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Definition
Amylin or Islet amyloid polypeptide (IAPP), a peptide of 37 amino acids is secreted by beta cells of pancreatic islets and a major component of amyloid deposits in patients with type 2 diabetes mellitus. Amylin may be called "insulin twin", as indicated constitutively by insulin in response to elevated blood glucose.

Discovery
Knowledge of the presence deposits of amyloid in the islets Langerhans important pathological feature of patients with diabetes has been known for a century. However, the discovery Amylin as a major component of amyloid deposits was by two independent groups in the 19,871, 2.

Features structural
The human amylin sequence KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY amino acid with a disulfide bond between cysteine residues 2 and 7. Characteristics, amidated C-terminal and disulfide bond are required for biological activity amylin3 complete. Amylin amino acid sequence is 46% and 43% identical to those of calcitonin gene-related neuropeptide CGRP and CGRP-2-1. The (20-29) fragment Amylin is central to the pathogenesis of islet amyloid4.

Mechanism of Action
Amylin is synthesized, packaged in the Golgi apparatus and secret inside granules secretory cells of the pancreatic beta islets. They have binding sites within the renal cortex in the juxtaglomerular apparatus and activates the renin angiotensin aldosterone. It also acts on the circulatory system by inhibiting the secretion of atrial natriuretic peptide (ANP) 5.

Feature
Amylin inhibits gastric emptying is important in controlling and delaying the type of meal-derived glucose. It inhibits the liver and output of glucose in the postprandial period. They have also been shown to inhibit the secretion of glucagon and somatostatin. Amylin causes vasodilatation, dilating the lack of striated muscles of blood vessels. It is also known to increase the level of thirst indicates you have an action in the center system6 nervous.

References
1. Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB (1987). Purification and characterization of a peptide amyloid-rich pancreas of patients with type 2 diabetes. Proc Natl Acad Sci 84 (23) :8628-32.
2. Westermark P, Wernstedt C, O'Brien TD, Hayden DW, Johnson KH (1987). Islet amyloid in diabetes mellitus type 2 diabetic cats adult human contains a putative polypeptide hormone novel. Am J Pathol, 127 (3) :414-417.
3. Roberts AN, Leighton B, Todd JA, Cockburn D, Schofield PN, Sutton R, Holt S, Boyd and Day AJ, Foot EA, et al (1989). Molecular characterization and functional amylin, a peptide associated with type 2 diabetes mellitus. Proc Natl Acad Sci, 86 (24) :9662-9666.
4. Guidobono M, Pagani F, Ticozzi C Sibilia V, Pecile A, Netti C (1997). Amylin protection of gastric erosions induced by indomethacin or ethanol in rats. Br J Pharmacol 120 (4) :581-586.
5. Piao FL, Cao C, Han JH, Kim SZ, Cho KW, Kim SH (2004). Amylin-induced suppression of ANP secretion through receptors for CGRP1 and salmon calcitonin. Regul Pept, 117: 59-166.
6. Hayden MR, Tyagi SC (2002). On Islet redox stress: multiple toxicities of insulin resistance, Metabolic Syndrome and Amylin derived islet amyloid in diabetes mellitus type 2. Journal of Pancrease

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Article Source: ArticlesBase.com - Amylin Peptides and Fragments

Order the molecules on the list below according to their ability to diffuse through a lipid bilayer?

Order the molecules on the list below according to their ability to diffuse through a lipid bilayer, beginning with the one that crosses the bilayer most readily. Explain your order.
a. Ca2+ d. glucose
b. CO2 e. RNA
c. ethanol f. H2O

CO2>ethanol>Ca>H2O>glucose>RNA

Gas is free disolvable. Next comes small lipid soluble and ethanol is more lipid soluble than the rest. Charged small ions and molecules are next, therefore Ca followed by water. Glucose is a larger charged molecule and therefore next and since RNA is the largest charged molecule in the list, it is last.

Molecular Plant Sciences at Virginia Tech

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