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Journal articles on the topic 'Islet Amyloid Polypeptide – genetics'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Hull, Rebecca L., Melissah R. Watts, Keiichi Kodama, et al. "Genetic background determines the extent of islet amyloid formation in human islet amyloid polypeptide transgenic mice." American Journal of Physiology-Endocrinology and Metabolism 289, no. 4 (2005): E703—E709. http://dx.doi.org/10.1152/ajpendo.00471.2004.

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Genetic background is important in determining susceptibility to metabolic abnormalities such as insulin resistance and β-cell dysfunction. Islet amyloid is associated with reduced β-cell mass and function and develops in the majority of our C57BL/6J × DBA/2J (F1) male human islet amyloid polypeptide (hIAPP) transgenic mice after 1 yr of increased fat feeding. To determine the relative contribution of each parental strain, C57BL/6J (BL6) and DBA/2J (DBA2), to islet amyloid formation, we studied male hIAPP mice on each background strain (BL6, n = 13; and DBA2 n = 11) and C57BL/6J × DBA/2J F1mic

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2

Wookey, Peter J., Loredanna Xuereb, Christos Tikellis, and Mark E. Cooper. "Amylin in the Periphery." Scientific World JOURNAL 3 (2003): 163–75. http://dx.doi.org/10.1100/tsw.2003.17.

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Amylin (islet amyloid polypeptide) is a peptide synthesized principally in the b-cells of the pancreatic islets together with insulin and has actions as a hormone, growth factor, and modifier of behavior. As a hormone, amylin acts to modify gastric motility, renal resorption, and has metabolic actions. It is postulated that the principal function of amylin as a hormone is the activation of physiological processes associated with feeding. As a growth factor, amylin acts on bone cells, renal proximal tubular cells, and islet b-cells. Amylin has important targets in the brain that mediate its act

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3

Christmanson, Lars, Fredrik Rorsman, Göran Stenman, Per Westermark, and Christer Betsholtz. "The human islet amyloid polypeptide (IAPP) gene." FEBS Letters 267, no. 1 (1990): 160–66. http://dx.doi.org/10.1016/0014-5793(90)80314-9.

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4

Zhang, Xin, Biao Cheng, Hao Gong, et al. "Porcine islet amyloid polypeptide fragments are refractory to amyloid formation." FEBS Letters 585, no. 1 (2010): 71–77. http://dx.doi.org/10.1016/j.febslet.2010.11.050.

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5

Westermark, Gunilla T., Samuel Gebre-Medhin, Donald F. Steiner, and Per Westermark. "Islet Amyloid Development in a Mouse Strain Lacking Endogenous Islet Amyloid Polypeptide (IAPP) but Expressing Human IAPP." Molecular Medicine 6, no. 12 (2000): 998–1007. http://dx.doi.org/10.1007/bf03402051.

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6

Fortin, Jessica S., Nurhanis B. M. Isa, Anisa M. Rashid, Thomas L. Thompson, and Malikah O’Dell. "Small molecules breaking down islet amyloid polypeptide self‐assembly." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.08776.

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7

Wakabayashi, Masaki, and Katsumi Matsuzaki. "Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts." FEBS Letters 583, no. 17 (2009): 2854–58. http://dx.doi.org/10.1016/j.febslet.2009.07.044.

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8

Kanatsuka, A., H. Makino, H. Ohsawa, et al. "Secretion of islet amyloid polypeptide in response to glucose." FEBS Letters 259, no. 1 (1989): 199–201. http://dx.doi.org/10.1016/0014-5793(89)81527-3.

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9

Nishi, M., G. I. Bell, and D. F. Steiner. "Sequence of a cDNA encoding Syrian hamster islet amyloid polypeptide precursor." Nucleic Acids Research 18, no. 22 (1990): 6726. http://dx.doi.org/10.1093/nar/18.22.6726.

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10

Cheung, David L. "Effect of surface chemistry on islet amyloid polypeptide conformation." Biointerphases 15, no. 5 (2020): 051001. http://dx.doi.org/10.1116/6.0000417.

