noted co-first author Emily Scarborough, from Penn. This dysregulated assembly likely contributes to disease. Indeed, the disease mutations also promote excess incorporation of the proteins into stress granules within a cell and the formation of clumps in the cells of animal models of human neurodegenerative disease.

"Neurodegenerative disease could ensue from unregulated fibril formation initiated spontaneously by environmental stress or another factor that regulates a protein’s assembly," says Scarborough.

"This paper reflects an amazing collaborative effort and provides a great example of how understanding the underlying pure protein biochemistry can help explain how genetic mutations might cause pathology and disease," says Shorter.

"The findings confirm a strong prediction that the disease-causing mutations make the prion-like segment ‘stickier’ and more prone to clump," added co-first author Zamia Diaz, also from Penn.

Diseases associated with fibrils forming from prion-like domains in proteins frequently show “spreading” pathology, in which cellular degeneration via inclusions starts in one center of the brain and “spreads” to neighboring tissue. Although not directly addressed in the Nature study, the findings suggest that cell-to-cell transmission of a self-templating protein could contribute to the spreading pathology that is characteristic of these diseases.

"Related proteins with prion-like domains must be considered candidates for initiating and perhaps propagating similar pathologies in muscle, brain, motor neurons, and bone," concluded Shorter.

Filed under neurodegenerative diseases motor neurons proteins Lou Gehrig's disease RNA metabolism medicine science

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Scientists Identify ‘Clean-Up’ Snafu That Kills Brain Cells in Parkinson’s Disease Researchers at Albert Einstein College of Medicine of Yeshiva University have discovered how the most common genetic mutations in familial Parkinson’s disease damage brain cells. The study, which published online in the journal Nature Neuroscience, could also open up treatment possibilities for both familial Parkinson’s and the more common form of Parkinson’s that is not inherited. "Our study found that abnormal forms of LRRK2 protein disrupt an important garbage-disposal process in cells that normally digests and recycles unwanted proteins including one called alpha-synuclein - the main component of those protein aggregates that gunk up nerve cells in Parkinson’s patients," said study leader Ana Maria Cuervo, M.D., Ph.D., professor of  developmental and molecular biology, of anatomy and structural biology, and of medicine and the Robert and Renee Belfer Chair for the Study of Neurodegenerative Diseases at Einstein. The name for the disrupted disposal process is chaperone-mediated autophagy (the word “autophagy” literally means “self-eating”). It involves specialized molecules that “guide” old and damaged proteins to enzyme-filled structures called lysosomes; there the proteins are digested into amino acids, which are then recycled within the cell. "We showed that when LRRK2 inhibits chaperone-mediated autophagy,alpha-synuclein doesn’t get broken down and instead accumulates to toxic levels in nerve cells,” said Dr. Cuervo. The study involved mouse neurons in tissue culture from four different animal models, neurons from the brains of patients with Parkinson’s with  LRRK2 mutations, and neurons derived from the skin cells of Parkinson’s patients via induced pluripotent stem (iPS) cell technology. All the lines of research confirmed the researchers’ discovery. "We’re now looking at ways to enhance the activity of this recycling system to see if we can prevent or delay neuronal death and disease," said Dr. Cuervo. "We’ve started to analyze some chemical compounds that look very promising." Dr. Cuervo hopes that such treatments could help patients with familial as well as nonfamilial Parkinson’s - the predominant form of the disease that also involves the buildup of alpha-synuclein. Dr. Cuervo is credited with discovering chaperone-mediated autophagy. She has published extensively on autophagy and its role in numerous diseases, such as cancer and Huntington’s disease, and its role in age-related conditions, including organ decline and weakened immunity. Dr. Cuervo is co-director of Einstein’s  Institute of Aging Research. (Image: Shutterstock)

Scientists Identify ‘Clean-Up’ Snafu That Kills Brain Cells in Parkinson’s Disease

Researchers at Albert Einstein College of Medicine of Yeshiva University have discovered how the most common genetic mutations in familial Parkinson’s disease damage brain cells. The study, which published online in the journal Nature Neuroscience, could also open up treatment possibilities for both familial Parkinson’s and the more common form of Parkinson’s that is not inherited.

