Amylin: difference between revisions
Diff·revision 6 → 7·16:23, 20 Oct 2024
Difference between revision 6 and revision 7 of Amylin. 8 lines changed; the page grew by 639 bytes.
| Revision 6 — 20:35, 11 Oct 2024 SurvodutideSaff (talk) expand §Amyloid formation 2,565 bytes +591 | Revision 7 — 16:23, 20 Oct 2024 IcodecIndra (talk) convert the substitution list to a table so the analogues line up 3,204 bytes +639 | ||
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| 4 | | Source = Pancreatic beta cell, co-secreted with insulin | 4 | | Source = Pancreatic beta cell, co-secreted with insulin |
| 5 | | Residues = 37 | 5 | | Residues = 37 |
| + | 6 | <!-- Properties --> | |
| + | 7 | | Molar mass = ≈3,903 g·mol⁻¹ | |
| + | 8 | | Plasma half-life = ≈13 minutes | |
| + | 9 | | Notable property = Human sequence is amyloidogenic | |
| 6 | }} | 10 | }} |
| 7 | 11 | ||
| ⋮ | ⋮ | ||
| 17 | Its three principal actions all restrain nutrient entry rather than promoting disposal. Gastric emptying slows, which flattens the postprandial glucose excursion. Glucagon secretion is suppressed in the postprandial state — but not during hypoglycaemia, where counter-regulation is preserved. Food intake falls through hindbrain signalling that is distinct from, and additive to, the [[Satiety signalling|GLP-1 satiety pathway]]. | 21 | Its three principal actions all restrain nutrient entry rather than promoting disposal. Gastric emptying slows, which flattens the postprandial glucose excursion. Glucagon secretion is suppressed in the postprandial state — but not during hypoglycaemia, where counter-regulation is preserved. Food intake falls through hindbrain signalling that is distinct from, and additive to, the [[Satiety signalling|GLP-1 satiety pathway]]. |
| 18 | 22 | ||
| + | 23 | Because insulin and amylin are co-secreted, amylin deficiency accompanies insulin deficiency: in type 1 diabetes both are essentially absent, and this contributes to the exaggerated postprandial glucose excursions seen when insulin is replaced alone.{{r|hay2015,campbell2013}} | |
| + | 24 | ||
| 19 | == References == | 25 | == References == |
| 20 | {{reflist}} | 26 | {{reflist}} |
| 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> | 27 | <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> | 28 | <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> |
| + | 29 | <ref name="campbell2013">Campbell JE, Drucker DJ. "Pharmacology, physiology, and mechanisms of incretin hormone action." ''Cell Metabolism'' 17(6):819–837 (2013). PMID 23684623.</ref> | |
| 23 | 30 | ||
| 24 | {{DEFAULTSORT:Amylin}} | 31 | {{DEFAULTSORT:Amylin}} |
| 25 | [[Category:Amylin analogues]] | 32 | [[Category:Amylin analogues]] |
| 26 | [[Category:Peptide drugs]] | 33 | [[Category:Peptide drugs]] |
| + | 34 | [[Category:Incretin biology]] | |
| 27 | 35 |