Latest news with #proteins
Daily Mail
11-07-2025
- Health
- Daily Mail
Bombshell Alzheimer's breakthrough that's set to be a huge gamechanger in curing the disease
Scientists have uncovered a new group of rogue proteins in the brain that could play a major role in triggering and worsening Alzheimer's disease. Until now, researchers believed that clumps of amyloid and tau proteins were the main culprits behind the devastating cognitive decline seen in Alzheimer's patients. Your browser does not support iframes.
Reuters
10-07-2025
- Science
- Reuters
Ancient proteins found in fossils up to 24 million years old
WASHINGTON, July 9 (Reuters) - Scientists in recent years have made progress in finding ancient DNA in fossils, gaining insight into organisms that lived long ago. But the oldest DNA obtained so far dates back about two million years. Proteins, a cell's molecular machinery, also offer valuable information and have the virtue of surviving much longer, as new research shows. Scientists have now extracted and sequenced proteins from dental fossils of extinct rhinoceroses, elephants and hippopotamuses, including from a rhino tooth 21-24 million years old. Separate research teams found protein fragments in fossils from vastly different environments - the frigid High Arctic of Canada and a scorching rift valley in Kenya. "Together, these complementary projects demonstrate that proteins - fundamental building blocks of living organisms that preserve information about evolutionary history - can be found in ancient fossils the world over," said Harvard University evolutionary biologist Daniel Green, lead author of the Kenya fossils study published in the journal Nature, opens new tab. This opens a new frontier for probing the deep evolutionary past, including the human lineage and perhaps even dinosaurs. "Ancient proteins can tell us about an organism's evolutionary history by providing molecular data from specimens too old for DNA preservation. This allows researchers to clarify evolutionary relationships across the tree of life, even for species that went extinct millions of years ago," said Ryan Sinclair Paterson, a postdoctoral researcher at the University of Copenhagen's Globe Institute and lead author of the Canada fossil study in Nature, opens new tab. DNA and proteins are fragile and degrade over time, but proteins are more resilient. The oldest-known DNA is from organisms that lived in Greenland two million years ago. Until now, the oldest-known proteins preserved well enough to offer insight on evolutionary relationships were about four million years old, from the Canadian Arctic. The new research pushes the boundaries of ancient protein research, a field called paleoproteomics, back by millions of years. Proteins were obtained from teeth of five rhino, elephant and hippo species that lived 1.5–18 million years ago in Kenya's Turkana region. The proteins showed the ties between the ancient animals and their modern-day relatives. Proteins also were extracted from a fragment of a tooth of an extinct rhino unearthed at a site called Haughton Crater in Nunavut, Canada's northernmost territory, that was up to 24 million years old. They showed how this species fit into the rhino family tree. Haughton Crater's cold and dry conditions were considered ideal for preserving proteins. Preservation in the hot climate of Turkana was more unexpected. DNA and proteins, fundamental molecules in biology, possess distinct structures and functions. Deoxyribonucleic acid is the blueprint for life, bearing instructions for an organism's development, growth and reproduction. Proteins perform numerous functions based on instructions from DNA. "Proteins are encoded by our genetic code, DNA, so protein sequences reveal information about relatedness between different individuals, and biological sex, among other things," Green said. The scientists extracted peptides - chains of organic compounds called amino acids that combine to form proteins - found inside tooth enamel. "Some proteins help build teeth, the hardest and most durable structures in animal bodies," Green added. "Enamel is mostly rock: a mineral called hydroxyapatite. But its formation is biologically mediated by proteins that guide both shape and hardness over time. Because these proteins become entombed deep within enamel mineral, we have some reason to expect that protein fragments can be preserved over many millions of years," Green said. Homo sapiens appeared about 300,000 years ago. Ancient proteins previously have been found in the teeth of some extinct species in the human evolutionary lineage, called hominins. The Turkana region has yielded important hominin fossils. "Hominins have evolutionary origins and/or diversification in the area where our samples derive, so our results have promise in future exploration of the enamel proteome (set of proteins) of our evolutionary ancestors from the Turkana Basin of Kenya," said study co-author Timothy Cleland, a physical scientist at the Smithsonian Museum Conservation Institute in Maryland. The proteins studied came from large-bodied species dating to the age of mammals that followed the demise of the dinosaurs that had dominated during the preceding Mesozoic era, which ended 66 million years ago. Green said that in the new research the number of detectable proteins declined in progressively older fossils. But Green did not rule out finding proteins dating to the age of dinosaurs, saying, "Newer and better methods for extracting and detecting ancient proteins could, perhaps, push paleoproteomics into the Mesozoic."
