Sandbox Ben Whiteside: Difference between revisions
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==Introduction== | ==Introduction== | ||
When consuming food, the human body is tasked with secreting hormones and chemical messengers that will help regulate homeostasis. After a meal, the body has to maintain homeostasis by reducing blood glucose and signaling that enough nutrients have been consumed. During feeding, cells in the body will secrete the ligand, amylin. [https://en.wikipedia.org/wiki/Amylin Amylin] is a 37 amino acid glucoregulatory hormone that is produced within [https://en.wikipedia.org/wiki/Beta_cell beta cells] of the pancreas. When there is an influx of nutrients in the gastrointestinal tract, the ligand will bind to the heterodimeric receptor, activating the receptor and triggering the corresponding signaling cascade. The overall effect of this cascade is increased satiety, delayed gastric emptying, and inhibition of [https://en.wikipedia.org/wiki/Glucagon glucagon] secretion <ref name=”Bower”>PMID:27061187</ref>. The amylin receptors are widely distributed throughout the central nervous system <ref name= | When consuming food, the human body is tasked with secreting hormones and chemical messengers that will help regulate homeostasis. After a meal, the body has to maintain homeostasis by reducing blood glucose and signaling that enough nutrients have been consumed. During feeding, cells in the body will secrete the ligand, amylin. [https://en.wikipedia.org/wiki/Amylin Amylin] is a 37 amino acid glucoregulatory hormone that is produced within [https://en.wikipedia.org/wiki/Beta_cell beta cells] of the pancreas. When there is an influx of nutrients in the gastrointestinal tract, the ligand will bind to the heterodimeric receptor, activating the receptor and triggering the corresponding signaling cascade. The overall effect of this cascade is increased satiety, delayed gastric emptying, and inhibition of [https://en.wikipedia.org/wiki/Glucagon glucagon] secretion <ref name=”Bower”>PMID:27061187</ref>. The amylin receptors are widely distributed throughout the central nervous system <ref name="Hay">PMID:26071095</ref>. The amylin [https://en.wikipedia.org/wiki/G_protein-coupled_receptor g-protein coupled receptor] <scene name='10/1038828/Entire_protein_scene/4'>(AMYR) </scene>is a heterodimeric protein containing a [https://en.wikipedia.org/wiki/Calcitonin calcitonin] receptor domain, as well as one of three [https://en.wikipedia.org/wiki/Receptor_activity-modifying_protein receptor activity modifying proteins] (RAMP 1,2, or 3)<ref name=”Cao”>PMID:35324283</ref>. | ||
RAMPs are accessory proteins required for the appropriate localization and function of GPCRs <ref name=”Parameswaran”>PMID:17010614</ref>. As of now, there are three notable roles of RAMPs. RAMPs can allow for the signaling and trafficking of GPCRs from the endoplasmic reticulum to the cell membrane. Additionally, RAMPs are known to alter the interactions between the receptor and ligands, potentially inhibiting or activating the receptor. Lastly, RAMPs are also thought to play a role in the internalization and subsequent inactivation of GPCRs, by signaling receptor fate and recycling from the cell membrane <ref name="Hay" />. In the case of the AMYR, the RAMP acts as a scaffold to hold the transmembrane domain in place. More importantly, the RAMP restricts the dynamic movement of the extracellular domain of the calcitonin receptor, anchoring the CTR into the membrane. | RAMPs are accessory proteins required for the appropriate localization and function of GPCRs <ref name=”Parameswaran”>PMID:17010614</ref>. As of now, there are three notable roles of RAMPs. RAMPs can allow for the signaling and trafficking of GPCRs from the endoplasmic reticulum to the cell membrane. Additionally, RAMPs are known to alter the interactions between the receptor and ligands, potentially inhibiting or activating the receptor. Lastly, RAMPs are also thought to play a role in the internalization and subsequent inactivation of GPCRs, by signaling receptor fate and recycling from the cell membrane <ref name="Hay" />. In the case of the AMYR, the RAMP acts as a scaffold to hold the transmembrane domain in place. More importantly, the RAMP restricts the dynamic movement of the extracellular domain of the calcitonin receptor, anchoring the CTR into the membrane. | ||