The potential of gene therapy to boost heart muscle function was explored in a recent University of Washington animal study. The findings suggest that it might be possible to use this approach to treat patients whose hearts have been weakened by heart attacks and other heart conditions.
Michael Regnier, UW professor and vice chair of bioengineering, Charles Murry, director of the Center for Cardiovascular Biology and co-director of the Institute for Stem Cell and Regenerative Medicine, and Sarah Nowakowski, a UW graduate student in bioengineering, led the study. The findings appeared online March 25 in the Proceedings of the National Academy of Sciences. (more…)
A study dating the age of more than 1 million single-letter variations in the human DNA code reveals that most of these mutations are of recent origin, evolutionarily speaking. These kinds of mutations change one nucleotide – an A, C, T or G – in the DNA sequence. Over 86 percent of the harmful protein-coding mutations of this type arose in humans just during the past 5,000 to 10,000 years.
Some of the remaining mutations of this nature may have no effect on people, and a few might be beneficial, according to the project researchers. While each specific mutation is rare, the findings suggest that the human population acquired an abundance of these single-nucleotide genetic variants in a relatively short time. (more…)
Researchers have devised a nanoscale sensor to electronically read the sequence of a single DNA molecule, a technique that is fast and inexpensive and could make DNA sequencing widely available.
The technique could lead to affordable personalized medicine, potentially revealing predispositions for afflictions such as cancer, diabetes or addiction. (more…)
*Berkeley Lab Researchers Identify Structure of Key Control Element Behind Protein Misfolding That Can Lead to Disease*
The gold standard for nanotechnology is nature’s own proteins. These biomolecular nanomachines – macromolecules forged from peptide chains of amino acids – are able to fold themselves into a dazzling multitude of shapes and forms that enable them to carry out an equally dazzling multitude of functions fundamental to life. As important as protein folding is to virtually all biological systems, the mechanisms behind this process have remained a mystery. The fog, however, is being lifted.
A team of researchers with the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab), using the exceptionally bright and powerful x-ray beams of the Advanced Light Source, have determined the crystal structure of a critical control element within chaperonin, the protein complex responsible for the correct folding of other proteins. The incorrect or “misfolding” of proteins has been linked to many diseases, including Alzheimer’s, Parkinson’s and some forms of cancer. (more…)