Yahoo
09-07-2025
- Science
- Yahoo
Ancient proteins found in fossils up to 24 million years old
By Will Dunham WASHINGTON (Reuters) -Scientists in recent years have made progress in finding ancient DNA in fossils, gaining insight into organisms that lived long ago. But the oldest DNA obtained so far dates back about two million years. Proteins, a cell's molecular machinery, also offer valuable information and have the virtue of surviving much longer, as new research shows. Scientists have now extracted and sequenced proteins from dental fossils of extinct rhinoceroses, elephants and hippopotamuses, including from a rhino tooth 21-24 million years old. Separate research teams found protein fragments in fossils from vastly different environments - the frigid High Arctic of Canada and a scorching rift valley in Kenya. "Together, these complementary projects demonstrate that proteins - fundamental building blocks of living organisms that preserve information about evolutionary history - can be found in ancient fossils the world over," said Harvard University evolutionary biologist Daniel Green, lead author of the Kenya fossils study published in the journal Nature. This opens a new frontier for probing the deep evolutionary past, including the human lineage and perhaps even dinosaurs. "Ancient proteins can tell us about an organism's evolutionary history by providing molecular data from specimens too old for DNA preservation. This allows researchers to clarify evolutionary relationships across the tree of life, even for species that went extinct millions of years ago," said Ryan Sinclair Paterson, a postdoctoral researcher at the University of Copenhagen's Globe Institute and lead author of the Canada fossil study in Nature. DNA and proteins are fragile and degrade over time, but proteins are more resilient. The oldest-known DNA is from organisms that lived in Greenland two million years ago. Until now, the oldest-known proteins preserved well enough to offer insight on evolutionary relationships were about four million years old, from the Canadian Arctic. The new research pushes the boundaries of ancient protein research, a field called paleoproteomics, back by millions of years. Proteins were obtained from teeth of five rhino, elephant and hippo species that lived 1.5–18 million years ago in Kenya's Turkana region. The proteins showed the ties between the ancient animals and their modern-day relatives. Proteins also were extracted from a fragment of a tooth of an extinct rhino unearthed at a site called Haughton Crater in Nunavut, Canada's northernmost territory, that was up to 24 million years old. They showed how this species fit into the rhino family tree. Haughton Crater's cold and dry conditions were considered ideal for preserving proteins. Preservation in the hot climate of Turkana was more unexpected. DNA and proteins, fundamental molecules in biology, possess distinct structures and functions. Deoxyribonucleic acid is the blueprint for life, bearing instructions for an organism's development, growth and reproduction. Proteins perform numerous functions based on instructions from DNA. "Proteins are encoded by our genetic code, DNA, so protein sequences reveal information about relatedness between different individuals, and biological sex, among other things," Green said. The scientists extracted peptides - chains of organic compounds called amino acids that combine to form proteins - found inside tooth enamel. "Some proteins help build teeth, the hardest and most durable structures in animal bodies," Green added. "Enamel is mostly rock: a mineral called hydroxyapatite. But its formation is biologically mediated by proteins that guide both shape and hardness over time. Because these proteins become entombed deep within enamel mineral, we have some reason to expect that protein fragments can be preserved over many millions of years," Green said. Homo sapiens appeared about 300,000 years ago. Ancient proteins previously have been found in the teeth of some extinct species in the human evolutionary lineage, called hominins. The Turkana region has yielded important hominin fossils. "Hominins have evolutionary origins and/or diversification in the area where our samples derive, so our results have promise in future exploration of the enamel proteome (set of proteins) of our evolutionary ancestors from the Turkana Basin of Kenya," said study co-author Timothy Cleland, a physical scientist at the Smithsonian Museum Conservation Institute in Maryland. The proteins studied came from large-bodied species dating to the age of mammals that followed the demise of the dinosaurs that had dominated during the preceding Mesozoic era, which ended 66 million years ago. Green said that in the new research the number of detectable proteins declined in progressively older fossils. But Green did not rule out finding proteins dating to the age of dinosaurs, saying, "Newer and better methods for extracting and detecting ancient proteins could, perhaps, push paleoproteomics into the Mesozoic."