"Our study found that abnormal forms of LRRK2 protein disrupt an important garbage-disposal process in cells that normally digests and recycles unwanted proteins including one called alpha-synuclein - the main component of those protein aggregates that gunk up nerve cells in Parkinson’s patients," said study leader Ana Maria Cuervo, M.D., Ph.D., professor of  developmental and molecular biology, of anatomy and structural biology, and of medicine and the Robert and Renee Belfer Chair for the Study of Neurodegenerative Diseases at Einstein.

The name for the disrupted disposal process is chaperone-mediated autophagy (the word “autophagy” literally means “self-eating”). It involves specialized molecules that “guide” old and damaged proteins to enzyme-filled structures called lysosomes; there the proteins are digested into amino acids, which are then recycled within the cell.

"We showed that when LRRK2 inhibits chaperone-mediated autophagy,
alpha-synuclein doesn’t get broken down and instead accumulates to toxic levels in nerve cells,” said Dr. Cuervo.

The study involved mouse neurons in tissue culture from four different animal models, neurons from the brains of patients with Parkinson’s with  LRRK2 mutations, and neurons derived from the skin cells of Parkinson’s patients via induced pluripotent stem (iPS) cell technology. All the lines of research confirmed the researchers’ discovery.

"We’re now looking at ways to enhance the activity of this recycling system to see if we can prevent or delay neuronal death and disease," said Dr. Cuervo. "We’ve started to analyze some chemical compounds that look very promising."

Dr. Cuervo hopes that such treatments could help patients with familial as well as nonfamilial Parkinson’s - the predominant form of the disease that also involves the buildup of alpha-synuclein.

Dr. Cuervo is credited with discovering chaperone-mediated autophagy. She has published extensively on autophagy and its role in numerous diseases, such as cancer and Huntington’s disease, and its role in age-related conditions, including organ decline and weakened immunity. Dr. Cuervo is co-director of Einstein’s  Institute of Aging Research.

(Image: Shutterstock)

Filed under neurodegenerative diseases parkinson's disease autophagy nerve cells proteins neuroscience science

459 notes

Clever Battery Completes Stretchable Electronics Package Northwestern University’s Yonggang Huang and the University of Illinois’ John A. Rogers are the first to demonstrate a stretchable lithium-ion battery — a flexible device capable of powering their innovative stretchable electronics. No longer needing to be connected by a cord to an electrical outlet, the stretchable electronic devices now could be used anywhere, including inside the human body. The implantable electronics could monitor anything from brain waves to heart activity, succeeding where flat, rigid batteries would fail. Huang and Rogers have demonstrated a battery that continues to work — powering a commercial light-emitting diode (LED) — even when stretched, folded, twisted and mounted on a human elbow. The battery can work for eight to nine hours before it needs recharging, which can be done wirelessly. The new battery enables true integration of electronics and power into a small, stretchable package. Details are published by the online journal Nature Communications. “We start with a lot of battery components side by side in a very small space, and we connect them with tightly packed, long wavy lines,” said Huang, a corresponding author of the paper. “These wires provide the flexibility. When we stretch the battery, the wavy interconnecting lines unfurl, much like yarn unspooling. And we can stretch the device a great deal and still have a working battery.” Huang led the portion of the research focused on theory, design and modeling. He is the Joseph Cummings Professor of Civil and Environmental Engineering and Mechanical Engineering at Northwestern’s McCormick School of Engineering and Applied Science. The power and voltage of the stretchable battery are similar to a conventional lithium-ion battery of the same size, but the flexible battery can stretch up to 300 percent of its original size and still function.

Clever Battery Completes Stretchable Electronics Package

Northwestern University’s Yonggang Huang and the University of Illinois’ John A. Rogers are the first to demonstrate a stretchable lithium-ion battery — a flexible device capable of powering their innovative stretchable electronics.

No longer needing to be connected by a cord to an electrical outlet, the stretchable electronic devices now could be used anywhere, including inside the human body. The implantable electronics could monitor anything from brain waves to heart activity, succeeding where flat, rigid batteries would fail.

Huang and Rogers have demonstrated a battery that continues to work — powering a commercial light-emitting diode (LED) — even when stretched, folded, twisted and mounted on a human elbow. The battery can work for eight to nine hours before it needs recharging, which can be done wirelessly.

The new battery enables true integration of electronics and power into a small, stretchable package. Details are published by the online journal Nature Communications.