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11

Hagihara, Mamoru, Ayaka Takei, Takeshi Ishii, et al. "Inhibitory effects of choline-O-sulfate on amyloid formation of human islet amyloid polypeptide." FEBS Open Bio 2, no. 1 (2012): 20–25. http://dx.doi.org/10.1016/j.fob.2012.02.001.

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12

Magzoub, Mazin, and Andrew D. Miranker. "Concentration‐dependent transitions govern the subcellular localization of islet amyloid polypeptide." FASEB Journal 26, no. 3 (2011): 1228–38. http://dx.doi.org/10.1096/fj.11-194613.

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13

Rulifson, Ingrid C., Ping Cao, Li Miao, et al. "Identification of Human Islet Amyloid Polypeptide as a BACE2 Substrate." PLOS ONE 11, no. 2 (2016): e0147254. http://dx.doi.org/10.1371/journal.pone.0147254.

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14

Betsholtz, Christer, Lars Christmansson, Ulla Engström, et al. "Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species." FEBS Letters 251, no. 1-2 (1989): 261–64. http://dx.doi.org/10.1016/0014-5793(89)81467-x.

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15

Mosselman, S., J. W. M. Höppener, C. J. M. Lips, and H. S. Jansz. "The complete islet amyloid polypeptide precursor is encoded by two exons." FEBS Letters 247, no. 1 (1989): 154–58. http://dx.doi.org/10.1016/0014-5793(89)81260-8.

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16

Mosselman, S., J. W. M. Höppener, J. Zandberg, et al. "Islet amyloid polypeptide: Identification and chromosomal localization of the human gene." FEBS Letters 239, no. 2 (1988): 227–32. http://dx.doi.org/10.1016/0014-5793(88)80922-0.

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17

Xue, Bingzhong, та Michael B. Zemel. "Agouti Signaling Protein Stimulates Islet Amyloid Polypeptide (Amylin) Secretion in Pancreatic β-Cells". Experimental Biology and Medicine 226, № 6 (2001): 565–69. http://dx.doi.org/10.1177/153537020122600609.

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18

Cadavez, Lisa, Joel Montane, Gema Alcarraz-Vizán, et al. "Chaperones Ameliorate Beta Cell Dysfunction Associated with Human Islet Amyloid Polypeptide Overexpression." PLoS ONE 9, no. 7 (2014): e101797. http://dx.doi.org/10.1371/journal.pone.0101797.

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19

Xie, Ling, Xiaohong Gu, Kenta Okamoto, Gunilla T. Westermark, and Klaus Leifer. "3D analysis of human islet amyloid polypeptide crystalline structures in Drosophila melanogaster." PLOS ONE 14, no. 10 (2019): e0223456. http://dx.doi.org/10.1371/journal.pone.0223456.

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20

Bedrood, S., S. A. Jayasinghe, and R. Langen. "61 IDENTIFYING STRUCTURAL FEATURES OF ISLET AMYLOID POLYPEPTIDE USING SITE-DIRECTED SPIN LABELING." Journal of Investigative Medicine 54, no. 1 (2006): S90.2—S90. http://dx.doi.org/10.2310/6650.2005.x0004.60.

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21

Visa, Montse, Gema Alcarraz‐Vizán, Joel Montane та ін. "Islet amyloid polypeptide exerts a novel autocrine action in β‐cell signaling and proliferation". FASEB Journal 29, № 7 (2015): 2970–79. http://dx.doi.org/10.1096/fj.15-270553.

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22

BRETHERTON-WATT, D., M. A. GHATEI, H. JAMAL, S. G. GILBEY, P. M. JONES, and S. R. BLOOM. "The Physiology of Calcitonin Gene?Related Peptide in the Islet Compared with That of Islet Amyloid Polypeptide (Amylin)." Annals of the New York Academy of Sciences 657, no. 1 Calcitonin Ge (1992): 299–312. http://dx.doi.org/10.1111/j.1749-6632.1992.tb22777.x.

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23

Schultz, Sebastian Wolfgang, K. Peter R. Nilsson, and Gunilla Torstensdotter Westermark. "Drosophila Melanogaster as a Model System for Studies of Islet Amyloid Polypeptide Aggregation." PLoS ONE 6, no. 6 (2011): e20221. http://dx.doi.org/10.1371/journal.pone.0020221.