CNA
09-07-2025
- Science
- CNA
Ancient proteins found in fossils up to 24 million years old
WASHINGTON :Scientists in recent years have made progress in finding ancient DNA in fossils, gaining insight into organisms that lived long ago. But the oldest DNA obtained so far dates back about two million years. Proteins, a cell's molecular machinery, also offer valuable information and have the virtue of surviving much longer, as new research shows. Scientists have now extracted and sequenced proteins from dental fossils of extinct rhinoceroses, elephants and hippopotamuses, including from a rhino tooth 21-24 million years old. Separate research teams found protein fragments in fossils from vastly different environments - the frigid High Arctic of Canada and a scorching rift valley in Kenya. "Together, these complementary projects demonstrate that proteins - fundamental building blocks of living organisms that preserve information about evolutionary history - can be found in ancient fossils the world over," said Harvard University evolutionary biologist Daniel Green, lead author of the Kenya fossils study published in the journal Nature. This opens a new frontier for probing the deep evolutionary past, including the human lineage and perhaps even dinosaurs. "Ancient proteins can tell us about an organism's evolutionary history by providing molecular data from specimens too old for DNA preservation. This allows researchers to clarify evolutionary relationships across the tree of life, even for species that went extinct millions of years ago," said Ryan Sinclair Paterson, a postdoctoral researcher at the University of Copenhagen's Globe Institute and lead author of the Canada fossil study in Nature. DNA and proteins are fragile and degrade over time, but proteins are more resilient. The oldest-known DNA is from organisms that lived in Greenland two million years ago. Until now, the oldest-known proteins preserved well enough to offer insight on evolutionary relationships were about four million years old, from the Canadian Arctic. The new research pushes the boundaries of ancient protein research, a field called paleoproteomics, back by millions of years. Proteins were obtained from teeth of five rhino, elephant and hippo species that lived 1.5–18 million years ago in Kenya's Turkana region. The proteins showed the ties between the ancient animals and their modern-day relatives. Proteins also were extracted from a fragment of a tooth of an extinct rhino unearthed at a site called Haughton Crater in Nunavut, Canada's northernmost territory, that was up to 24 million years old. They showed how this species fit into the rhino family tree. Haughton Crater's cold and dry conditions were considered ideal for preserving proteins. Preservation in the hot climate of Turkana was more unexpected. DNA and proteins, fundamental molecules in biology, possess distinct structures and functions. Deoxyribonucleic acid is the blueprint for life, bearing instructions for an organism's development, growth and reproduction. Proteins perform numerous functions based on instructions from DNA. "Proteins are encoded by our genetic code, DNA, so protein sequences reveal information about relatedness between different individuals, and biological sex, among other things," Green said. The scientists extracted peptides - chains of organic compounds called amino acids that combine to form proteins - found inside tooth enamel. "Some proteins help build teeth, the hardest and most durable structures in animal bodies," Green added. "Enamel is mostly rock: a mineral called hydroxyapatite. But its formation is biologically mediated by proteins that guide both shape and hardness over time. Because these proteins become entombed deep within enamel mineral, we have some reason to expect that protein fragments can be preserved over many millions of years," Green said. Homo sapiens appeared about 300,000 years ago. Ancient proteins previously have been found in the teeth of some extinct species in the human evolutionary lineage, called hominins. The Turkana region has yielded important hominin fossils. "Hominins have evolutionary origins and/or diversification in the area where our samples derive, so our results have promise in future exploration of the enamel proteome (set of proteins) of our evolutionary ancestors from the Turkana Basin of Kenya," said study co-author Timothy Cleland, a physical scientist at the Smithsonian Museum Conservation Institute in Maryland. The proteins studied came from large-bodied species dating to the age of mammals that followed the demise of the dinosaurs that had dominated during the preceding Mesozoic era, which ended 66 million years ago. Green said that in the new research the number of detectable proteins declined in progressively older fossils. But Green did not rule out finding proteins dating to the age of dinosaurs, saying, "Newer and better methods for extracting and detecting ancient proteins could, perhaps, push paleoproteomics into the Mesozoic."