“We start with a lot of battery components side by side in a very small space, and we connect them with tightly packed, long wavy lines,” said Huang, a corresponding author of the paper. “These wires provide the flexibility. When we stretch the battery, the wavy interconnecting lines unfurl, much like yarn unspooling. And we can stretch the device a great deal and still have a working battery.”

Huang led the portion of the research focused on theory, design and modeling. He is the Joseph Cummings Professor of Civil and Environmental Engineering and Mechanical Engineering at Northwestern’s McCormick School of Engineering and Applied Science.

The power and voltage of the stretchable battery are similar to a conventional lithium-ion battery of the same size, but the flexible battery can stretch up to 300 percent of its original size and still function.

Filed under battery stretchable battery BCI implantable electronics implants technology science

96 notes

“Seq-ing” Insights into the Epigenetics of Neuronal Gene Regulation The epigenetic control of neuronal gene expression patterns has emerged as an underlying regulatory mechanism for neuronal function, identity, and plasticity, in which short- to long-lasting adaptation is required to dynamically respond and process external stimuli. To achieve a comprehensive understanding of the physiology and pathology of the brain, it becomes essential to understand the mechanisms that regulate the epigenome and transcriptome in neurons. Here, we review recent advances in the study of regulated neuronal gene expression, which are dramatically expanding as a result of the development of new and powerful contemporary methodologies, based on next-generation sequencing. This flood of new information has already transformed our understanding of many biological processes and is now driving discoveries elucidating the molecular mechanisms of brain function in cognition, behavior, and disease and may also inform the study of neuronal identity, diversity, and neuronal reprogramming.

“Seq-ing” Insights into the Epigenetics of Neuronal Gene Regulation

The epigenetic control of neuronal gene expression patterns has emerged as an underlying regulatory mechanism for neuronal function, identity, and plasticity, in which short- to long-lasting adaptation is required to dynamically respond and process external stimuli. To achieve a comprehensive understanding of the physiology and pathology of the brain, it becomes essential to understand the mechanisms that regulate the epigenome and transcriptome in neurons. Here, we review recent advances in the study of regulated neuronal gene expression, which are dramatically expanding as a result of the development of new and powerful contemporary methodologies, based on next-generation sequencing. This flood of new information has already transformed our understanding of many biological processes and is now driving discoveries elucidating the molecular mechanisms of brain function in cognition, behavior, and disease and may also inform the study of neuronal identity, diversity, and neuronal reprogramming.

Filed under epigenetics gene expression deep sequencing neurons neuronal function brain development genetics neuroscience science

562 notes

Back in 2004, I was awakened early one morning by a loud clatter. I ran outside, only to discover that a car had smashed into the corner of my house. As I went to speak with the driver, he threw the car into reverse and sped off, striking me and running over my right foot as I fell to the ground. When his car hit me, I was wearing a computerized-vision system I had invented to give me a better view of the world. The impact and fall injured my leg and also broke my wearable computing system, which normally overwrites its memory buffers and doesn’t permanently record images. But as a result of the damage, it retained pictures of the car’s license plate and driver, who was later identified and arrested thanks to this record of the incident. Was it blind luck (pardon the expression) that I was wearing this vision-enhancing system at the time of the accident? Not at all: I have been designing, building, and wearing some form of this gear for more than 35 years. I have found these systems to be enormously empowering. For example, when a car’s headlights shine directly into my eyes at night, I can still make out the driver’s face clearly. That’s because the computerized system combines multiple images taken with different exposures before displaying the results to me. I’ve built dozens of these systems, which improve my vision in multiple ways. Some versions can even take in other spectral bands. If the equipment includes a camera that is sensitive to long-wavelength infrared, for example, I can detect subtle heat signatures, allowing me to see which seats in a lecture hall had just been vacated, or which cars in a parking lot most recently had their engines switched off. Other versions enhance text, making it easy to read signs that would otherwise be too far away to discern or that are printed in languages I don’t know. Believe me, after you’ve used such eyewear for a while, you don’t want to give up all it offers. Wearing it, however, comes with a price. For one, it marks me as a nerd. For another, the early prototypes were hard to take on and off. These versions had an aluminum frame that wrapped tightly around the wearer’s head, requiring special tools to remove. Steve Mann: My “Augmediated” Life - What I’ve learned from 35 years of wearing computerized eyewear

Back in 2004, I was awakened early one morning by a loud clatter. I ran outside, only to discover that a car had smashed into the corner of my house. As I went to speak with the driver, he threw the car into reverse and sped off, striking me and running over my right foot as I fell to the ground. When his car hit me, I was wearing a computerized-vision system I had invented to give me a better view of the world. The impact and fall injured my leg and also broke my wearable computing system, which normally overwrites its memory buffers and doesn’t permanently record images. But as a result of the damage, it retained pictures of the car’s license plate and driver, who was later identified and arrested thanks to this record of the incident.