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24

Milton, Nathaniel G. N., and J. Robin Harris. "Human Islet Amyloid Polypeptide Fibril Binding to Catalase: A Transmission Electron Microscopy and Microplate Study." Scientific World JOURNAL 10 (2010): 879–93. http://dx.doi.org/10.1100/tsw.2010.73.

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The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrilsin vitroandin vivo. Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-β (Aβ) and prion protein (PrP) fibrils. Previous studies have shown that catalase binds to Aβ fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. This study presents a transmission electron microscopy (TEM)—based analysis of fibril formation and the binding of human erythrocyte catalas

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25

van Mansfeld, A. D. M., S. Mosselman, J. W. M. Höppener, et al. "Islet amyloid polypeptide: Structure and upstream sequences of the IAPP gene in rat and man." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1087, no. 2 (1990): 235–40. http://dx.doi.org/10.1016/0167-4781(90)90210-s.

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26

Westermark, Per, and Kenneth H. Johnson. "The pathogenesis of maturity-onset diabetes mellitus: Is there a link to islet amyloid polypeptide?" BioEssays 9, no. 1 (1988): 30–33. http://dx.doi.org/10.1002/bies.950090109.

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27

Sussel, L., J. Kalamaras, D. J. Hartigan-O'Connor, et al. "Mice lacking the homeodomain transcription factor Nkx2.2 have diabetes due to arrested differentiation of pancreatic beta cells." Development 125, no. 12 (1998): 2213–21. http://dx.doi.org/10.1242/dev.125.12.2213.

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The endocrine pancreas is organized into clusters of cells called islets of Langerhans comprising four well-defined cell types: alpha beta, delta and PP cells. While recent genetic studies indicate that islet development depends on the function of an integrated network of transcription factors, the specific roles of these factors in early cell-type specification and differentiation remain elusive. Nkx2.2 is a member of the mammalian NK2 homeobox transcription factor family that is expressed in the ventral CNS and the pancreas. Within the pancreas, we demonstrate that Nkx2.2 is expressed in alp

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28

Peinado, Juan R., Furqan Sami, Nina Rajpurohit, and Iris Lindberg. "Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAAS." FEBS Letters 587, no. 21 (2013): 3406–11. http://dx.doi.org/10.1016/j.febslet.2013.09.006.

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29

Konno, Takashi, Shigetoshi Oiki, and Takashi Morii. "Synergistic action of polyanionic and non-polar cofactors in fibrillation of human islet amyloid polypeptide." FEBS Letters 581, no. 8 (2007): 1635–38. http://dx.doi.org/10.1016/j.febslet.2007.03.030.

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30

Gharibyan, Anna L., Tohidul Islam, Nina Pettersson, et al. "Apolipoprotein E Interferes with IAPP Aggregation and Protects Pericytes from IAPP-Induced Toxicity." Biomolecules 10, no. 1 (2020): 134. http://dx.doi.org/10.3390/biom10010134.

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Apolipoprotein E (ApoE) has become a primary focus of research after the discovery of its strong linkage to Alzheimer’s disease (AD), where the ApoE4 variant is the highest genetic risk factor for this disease. ApoE is commonly found in amyloid deposits of different origins, and its interaction with amyloid-β peptide (Aβ), the hallmark of AD, is well known. However, studies on the interaction of ApoEs with other amyloid-forming proteins are limited. Islet amyloid polypeptide (IAPP) is an amyloid-forming peptide linked to the development of type-2 diabetes and has also been shown to be involved

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31

Schultz, Nina, Shorena Janelidze, Elin Byman, et al. "Levels of islet amyloid polypeptide in cerebrospinal fluid and plasma from patients with Alzheimer’s disease." PLOS ONE 14, no. 6 (2019): e0218561. http://dx.doi.org/10.1371/journal.pone.0218561.

