Led by Senior Research Scientist Silvia Sanchez-Martinez in the lab of UW Department of Molecular Biology Assistant Professor Thomas Boothby, the research study supplies extra proof that tardigrade proteins ultimately could be utilized to make life-saving treatments offered to individuals where refrigeration is not possible– and improve storage of cell-based therapies, such as stem cells.Measuring less than half a millimeter long, tardigrades– likewise understood as water bears– can make it through being entirely dried out; being frozen to simply above outright no (about minus 458 degrees Fahrenheit, when all molecular motion stops); warmed to more than 300 degrees Fahrenheit; irradiated several thousand times beyond what a human might stand up to; and even make it through the vacuum of external space.University of Wyoming Senior Research Scientist Silvia Sanchez-Martinez, left, and Department of Molecular Biology Assistant Professor Thomas Boothby led new research study offering extra proof that tardigrade proteins eventually could be used to make life-saving treatments offered to people where refrigeration is not possible. “Furthermore, simply like tardigrades, when you put human cells that have these proteins into biostasis, they end up being more resistant to stresses, conferring some of the tardigrades capabilities to the human cells.”Our findings supply an avenue for pursuing technologies focused on the induction of biostasis in cells and even whole organisms to slow aging and boost storage and stability,” the researchers concluded.Previous research by Boothbys team showed that natural and engineered variations of tardigrade proteins can be utilized to support an essential pharmaceutical used to treat people with hemophilia and other conditions without the need for refrigeration.Tardigrades ability to make it through being dried out has actually puzzled scientists, as the creatures do so in a manner that appears to vary from a number of other organisms with the ability to get in suspended animation.Reference: “Labile assembly of a tardigrade protein causes biostasis” by S. Sanchez-Martinez, K. Nguyen, S. Biswas, V. Nicholson, A. V. Romanyuk, J. Ramirez, S. Kc, A. Akter, C. Childs, E. K. Meese, E. T. Usher, G. M. Ginell, F. Yu, E. Gollub, M. Malferrari, F. Francia, G. Venturoli, E. W. Martin, F. Caporaletti, G. Giubertoni, S. Woutersen, S. Sukenik, D. N. Woolfson, A. S. Holehouse and T. C. Boothby, 19 March 2024, Protein Science.DOI: 10.1002/ professional.4941 The research was funded by the National Institutes of Health, the NASA Astrobiology Institute, and the U.S. National Science Foundation.
