Sandbox Reserved 911
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{{Johnson_CH462_Spring2014}} | {{Johnson_CH462_Spring2014}} | ||
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| - | <Structure load='2VYA' size='350' frame='true' align='right' caption='Fatty Acid Amide Hydrolase 1' scene='57/573125/2vya/1' | + | <Structure load='2VYA' size='350' frame='true' align='right' caption='Fatty Acid Amide Hydrolase 1' scene='57/573125/2vya/1'> |
==Introduction== | ==Introduction== | ||
Fatty acid amide hydrolase (FAAH) degrades fatty acid amides to terminate their signaling activity. A serine hydrolase from the [http://en.wikipedia.org/wiki/Amidase Amidase] signature superfamily of enzymes ([http://proteopedia.org/wiki/index.php/Category:Amidase other amidases]), FAAH degrades endocannabinoid signaling lipids, molecules associated with pain relief. Because [http://en.wikipedia.org/wiki/Endocannabinoid_system endocannabinoids] are lipid molecules, they cannot be compartmentalized in vesicles (the degradation method for other neurotransmitters) and must instead be degraded in the bilayer of the cell membrane. FAAH is an integral membrane protein that degrades FAAs as they enter the membrane bilayer. Current research about FAAH aims to find inhibitors for the enzyme, which would prolong the pain alleviation provided by endocannabinoid molecules. | Fatty acid amide hydrolase (FAAH) degrades fatty acid amides to terminate their signaling activity. A serine hydrolase from the [http://en.wikipedia.org/wiki/Amidase Amidase] signature superfamily of enzymes ([http://proteopedia.org/wiki/index.php/Category:Amidase other amidases]), FAAH degrades endocannabinoid signaling lipids, molecules associated with pain relief. Because [http://en.wikipedia.org/wiki/Endocannabinoid_system endocannabinoids] are lipid molecules, they cannot be compartmentalized in vesicles (the degradation method for other neurotransmitters) and must instead be degraded in the bilayer of the cell membrane. FAAH is an integral membrane protein that degrades FAAs as they enter the membrane bilayer. Current research about FAAH aims to find inhibitors for the enzyme, which would prolong the pain alleviation provided by endocannabinoid molecules. | ||
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FAAH primarily degrades [http://www.chm.bris.ac.uk/motm/anandamide/ananh.htm anandamide] (AEA), a naturally-occurring lipid that functions in the brain. AEA brings pain relief to the body. Inhibiting FAAH would likely sustain AEA signaling, leading to prolonged pain relief and decreased inflammation. | FAAH primarily degrades [http://www.chm.bris.ac.uk/motm/anandamide/ananh.htm anandamide] (AEA), a naturally-occurring lipid that functions in the brain. AEA brings pain relief to the body. Inhibiting FAAH would likely sustain AEA signaling, leading to prolonged pain relief and decreased inflammation. | ||
[[Image:AEA image.png|200 px|left|thumb|[http://en.wikipedia.org/wiki/File:Anandamide_skeletal.svg Anandamide]]] | [[Image:AEA image.png|200 px|left|thumb|[http://en.wikipedia.org/wiki/File:Anandamide_skeletal.svg Anandamide]]] | ||
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Revision as of 12:13, 25 March 2014
| This Sandbox is Reserved from Jan 06, 2014, through Aug 22, 2014 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 911 through Sandbox Reserved 922. |
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