The team focused their research on spinal cord injuries, caused when the spinal cord is damaged by trauma rather than disease. Depending on the severity a spinal injury can lead from pain to full paralysis, with high social and medical care costs. As the spinal cord lacks the ability to regenerate, the potential for patient recovery is severely limited.
"Our research offers the first evidence that the spinal cord meninges, the system of membranes which cover the surface of the brain and the spinal cord, contains stem cells which are capable of self-renewal and proliferation," said lead authors Dr Ilaria Decimo and Dr Francesco Bifari, at the University of Verona.
Following a spinal injury meningeal cells increase in number and migrate to form glial scars and the team believe this process explains part of the mechanism of stem cell activation in central nervous system diseases; a mechanism which could in turn be used for treatments. Dr Decimo's team microdissected samples of spinal cord meninges from adult rats revealing that meningeal cells contain crucial stem cell properties. It is these properties which increase following a spinal cord injury.
"Our research emphasizes the role of meninges cells in the reaction to spinal cord trauma and indicates for the first time that spinal cord meninges harbour stem cells which are activated by injury," concluded Dr, Decimo. "Further testing could result in a strategic turnaround for advancing regenerative medicine for treating neurological disorders and spinal cord injuries."
"This study underlines the importance of endogenous stem cells," said STEM CELLS Editor Dr Miodrag Stojkovic. "Identification of these cells is crucial for understanding the basic mechanisms of cell biology and tissue repair, but also to identify drugs and chemicals which might be used to mobilize meningeal stem cells."
Ben Norman | EurekAlert!
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
Two research teams have succeeded simultaneously in measuring the long-sought Thorium nuclear transition, which enables extremely precise nuclear clocks. TU Wien (Vienna) is part of both teams.
If you want to build the most accurate clock in the world, you need something that "ticks" very fast and extremely precise. In an atomic clock, electrons are...
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