WIRED
06-07-2025
- Health
- WIRED
How the Binding of Two Brain Molecules Creates Memories That Last a Lifetime
Jul 6, 2025 2:00 AM An interaction between two proteins points to a molecular basis for memory. But how do memories last when the molecules that form them turn over within days, weeks, or months? Illustration: Carlos Arrojo for Quanta Magazine The original version of this story appeared in Quanta Magazine . When Todd Sacktor was about to turn 3, his 4-year-old sister died of leukemia. 'An empty bedroom next to mine. A swing set with two seats instead of one,' he said, recalling the lingering traces of her presence in the house. 'There was this missing person—never spoken of—for which I had only one memory.' That memory, faint but enduring, was set in the downstairs den of their home. A young Sacktor asked his sister to read him a book, and she brushed him off: 'Go ask your mother.' Sacktor glumly trudged up the stairs to the kitchen. It's remarkable that, more than 60 years later, Sacktor remembers this fleeting childhood moment at all. The astonishing nature of memory is that every recollection is a physical trace, imprinted into brain tissue by the molecular machinery of neurons. How the essence of a lived moment is encoded and later retrieved remains one of the central unanswered questions in neuroscience. Sacktor became a neuroscientist in pursuit of an answer. At the State University of New York Downstate in Brooklyn, he studies the molecules involved in maintaining the neuronal connections underlying memory. The question that has always held his attention was first articulated in 1984 by the famed biologist Francis Crick: How can memories persist for years, even decades, when the body's molecules degrade and are replaced in a matter of days, weeks or, at most, months? In 2024, working alongside a team that included his longtime collaborator André Fenton, a neuroscientist at New York University, Sacktor offered a potential explanation in a paper published in Science Advances . The researchers discovered that a persistent bond between two proteins is associated with the strengthening of synapses, which are the connections between neurons. Synaptic strengthening is thought to be fundamental to memory formation. As these proteins degrade, new ones take their place in a connected molecular swap that maintains the bond's integrity and, therefore, the memory. In 1984, Francis Crick described a biological conundrum: Memories last years, while most molecules degrade in days or weeks. 'How then is memory stored in the brain so that its trace is relatively immune to molecular turnover?' he wrote in Nature. Photograph: National Library of Medicine/Science Source The researchers present 'a very convincing case' that 'the interaction between these two molecules is needed for memory storage,' said Karl Peter Giese, a neurobiologist at King's College London who was not involved with the work. The findings offer a compelling response to Crick's dilemma, reconciling the discordant timescales to explain how ephemeral molecules maintain memories that last a lifetime. Molecular Memory Early in his career, Sacktor made a discovery that would shape the rest of his life. After studying under the molecular memory pioneer James Schwartz at Columbia University, he opened his own lab at SUNY Downstate to search for a molecule that might help explain how long-term memories persist. The molecule he was looking for would be in the brain's synapses. In 1949, the psychologist Donald Hebb proposed that repeatedly activating neurons strengthens the connections between them, or, as the neurobiologist Carla Shatz later put it: 'Cells that fire together, wire together.' In the decades since, many studies have suggested that the stronger the connection between neurons that hold memories, the better the memories persist. In the early 1990s, in a dish in his lab, Sacktor stimulated a slice of a rat's hippocampus—a small region of the brain linked to memories of events and places, such as the interaction Sacktor had with his sister in the den—to activate neural pathways in a way that mimicked memory encoding and storage. Then he searched for any molecular changes that had taken place. Every time he repeated the experiment, he saw elevated levels of a certain protein within the synapses. 