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32

Lam, Vincent Kwok Lim, Ronald Ching Wan Ma, Heung Man Lee, et al. "Genetic Associations of Type 2 Diabetes with Islet Amyloid Polypeptide Processing and Degrading Pathways in Asian Populations." PLoS ONE 8, no. 6 (2013): e62378. http://dx.doi.org/10.1371/journal.pone.0062378.

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33

Balali-Mood, Kia, Richard H. Ashley, Thomas Hauß, and Jeremy P. Bradshaw. "Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin." FEBS Letters 579, no. 5 (2005): 1143–48. http://dx.doi.org/10.1016/j.febslet.2004.12.085.

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34

Paulsson, Johan F., Johnny Ludvigsson, Annelie Carlsson, et al. "High Plasma Levels of Islet Amyloid Polypeptide in Young with New-Onset of Type 1 Diabetes Mellitus." PLoS ONE 9, no. 3 (2014): e93053. http://dx.doi.org/10.1371/journal.pone.0093053.

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35

Gill, Anne M., and Terence T. Yen. "Effects of ciglitazone on endogenous plasma islet amyloid polypeptide and insulin sensitivity in obese-diabetic viable yellow mice." Life Sciences 48, no. 7 (1991): 703–10. http://dx.doi.org/10.1016/0024-3205(91)90546-n.

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36

Radovan, Diana, Norbert Opitz, and Roland Winter. "Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol." FEBS Letters 583, no. 9 (2009): 1439–45. http://dx.doi.org/10.1016/j.febslet.2009.03.059.

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37

KIKUCHI, YOSHIFUMI, MASARU KOIZUMI, TOORU SHIMOSEGAWA, JYUNYA KASHIMURA, SUSUMU SUZUKI, and TAKAYOSHI TOYOTA. "Islet Amyloid Polypeptide has No Effect on Amylase Release from Rat Pancreatic Acini Stimulated by CCK-8, Secretin, Carbachol and VIP." Tohoku Journal of Experimental Medicine 165, no. 1 (1991): 41–48. http://dx.doi.org/10.1620/tjem.165.41.

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38

Kong, Siyuan, Jinxue Ruan, Kaiyi Zhang, et al. "Kill two birds with one stone: making multi-transgenic pre-diabetes mouse models through insulin resistance and pancreatic apoptosis pathogenesis." PeerJ 6 (April 17, 2018): e4542. http://dx.doi.org/10.7717/peerj.4542.

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Background Type 2 diabetes is characterized by insulin resistance accompanied by defective insulin secretion. Transgenic mouse models play an important role in medical research. However, single transgenic mouse models may not mimic the complex phenotypes of most cases of type 2 diabetes. Methods Focusing on genes related to pancreatic islet damage, peripheral insulin resistance and related environmental inducing factors, we generated single-transgenic (C/EBP homology protein, CHOP) mice (CHOP mice), dual-transgenic (human islet amyloid polypeptide, hIAPP; CHOP) mice (hIAPP-CHOP mice) and tripl

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39

Cho, William C. S., Tai-Tung Yip, Wai-Shing Chung, Albert W. N. Leung, Christopher H. K. Cheng, and Kevin K. M. Yue. "Potential Biomarkers Found by Protein Profiling May Provide Insight for the Macrovascular Pathogenesis of Diabetes Mellitus." Disease Markers 22, no. 3 (2006): 153–66. http://dx.doi.org/10.1155/2006/450762.

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Diabetes mellitus (DM) is an alarming threat to health of mankind, yet its pathogenesis is unclear. The purpose of this study was to find potential biomarkers to serve as indicators for the pathogenesis of DM in a time course manner. Based on our previous findings that oxidative stress occurred at week 8, aorta lysate and sera of 102 streptozotocin (STZ)-induced diabetic and 85 control male Sprague-Dawley rats were obtained at the 4th, 8th and 12th week after STZ injection. The protein profiles were studied employing surface-enhanced laser desorption/ionization time-of-flight mass spectrometry

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40

Westermark, P., E. Wilander, and K. H. Johnson. "ISLET AMYLOID POLYPEPTIDE." Lancet 330, no. 8559 (1987): 623. http://dx.doi.org/10.1016/s0140-6736(87)93008-x.

