The animation explores "the mechanisms that allow a white blood cell to sense its surroundings and respond to an external stimulus."
The technology used to study brain neurons in real time has been adapted for the real time study of other biological processes. This is going to rapidly boost our understanding of exactly how our cells and plant cells work. We can then modify those processes to boost food production or drugs and other products produced by biological means. Computer simulations will help to guide the understanding and the modifications of the processes. This will also accelerate transhumanist efforts to transcend current biology and improve human capabilities.
New technology addresses metabolism studyig problems by measuring sugar flux in real time in individual cells, with subcellular resolution.
Frommer and his colleagues have used similar imaging tags, called fluorescent resonance energy transfer (FRET) sensors, to track sugars and neurotransmitters in animal cells. Most recently, the group used FRET sensors to study glutamate, an important mammalian neurotransmitter. Frommer has tracked glucose in cultured mammalian cells, but until now, plant tissues had proven problematic because of interference from the plants' virus defense mechanisms, as well as high background fluorescence in some plants.
To surmount these issues, Frommer's team dramatically improved the sensors, while inserting them in mutant Arabidopsis plants with disabled defense genes. The fluorescent tags worked well where they had failed before.
FRET sensors are encoded by genes that, in theory, can be engineered into any cell line or organism. They are made of two fluorescent proteins that produce different colors of light--one cyan and one yellow--connected by a third protein that resembles a hinged clam shell. The two fluorescent proteins are derived from jellyfish, and the third from a bacterium; the shape of the clam shell protein determines which sugar or other molecule the sensor can detect. When a target molecule such as glucose or sucrose binds to the third protein, the hinge opens, changing the distance and orientation of the fluorescent proteins. This physical change affects the energy transfer between the cyan and yellow markers.
When the researchers hit the tags with light of a specific wavelength, the cyan tag starts to fluoresce. If the yellow tag is close enough, the cyan tag will transfer its energy to the yellow tag, causing it to resonate and fluoresce as well. This energy transfer affects how much cyan and yellow fluorescence can be seen, and by calculating this ratio, researchers can accurately track molecules such as glucose and sucrose in both time and space.
"The strength of this technology lies in its elegant simplicity; with the power of computational design, we can potentially design FRET tags to detect virtually any small molecule in living cells," Frommer said.