Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity
Amylin, (or islet amyloid polypeptide; IAPP), a 37-amino acid peptide hormone, is released in response to nutrients, including glucose, lipids or amino acids. Amylin is co-stored and co-secreted with insulin by pancreatic islet β-cells. Amylin inhibits food intake, delays gastric emptying,...
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MDPI AG
2018-08-01
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| Series: | Cells |
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| Online Access: | http://www.mdpi.com/2073-4409/7/8/95 |
| _version_ | 1797759801309003776 |
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| author | Yoshimitsu Kiriyama Hiromi Nochi |
| author_facet | Yoshimitsu Kiriyama Hiromi Nochi |
| author_sort | Yoshimitsu Kiriyama |
| collection | DOAJ |
| description | Amylin, (or islet amyloid polypeptide; IAPP), a 37-amino acid peptide hormone, is released in response to nutrients, including glucose, lipids or amino acids. Amylin is co-stored and co-secreted with insulin by pancreatic islet β-cells. Amylin inhibits food intake, delays gastric emptying, and decreases blood glucose levels, leading to the reduction of body weight. Therefore, amylin as well as insulin play important roles in controlling the level of blood glucose. However, human amylin aggregates and human amylin oligomers cause membrane disruption, endoplasmic reticulum (ER) stress and mitochondrial damage. Since cytotoxicity of human amylin oligomers to pancreatic islet β-cells can lead to diabetes, the protection of pancreatic islet β cells from cytotoxic amylin is crucial. Human amylin oligomers also inhibit autophagy, although autophagy can function to remove amylin aggregates and damaged organelles. Small molecules, including β-sheet breaker peptides, chemical chaperones, and foldamers, inhibit and disaggregate amyloid formed by human amylin, suggesting the possible use of these small molecules in the treatment of diabetes. In this review, we summarize recent findings regarding the role and cytotoxicity of amylin and the protection of pancreatic islet β-cells from cytotoxicity of amylin. |
| first_indexed | 2024-03-12T18:49:41Z |
| format | Article |
| id | doaj.art-76622a3b2a93478291098a0f64ad2f81 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-12T18:49:41Z |
| publishDate | 2018-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-76622a3b2a93478291098a0f64ad2f812023-08-02T07:21:26ZengMDPI AGCells2073-44092018-08-01789510.3390/cells7080095cells7080095Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin CytotoxicityYoshimitsu Kiriyama0Hiromi Nochi1Kagawa School of Pharmaceutical Sciences, Tokushima Bunri University, Shido 1314-1, Kagawa, Sanuki 769-2193, JapanKagawa School of Pharmaceutical Sciences, Tokushima Bunri University, Shido 1314-1, Kagawa, Sanuki 769-2193, JapanAmylin, (or islet amyloid polypeptide; IAPP), a 37-amino acid peptide hormone, is released in response to nutrients, including glucose, lipids or amino acids. Amylin is co-stored and co-secreted with insulin by pancreatic islet β-cells. Amylin inhibits food intake, delays gastric emptying, and decreases blood glucose levels, leading to the reduction of body weight. Therefore, amylin as well as insulin play important roles in controlling the level of blood glucose. However, human amylin aggregates and human amylin oligomers cause membrane disruption, endoplasmic reticulum (ER) stress and mitochondrial damage. Since cytotoxicity of human amylin oligomers to pancreatic islet β-cells can lead to diabetes, the protection of pancreatic islet β cells from cytotoxic amylin is crucial. Human amylin oligomers also inhibit autophagy, although autophagy can function to remove amylin aggregates and damaged organelles. Small molecules, including β-sheet breaker peptides, chemical chaperones, and foldamers, inhibit and disaggregate amyloid formed by human amylin, suggesting the possible use of these small molecules in the treatment of diabetes. In this review, we summarize recent findings regarding the role and cytotoxicity of amylin and the protection of pancreatic islet β-cells from cytotoxicity of amylin.http://www.mdpi.com/2073-4409/7/8/95amylinIAPPdiabetesautophagyβ-sheet breakerchemical chaperonefoldamer |
| spellingShingle | Yoshimitsu Kiriyama Hiromi Nochi Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity Cells amylin IAPP diabetes autophagy β-sheet breaker chemical chaperone foldamer |
| title | Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity |
| title_full | Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity |
| title_fullStr | Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity |
| title_full_unstemmed | Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity |
| title_short | Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity |
| title_sort | role and cytotoxicity of amylin and protection of pancreatic islet β cells from amylin cytotoxicity |
| topic | amylin IAPP diabetes autophagy β-sheet breaker chemical chaperone foldamer |
| url | http://www.mdpi.com/2073-4409/7/8/95 |
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