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41

Bretherton-Watt, Deborah, and Stephen R. Bloom. "Islet amyloid polypeptide." Trends in Endocrinology & Metabolism 2, no. 6 (1991): 203–6. http://dx.doi.org/10.1016/1043-2760(91)90025-i.

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42

Wu, Chun, and Joan-Emma Shea. "Structural Similarities and Differences between Amyloidogenic and Non-Amyloidogenic Islet Amyloid Polypeptide (IAPP) Sequences and Implications for the Dual Physiological and Pathological Activities of These Peptides." PLoS Computational Biology 9, no. 8 (2013): e1003211. http://dx.doi.org/10.1371/journal.pcbi.1003211.

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43

Wang, Qianqian, Jingjing Guo, Pingzu Jiao, Huanxiang Liu та Xiaojun Yao. "Exploring the Influence of EGCG on the β-Sheet-Rich Oligomers of Human Islet Amyloid Polypeptide (hIAPP1–37) and Identifying Its Possible Binding Sites from Molecular Dynamics Simulation". PLoS ONE 9, № 4 (2014): e94796. http://dx.doi.org/10.1371/journal.pone.0094796.

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44

Clark, Anne, Eelco J. P. de Koning, and John F. Morris. "Formation of islet amyloid from islet amyloid polypeptide." Biochemical Society Transactions 21, no. 1 (1993): 169–73. http://dx.doi.org/10.1042/bst0210169.

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45

Epstein, Franklin H., Kenneth H. Johnson, Timothy D. O'Brien, Christer Betsholtz, and Per Westermark. "Islet Amyloid, Islet-Amyloid Polypeptide, and Diabetes Mellitus." New England Journal of Medicine 321, no. 8 (1989): 513–18. http://dx.doi.org/10.1056/nejm198908243210806.

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46

Westermark, Per, Arne Andersson, and Gunilla T. Westermark. "Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus." Physiological Reviews 91, no. 3 (2011): 795–826. http://dx.doi.org/10.1152/physrev.00042.2009.

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Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon secretion, and at distant targets. It has binding sites in the brain, possibly contributing also to satiety regulation and inhibits gastric emptying. Effects on several other organs have also been described. IAPP was discovered through its ability to aggregate into pancreatic islet amyloid deposits, which are seen particularly in association with

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47

Westermark, Gunilla, and Per Westermark. "Islet Amyloid Polypeptide and Diabetes." Current Protein & Peptide Science 14, no. 4 (2013): 330–37. http://dx.doi.org/10.2174/13892037113149990050.

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48

Sugawara, Kazuhiko, Tetsuro Kobayashi, Koji Nakanishi, et al. "Marked Islet Amyloid Polypeptide-Positive Amyloid Deposition." Pancreas 8, no. 3 (1993): 312–15. http://dx.doi.org/10.1097/00006676-199305000-00005.

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49

Gilbey, Stephen G., Mohammad A. Ghatei, Deborah Bretherton-Watt, et al. "Islet amyloid polypeptide: production by an osteoblast cell line and possible role as a paracrine regulator of osteoclast function in man." Clinical Science 81, no. 6 (1991): 803–8. http://dx.doi.org/10.1042/cs0810803.

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1. The recently discovered peptide islet amyloid polypeptide shows considerable sequence homology with calcitonin-gene-related peptide, itself an alternative product of the calcitonin gene. The possibility that islet amyloid polypeptide might affect calcium homoeostasis and bone cell function was investigated. 2. Islet amyloid polypeptide messenger RNA was found to be expressed by human HTb 96 osteoblast-like cells in culture, and islet amyloid polypeptide immunoreactivity was present in the cell culture medium. 3. Infusion of islet amyloid polypeptide (150 pmol min−1 kg−1) caused a fall in se

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50

Leckström, Arnold, Kaj Björklund, Johan Permert, Rutger Larsson, and Per Westermark. "Renal Elimination of Islet Amyloid Polypeptide." Biochemical and Biophysical Research Communications 239, no. 1 (1997): 265–68. http://dx.doi.org/10.1006/bbrc.1997.7465.

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