Ancient Protein Messaging System Mapped
It is astounding what one can do on a single microarray. For example, discovering the extent to which our bodies use a simple signaling mechanism that has been around since the dawn of evolution.
In the protein world, molecules are shaped and customized for specific and precise purposes. Even the addition of a slight detail can change its effect. A good example is nitrosylation, attaching a nitric oxide (NO) to the end of an amino acid (protein building block) called cysteine. This attachment is used as a signaling mechanism to switch proteins on and off, and is employed in cell function regulation in almost all forms of life. It is linked to Parkinson’s, Alzheimer’s, ALS, and cancer. But with all its importance, there is still much we don’t know about this mechanism, especially the full extent of roles it plays in cells. However, in October researchers at Johns Hopkins University mapped out the entire collection of nitrosylated proteins in the human body (also called the human nitrosoproteome). They deposited the full set of 16,368 human proteins onto a single microarray slide using Arrayit’s NanoPrint LM210 microarrayer. Employing a technique called the Biotin Switch Method, they replaced all the nitric oxide groups with a chemical called biotin, which is easier to analyze. They found 834 proteins that were nitrosylated and cut across a wide range of biological functions, including metabolism, cell growth, DNA regulation, and muscle functioning. 131 of the proteins did not fall into any group. The 834 proteins contained 5,933 cysteines with an NO group altogether, with the modified amino acid showing up in positions on the protein structure that hadn’t been seen before. To read more about this advancement, check out the original paper here: http://www.mcponline.org/content/early/2013/10/08/mcp.M113.032235.full.pdf+html |
Arrayit Corporation
524 East Weddell Drive, Sunnyvale, CA 94089 USA Phone: 408-744-1331 Fax: 408-744-1711
524 East Weddell Drive, Sunnyvale, CA 94089 USA Phone: 408-744-1331 Fax: 408-744-1711