'By the fourth time, I was like, this is it,' he said. It was protein kinase M zeta, or PKMζ for short. As the rats' hippocampal tissue was stimulated, synaptic connections strengthened and levels of PKMζ increased. By the time he published his findings in 1993, he was convinced that PKMζ was crucial for memory. Todd Sacktor has devoted his career to pursuing the molecular nature of memory. Photograph: SUNY Downstate Health Sciences University Over the next two decades, he would go on to build a body of work showing that PKMζ's presence helps maintain memories long after their initial formation. When Sacktor blocked the molecule's activity an hour after a memory was formed, he saw that synaptic strengthening was reversed. This discovery suggested that PKMζ was 'necessary and sufficient' to preserve a memory over time, he wrote in Nature Neuroscience in 2002. In contrast, hundreds of other localized molecules impacted synaptic strengthening only if disrupted within a few minutes of a memory's formation. It appeared to be a singular molecular key to long-term memory. To test his hypothesis in live animals, he teamed up with Fenton, who worked at SUNY Downstate at the time and had experience training lab animals and running behavioral experiments. In 2006, the duo published their first paper showing that blocking PKMζ could erase rats' memories a day or a month after they had formed. This suggested that the persistent activity of PKMζ is required to maintain a memory. The paper was a bombshell. Sacktor and Fenton's star protein PKMζ gained widespread attention, and labs around the world found that blocking it could erase various types of memories, including those related to fear and taste. PKMζ seemed like a sweeping explanation for how memories form and are maintained at the molecular level. But then their hypothesis lost momentum. Other researchers genetically engineered mice to lack PKMζ, and in 2013, two independent studies showed that these mice could still form memories. This cast doubt on the protein's role and brought much of the ongoing research to a halt. Sacktor and Fenton were undeterred. 'We knew we had to figure it out,' Sacktor said. In 2016, they published a rebuttal, demonstrating that in the absence of PKMζ, mice recruit a backup mechanism, involving another molecule, to strengthen synapses. The existence of a compensatory molecule wasn't a surprise. 'The biological system is not such that you lose one molecule and everything goes. That's very rare,' Giese said. But identifying this compensatory molecule prompted a new question: How did it know where to go to replace PKMζ? It would take Sacktor and Fenton nearly another decade to find out. The Maintenance Bond A classic test of a molecule's importance is to block it and see what breaks. Determined to pin down PKMζ's role once and for all, Sacktor and Fenton set out to design a way to disrupt it more precisely than ever before. They developed a new molecule to inhibit the activity of PKMζ. It 'worked beautifully,' Sacktor said. But it wasn't clear how. One day in 2020, Matteo Bernabo, a graduate student from a collaborating lab at McGill University, was presenting findings related to the PKMζ inhibitor when a clue emerged from the audience. 'I suggested that it worked by blocking the PKMζ's interaction with KIBRA,' recalled Wayne Sossin, a neuroscientist at McGill. KIBRA is a scaffolding protein. Like an anchor, it holds other proteins in place inside a synapse. In the brain, it is abundant in regions associated with learning and memory. 'It's not a protein that a lot of people work on,' Sossin said, but there is considerable 'independent evidence that KIBRA has something to do with memory'—and even that it is associated with PKMζ. Most research has focused on KIBRA's role in cancer. 