Was it blind luck (pardon the expression) that I was wearing this vision-enhancing system at the time of the accident? Not at all: I have been designing, building, and wearing some form of this gear for more than 35 years. I have found these systems to be enormously empowering. For example, when a car’s headlights shine directly into my eyes at night, I can still make out the driver’s face clearly. That’s because the computerized system combines multiple images taken with different exposures before displaying the results to me.

I’ve built dozens of these systems, which improve my vision in multiple ways. Some versions can even take in other spectral bands. If the equipment includes a camera that is sensitive to long-wavelength infrared, for example, I can detect subtle heat signatures, allowing me to see which seats in a lecture hall had just been vacated, or which cars in a parking lot most recently had their engines switched off. Other versions enhance text, making it easy to read signs that would otherwise be too far away to discern or that are printed in languages I don’t know.

Believe me, after you’ve used such eyewear for a while, you don’t want to give up all it offers. Wearing it, however, comes with a price. For one, it marks me as a nerd. For another, the early prototypes were hard to take on and off. These versions had an aluminum frame that wrapped tightly around the wearer’s head, requiring special tools to remove.

Steve Mann: My “Augmediated” Life - What I’ve learned from 35 years of wearing computerized eyewear

Filed under vision visual system computerized eyewear augmented reality technology science

2,854 notes

Japan’s Robot Suit Gets Global Safety Certificate A robot suit that can help the elderly or disabled get around was given its global safety certificate in Japan on Wednesday, paving the way for its worldwide rollout. The Hybrid Assistive Limb, or HAL, is a power-assisted pair of legs developed by Japanese robot maker Cyberdyne, which has also developed similar robot arms. A quality assurance body issued the certificate based on a draft version of an international safety standard for personal robots that is expected to be approved later this year, the ministry for the economy, trade and industry said. The metal-and-plastic exoskeleton has become the first nursing-care robot certified under the draft standard, a ministry official said. Battery-powered HAL, which detects muscle impulses to anticipate and support the user’s body movements, is designed to help the elderly with mobility or help hospital or nursing carers to lift patients. Cyberdyne, based in Tsukuba, northeast of Tokyo, has so far leased some 330 suits to 150 hospitals, welfare and other facilities in Japan since 2010, at 178,000 yen ($1,950) per suit per year. "It is very significant that Japan has obtained this certification before others in the world," said Yoshiyuki Sankai, the head of Cyberdyne. The company is unrelated to the firm of the same name responsible for the cyborg assassin played by Arnold Schwarzenegger in the 1984 film “The Terminator”. "This is a first step forward for Japan, the great robot nation, to send our message to the world about robots of the future," said Sankai, who is also a professor at Tsukuba University. A different version of HAL — coincidentally the name of the evil supercomputer in Stanley Kubrick’s “2001: A Space Odyssey” — has been developed for workers who need to wear heavy radiation protection as part of the clean-up at the crippled Fukushima nuclear plant. Industrial robots have long been used in Japan, and robo-suits are gradually making inroads into hospitals and retirement homes. But critics say the government has been slow in creating a safety framework for such robots in a country whose rapidly-ageing population is expected to enjoy ever longer lives.

Japan’s Robot Suit Gets Global Safety Certificate

A robot suit that can help the elderly or disabled get around was given its global safety certificate in Japan on Wednesday, paving the way for its worldwide rollout.

The Hybrid Assistive Limb, or HAL, is a power-assisted pair of legs developed by Japanese robot maker Cyberdyne, which has also developed similar robot arms.

A quality assurance body issued the certificate based on a draft version of an international safety standard for personal robots that is expected to be approved later this year, the ministry for the economy, trade and industry said.

The metal-and-plastic exoskeleton has become the first nursing-care robot certified under the draft standard, a ministry official said.

Battery-powered HAL, which detects muscle impulses to anticipate and support the user’s body movements, is designed to help the elderly with mobility or help hospital or nursing carers to lift patients.

