The Cell Utilizes A Switch Board System!

[President Wilson]

Look at this quote from one of the Worlds Top Scientific Journals - Nature

Reference: Nature, pp. 858-861, 20 June 2002.

<font color="green"> Large manufacturers need centralized communication so things are supplied when and where needed, and in the right amounts. So, too, in living cells researchers have discovered that cells have a switchboard system that coordinates the barrage of cues and messages they receive and transmit.

It had been thought that cell communication, or signal transduction, was an 'automatic' cascade of biochemical events. But this study found that even before a message makes it through the outer cell membrane to the inner nucleus, the cell activates a molecular switch to guide how and in what form the message will be delivered.

Our results add a layer of complexity to understanding how messages are communicated by cells, says one researcher. 'Without this switchboard system , the cell would go crazy and overload.

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That is absolutely phenominal to say the least

that is awesome....but really makes sence and simple if you think about it...i mean how else could it control itself in such a perfect manner withough something to guide it, and control everything?

[President Wilson]

[ QUOTE ]
i mean how else could it control itself in such a perfect manner withough something to guide it, and control everything?


[/ QUOTE ]

This is true. The system must be extremely efficient. I know it is calculated that the human body processes more information in a single 24 hour period than all of human knowledge combined. The figure is 10 ^ 24th power of bits for the total information processed in a day, which exceeds human knowledge by a factor of 1,000,000. Which means, the cell must have incredible processing, and regulating systems. Or as the Scientist in Nature stated, things would go crazy

[Fireproof]

Wow. Talk about 'intelligent design' by an amazing Creator!

[Adam Knowlden]

The incredible complexity at the cellular level of the human body is insane!

Check out this clip:

ARCHITECTURE OF A CELL-MEMBRANE WATER CHANNEL: High Resolution Unveils Secrets of Specificity and Speed

<font color="red"> The structure of one of the basic members of the cell-membrane water-channel family, a protein called aquaporin 1 (AQP1), has been determined to a resolution of 2.2 angstroms -- 22 hundred-billionths of a meter. The structure reveals the elegantly simple means by which AQP1 can transport water through the cell membrane at a high rate while effectively blocking everything else -- even individual protons, the nuclei of hydrogen atoms.
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[Venom]

Awesome! /forum/images/graemlins/laugh.gif

[Adam Knowlden]

http://www.lbl.gov/Science-Articles/Archive/assets/images/2001/Dec-19-2001/AQP1-pore-sideview.jpg

"A side view of a pore (blue dots) in the water-channel protein AQP1, which pierces the cell membrane. Cell exterior is at top, interior at bottom. The pore is about 2.8 angstroms across at its narrowest. "

[ QUOTE ]
Body temperature, digestion, reproduction, fluid pressure in the eye, and water conservation in the kidney are only a few of the processes in humans that depend on the proper functioning of cellular water channels.

"Membrane proteins are a very large class of proteins; some 30 percent of the genes in the human genome code for them. But they are notoriously difficult to crystallize, and only a few structures have been solved at very high resolution," Jap says.


[/ QUOTE ]

AQP1 is interesting because it is so specific for water" says Jap. "The key question was how it achieves this specificity.

http://www.lbl.gov/Science-Articles/Archive/assets/images/2001/Dec-19-2001/AQP1-topview.jpg

"From outside the cell, the four units of the water-channel protein AQP1 are visible, each with a pore that penetrates the cell membrane."


"Body temperature, digestion, reproduction, fluid pressure in the eye, and water conservation in the kidney are only a few of the processes in humans that depend on the proper functioning of cellular water channels."

"Membrane proteins are a very large class of proteins; some 30 percent of the genes in the human genome code for them. But they are notoriously difficult to crystallize, and only a few structures have been solved at very high resolution," Jap says.

"AQP1 is interesting because it is so specific for water" says Jap. "The key question was how it achieves this specificity. Theorists had come up with lots of ideas, but before we saw the structure in high-resolution, nobody knew how it was accomplished."

Architecturally, AQP1 is an assembly of four units, each with three major structural features: each has an entrance, or "vestibule," on the outside of the cell envelope, connected to a similar vestibule inside the cell by a long, narrow pore.

From outside the cell, the four units of the water-channel protein AQP1 are visible, each with a pore that penetrates the cell membrane.

"The secret of AQP1's specificity is two-fold: it selects for size and for chemical nature," Jap says. "There is a very narrow constriction in the pore, which admits no molecule bigger than water. To keep out molecules smaller than water there is also a chemical filter, formed by the specific orientation and distribution of the amino acid residues lining the pore."

Molecules attempting to enter the channel are bound to water molecules that are stripped away in the pore; charged species are therefore left with net electrical charge. "The filter strongly rejects charged molecules or ions, even as small as single protons," Jap explains.

The unique distribution of amino acid residues along the pore wall also accounts for the channel's ability to move water quickly, explains Peter Walian, a member of the team that solved the structure. "It's a schizophrenic environment, half hydrophilic and half hydrophobic" -- that is, half water-loving and half water-fearing. "Water molecules readily get in because of the hydrophilic sites, but the hydrophobic regions prevent them from binding too frequently."

Thus water and only water flows freely in and out of the cell through AQP1's pores, the direction of flow depending only on changing relative pressure inside and outside the cell. "It's a beautiful mechanism," Walian remarks. "It's remarkable that nobody thought of it before now."


"Structural basis of water specific transport through AQP1 water channel," by Haixin Sui, Bong-Gyoon Han, John K. Lee, Peter Walian, and Bing K. Jap, appears in the 20 December 2001 issue of the journal Nature.

[Pesca]

wow, thats insane!!

[William Ustav]

Really incredible! But, like it's been said here, it all makes so much sense!!! /forum/images/graemlins/laugh.gif

[**DONOTDELETE**]

[jlong]

Interesting, the human body is truely amazing.

Could we hire this switch board to handle our incoming calls at work. /forum/images/graemlins/smile.gif