'In the nervous system,' he said, 'there are only three or four of us [studying it].' Sacktor and Fenton joined them. André Fenton and his team found that an interaction between two proteins is key to keeping memory intact over time. Photograph: Lisa Robinson To find out if KIBRA and PKMζ work together in response to synaptic activity, the researchers used a technique that makes interacting proteins glow. When they applied electrical pulses to hippocampal slices, glowing dots of evidence appeared: Following bursts of synaptic activity that produced long-term synaptic strengthening, a multitude of KIBRA-PKMζ complexes formed, and they were persistent. Then the team tested the bond during real memory formation by giving mice a drug to disrupt the formation of these complexes. They saw that the mice's synaptic strength and task memory were lost—and that once the drug wore off, the erased memory did not return, but the mice could acquire and remember new memories once again. But are the KIBRA-PKMζ complexes needed to maintain memory over the long term? To find out, the researchers disrupted the complex four weeks after a memory was formed. Doing so did indeed wipe out the memory. This suggested that the interaction between KIBRA and PKMζ is crucial not only for forming memories, but also for keeping them intact over time. Illustration: Carlos Arrojo for Quanta Magazine 'It's the persistent association between two proteins that maintains the memory, rather than a protein that lasts by itself for the lifetime of the memory,' said Panayiotis Tsokas, a neuroscientist working with Sacktor and lead author on the new Science Advances paper. The KIBRA and PKMζ proteins stabilize each other by forming a bond. That way, when a protein degrades and needs to be replaced, the other remains in place. The bond itself and its location at the specific synapses that were activated during learning are preserved, allowing a new partner to slot itself in, perpetuating the alliance over time. Individually, PKMζ and KIBRA don't last a lifetime—but by binding to each other, they help ensure your memories might. The discovery addresses the conundrum first identified by Crick, namely how memories persist despite the relatively short lifetimes of all biological molecules. 'There had to be a very, very interesting answer, an elegant answer, for how this could come about,' Fenton said. 'And that elegant answer is the KIBRA-PKMζ interacting story.' This work also answers a question that researchers had put on the shelf. Sacktor's earlier study showed that increasing levels of PKMζ strengthened synapses and memories. But how did the molecule know where to go within the neuron? 'We figured, well, one day, maybe we'll understand that,' Sacktor said. Now, the researchers think that KIBRA acts as a synaptic tag that guides PKMζ. If true, this would help explain how only the specific synapses involved in a particular physical memory trace are strengthened, when a neuron may have thousands of synapses that connect it to various other cells. 'These experiments very nicely show that KIBRA is necessary for maintaining the activity of PKMζ at the synapse,' said David Glanzman, a neurobiologist at the University of California, Los Angeles, who was not involved in the study. However, he cautioned that this doesn't necessarily translate to maintaining memory because synaptic strengthening is not the only model for how memory works. Glanzman's own past research on sea slugs at first appeared to show that disrupting a molecule analogous to PKMζ erases memory. 'Originally, I said it was erased,' Glanzman said, 'but later experiments showed we could bring the memory back.' These findings prompted him to reconsider whether memory is truly stored as changes in the strength of synaptic connections. Glanzman, who has worked for 40 years under the synaptic model, is a recent proponent of an alternative view called the molecular-encoding model, which posits that molecules inside a neuron store memories. While he has no doubt that synaptic strengthening follows memory formation, and that PKMζ plays a major role in this process, he remains unsure if the molecule also stores the memory itself. Still, Glanzman emphasized that this study addresses some of the challenges of the synaptic model, such as molecular turnover and synapse targeting, by 'providing evidence that KIBRA and PKMζ form a complex that is synapse-specific and persists longer than either individual molecule.' Although Sacktor and Fenton believe that this protein pair is fundamental to memory, they know that there may be other factors yet to be discovered that help memories persist. Just as PKMζ led them to KIBRA, the complex might lead them further still. Original story reprinted with permission from Quanta Magazine, an editorially independent publication of the Simons Foundation whose mission is to enhance public understanding of science by covering research developments and trends in mathematics and the physical and life sciences.