Cyberdyne, based in Tsukuba, northeast of Tokyo, has so far leased some 330 suits to 150 hospitals, welfare and other facilities in Japan since 2010, at 178,000 yen ($1,950) per suit per year.

"It is very significant that Japan has obtained this certification before others in the world," said Yoshiyuki Sankai, the head of Cyberdyne.

The company is unrelated to the firm of the same name responsible for the cyborg assassin played by Arnold Schwarzenegger in the 1984 film “The Terminator”.

"This is a first step forward for Japan, the great robot nation, to send our message to the world about robots of the future," said Sankai, who is also a professor at Tsukuba University.

A different version of HAL — coincidentally the name of the evil supercomputer in Stanley Kubrick’s “2001: A Space Odyssey” — has been developed for workers who need to wear heavy radiation protection as part of the clean-up at the crippled Fukushima nuclear plant.

Industrial robots have long been used in Japan, and robo-suits are gradually making inroads into hospitals and retirement homes.

But critics say the government has been slow in creating a safety framework for such robots in a country whose rapidly-ageing population is expected to enjoy ever longer lives.

Filed under robots robotics HAL robot suit HAL rehabilitation science

262 notes

Reconstructing the Past: How Recalling Memories Alters Them Recently the neurologist and author Oliver Sacks recalled a vivid childhood memory, recounted in his autobiography, Uncle Tungsten. During WWII he lived in London during the Blitz, and on one occasion: "…an incendiary bomb, a thermite bomb, fell behind our house and burned with a terrible, white-hot heat. My father had a stirrup pump, and my brothers carried pails of water to him, but water seemed useless against this infernal fire—indeed, made it burn even more furiously. There was a vicious hissing and sputtering when the water hit the white-hot metal, and meanwhile the bomb was melting its own casing and throwing blobs and jets of molten metal in all directions." Except when his autobiography came out, one of his older brothers told him he’d misremembered the event. In fact both of them had been at school when the bomb struck so they could not have witnessed the explosion. The ‘false’ memory, it turned out, was implanted by a letter. Their elder brother had written to them, describing the frightening event, and this had lodged in his mind. Over the years the letter had gone from a third-person report to a first-person ‘memory’. Turning the memory over in his mind, Sacks writes that he still cannot see how the memory of the bomb exploding can be false. There is no difference between this memory and others he knows to be true; it felt like he was really there. This sort of experience is probably much more common than we might like to imagine. Many memories which have the scent of authenticity may turn out to be misremembered, if not totally fictitious events, if only we could check. Without some other source with which to corroborate, it is hard verify the facts, especially for events that took place long ago. That these sorts of distortions to memory happen is unquestioned, what fascinates is how it comes about. Does the long passage of time warp the memory, or is there some more active process that causes the change? A study published recently sheds some light on this process and provides a model for how memories like Sack’s become distorted.

Reconstructing the Past: How Recalling Memories Alters Them

Recently the neurologist and author Oliver Sacks recalled a vivid childhood memory, recounted in his autobiography, Uncle Tungsten.

During WWII he lived in London during the Blitz, and on one occasion:

"…an incendiary bomb, a thermite bomb, fell behind our house and burned with a terrible, white-hot heat. My father had a stirrup pump, and my brothers carried pails of water to him, but water seemed useless against this infernal fire—indeed, made it burn even more furiously. There was a vicious hissing and sputtering when the water hit the white-hot metal, and meanwhile the bomb was melting its own casing and throwing blobs and jets of molten metal in all directions."

Except when his autobiography came out, one of his older brothers told him he’d misremembered the event. In fact both of them had been at school when the bomb struck so they could not have witnessed the explosion.

The ‘false’ memory, it turned out, was implanted by a letter. Their elder brother had written to them, describing the frightening event, and this had lodged in his mind. Over the years the letter had gone from a third-person report to a first-person ‘memory’.

Turning the memory over in his mind, Sacks writes that he still cannot see how the memory of the bomb exploding can be false. There is no difference between this memory and others he knows to be true; it felt like he was really there.

This sort of experience is probably much more common than we might like to imagine. Many memories which have the scent of authenticity may turn out to be misremembered, if not totally fictitious events, if only we could check. Without some other source with which to corroborate, it is hard verify the facts, especially for events that took place long ago.

That these sorts of distortions to memory happen is unquestioned, what fascinates is how it comes about. Does the long passage of time warp the memory, or is there some more active process that causes the change?

