Amylin: difference between revisions
Diff·revision 5 → 6·20:35, 11 Oct 2024
Difference between revision 5 and revision 6 of Amylin. 3 lines changed; the page grew by 591 bytes.
| Revision 5 — 07:46, 30 Sep 2024 SemaglutideSasha (talk) split §Pharmacology into receptor binding and downstream signalling 1,974 bytes ±0 | Revision 6 — 20:35, 11 Oct 2024 SurvodutideSaff (talk) expand §Amyloid formation 2,565 bytes +591 | ||
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| 10 | Amylin does not have a dedicated receptor. It acts at the calcitonin receptor in complex with one of three receptor-activity-modifying proteins, RAMP1, RAMP2 or RAMP3, which together constitute the AMY1, AMY2 and AMY3 receptors. The principal site of action for the satiety effect is the area postrema, outside the blood-brain barrier.{{r|hay2015}} | 10 | Amylin does not have a dedicated receptor. It acts at the calcitonin receptor in complex with one of three receptor-activity-modifying proteins, RAMP1, RAMP2 or RAMP3, which together constitute the AMY1, AMY2 and AMY3 receptors. The principal site of action for the satiety effect is the area postrema, outside the blood-brain barrier.{{r|hay2015}} |
| 11 | 11 | ||
| + | 12 | The human sequence is amyloidogenic: it aggregates into fibrils, and islet amyloid deposits derived from it are found in the pancreas in most people with long-standing type 2 diabetes. This property made native amylin undevelopable as a medicine and forced the design of non-aggregating analogues; see [[Amylin receptor agonist]].{{r|westermark2011}} | |
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| 12 | == Physiology == | 14 | == Physiology == |
| 13 | Amylin is co-packaged with insulin in the beta-cell secretory granule and released by the same stimuli, so its plasma profile mirrors that of insulin. Fasting concentrations are in the low picomolar range and rise several-fold after a meal.{{r|hay2015}} | 15 | Amylin is co-packaged with insulin in the beta-cell secretory granule and released by the same stimuli, so its plasma profile mirrors that of insulin. Fasting concentrations are in the low picomolar range and rise several-fold after a meal.{{r|hay2015}} |
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| 18 | {{reflist}} | 20 | {{reflist}} |
| 19 | <ref name="hay2015">Hay DL, Chen S, Lutz TA, Parkes DG, Roth JD. "Amylin: pharmacology, physiology, and clinical potential." ''Pharmacological Reviews'' 67(3):564–600 (2015). DOI:10.1124/pr.115.010629. PMID 26071095.</ref> | 21 | <ref name="hay2015">Hay DL, Chen S, Lutz TA, Parkes DG, Roth JD. "Amylin: pharmacology, physiology, and clinical potential." ''Pharmacological Reviews'' 67(3):564–600 (2015). DOI:10.1124/pr.115.010629. PMID 26071095.</ref> |
| + | 22 | <ref name="westermark2011">Westermark P, Andersson A, Westermark GT. "Islet amyloid polypeptide, islet amyloid, and diabetes mellitus." ''Physiological Reviews'' 91(3):795–826 (2011). DOI:10.1152/physrev.00042.2009. PMID 21742788.</ref> | |
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| 21 | {{DEFAULTSORT:Amylin}} | 24 | {{DEFAULTSORT:Amylin}} |