A study published recently sheds some light on this process and provides a model for how memories like Sack’s become distorted.

Filed under memory false memory episodic memory autobiographical memory psychology neuroscience science

104 notes

Every science writer loves a good challenge to dogma. I wish I had been in the working world in the spring of 1992, when one such intellectual overhaul happened in neuroscience. The dogma: Neurons, unlike most of the body’s cells, can’t be replenished. You’re born with just 100 billion of them and you better use them wisely. The challenge: Samuel Weiss and Brent Reynolds reported in Science that brain tissue taken from adult mice could be chemically coaxed into making new neurons. “It left us speechless,” Weiss told the New York Times. Everybody else was pretty stunned, too. Over the next six years, other researchers confirmed that this so-called neurogenesis happens in the adult hippocampus of many animals, including tree shrews, marmosets, Old World monkeys and people. Today, more than two decades since the splashy Science report, adult neurogenesis is a bona fide subfield, with hundreds of labs studying it around the world. But after all this time, researchers still don’t really know what it’s for. Studies have uncovered a wide variety of environmental stimuli — what you might think of as inputs — that affect neurogenesis in the dentate gyrus, a part of the hippocampus. Running and antidepressants can ramp up neurogenesis, for example, while stress, social isolation, sleep deprivation and aging can shut it down. Scientists have also looked at the outputs of neurogenesis, showing that a boost of new neurons may be important for exploratory behavior and certain kinds of learning, such as navigating a new space. But how do the inputs lead to the outputs? “I like to think of the dentate as an association machine,” says Sam Pleasure, a neuroscientist at the University of California, San Francisco. All day long, he says, we’re walking around the world trying to associate various sensations and emotions — big dog with fangs, small screaming toddler, perilous traffic intersection — so that we can remember them later. “All these stimuli are happening and converge on this circuit, and they somehow affect how new neurons are recruited into the circuit, and that ends up coming out as the ability to form new memories.” But how it all works on the molecular level is a black box. Two papers published in Cell Stem Cell [1 , 2]open that box a little bit. They identify molecular inhibitors — what Pleasure calls “wet blankets” — that turn off neurogenesis in certain contexts. Opening the Black Box of Neurogenesis by Virginia Hughes

Every science writer loves a good challenge to dogma. I wish I had been in the working world in the spring of 1992, when one such intellectual overhaul happened in neuroscience. The dogma: Neurons, unlike most of the body’s cells, can’t be replenished. You’re born with just 100 billion of them and you better use them wisely. The challenge: Samuel Weiss and Brent Reynolds reported in Science that brain tissue taken from adult mice could be chemically coaxed into making new neurons.

“It left us speechless,” Weiss told the New York Times. Everybody else was pretty stunned, too. Over the next six years, other researchers confirmed that this so-called neurogenesis happens in the adult hippocampus of many animals, including tree shrews, marmosets, Old World monkeys and people. Today, more than two decades since the splashy Science report, adult neurogenesis is a bona fide subfield, with hundreds of labs studying it around the world.

But after all this time, researchers still don’t really know what it’s for. Studies have uncovered a wide variety of environmental stimuli — what you might think of as inputs — that affect neurogenesis in the dentate gyrus, a part of the hippocampus. Running and antidepressants can ramp up neurogenesis, for example, while stress, social isolation, sleep deprivation and aging can shut it down. Scientists have also looked at the outputs of neurogenesis, showing that a boost of new neurons may be important for exploratory behavior and certain kinds of learning, such as navigating a new space. But how do the inputs lead to the outputs?

“I like to think of the dentate as an association machine,” says Sam Pleasure, a neuroscientist at the University of California, San Francisco. All day long, he says, we’re walking around the world trying to associate various sensations and emotions — big dog with fangs, small screaming toddler, perilous traffic intersection — so that we can remember them later. “All these stimuli are happening and converge on this circuit, and they somehow affect how new neurons are recruited into the circuit, and that ends up coming out as the ability to form new memories.” But how it all works on the molecular level is a black box.

Two papers published in Cell Stem Cell [1 , 2]open that box a little bit. They identify molecular inhibitors — what Pleasure calls “wet blankets” — that turn off neurogenesis in certain contexts.

Opening the Black Box of Neurogenesis by Virginia Hughes

Filed under neurons neurogenesis hippocampus dentate gyrus neuroscience science

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