Porcine islet amyloid polypeptide fragments are refractory to amyloid formation

Zhang, Xin; Cheng, Biao; Gong, Hao; Li, Chuanzhou; Chen, Hong; Zheng, Ling; Huang, Kun

doi:10.1016/j.febslet.2010.11.050

Cited by 40 publications

(25 citation statements)

References 40 publications

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“…All groups were static incubated at 65°C to form aggregates. The aggregation status of designated time points was determined by ThT fluorescence (a final ThT concentration of 20 μM) assay recorded on a Hitachi FL-2700 fluorometer (Hitachi, Japan) at 482 nm with an excitation wavelength of 450 nm as we previously described59. The data were normalized against the DMSO or quinone controls background measured at the corresponding concentrations.…”

Section: Methodsmentioning

confidence: 99%

Effects of several quinones on insulin aggregation

Gong

Peng

et al. 2014

Sci Rep

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124

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Protein misfolding and aggregation are associated with more than twenty diseases, such as neurodegenerative diseases and metabolic diseases. The amyloid oligomers and fibrils may induce cell membrane disruption and lead to cell apoptosis. A great number of studies have focused on discovery of amyloid inhibitors which may prevent or treat amyloidosis diseases. Polyphenols have been extensively studied as a class of amyloid inhibitors, with several polyphenols under clinical trials as anti-neurodegenerative drugs. As oxidative intermediates of natural polyphenols, quinones widely exist in medicinal plants or food. In this study, we used insulin as an amyloid model to test the anti-amyloid effects of four simple quinones and four natural anthraquinone derivatives from rhubarb, a traditional herbal medicine used for treating Alzheimer's disease. Our results demonstrated that all eight quinones show inhibitory effects to different extent on insulin oligomerization, especially for 1,4-benzoquinone and 1,4-naphthoquinone. Significantly attenuated oligomerization, reduced amount of amyloid fibrils and reduced hemolysis levels were found after quinones treatments, indicating quinones may inhibit insulin from forming toxic oligomeric species. The results suggest a potential action of native anthraquinone derivatives in preventing protein misfolding diseases, the quinone skeleton may thus be further explored for designing effective anti-amyloidosis compounds.

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Section: Methodsmentioning

confidence: 99%

Effects of several quinones on insulin aggregation

Gong

Peng

et al. 2014

Sci Rep

Self Cite

124

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“…ThT fluorescence assays were preformed on a Hitachi FL-2700 fluorometer to detect the formation of amyloid at designated time points. The final assay solution contains 25 mM PBS (pH 7.4), 50 mM NaCl and 20 µM thioflavin-T [27]. ThT fluorescence was recorded at 482 nm with an excitation wavelength of 450 nm.…”

Section: Methodsmentioning

confidence: 99%

Bisphenol A Accelerates Toxic Amyloid Formation of Human Islet Amyloid Polypeptide: A Possible Link between Bisphenol A Exposure and Type 2 Diabetes

et al. 2013

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Bisphenol A (BPA) is a chemical compound widely used in manufacturing plastic products. Recent epidemiological studies suggest BPA exposure is positively associated with the incidence of type 2 diabetes mellitus (T2DM), however the mechanisms underlying this link remain unclear. Human islet amyloid polypeptide (hIAPP) is a hormone synthesized and secreted by the pancreatic β-cells. Misfolding of hIAPP into toxic oligomers and mature fibrils can disrupt cell membrane and lead to β-cell death, which is regarded as one of the causative factors of T2DM. To test whether there are any connections between BPA exposure and hIAPP misfolding, we investigated the effects of BPA on hIAPP aggregation using thioflavin-T based fluorescence, transmission electronic microscopy, circular dichroism, dynamic light scattering, size-exclusion chromatography,fluorescence-dye leakage assay in an artificial micelle system and the generation of reactive oxygen species in INS-1 cells. We demonstrated that BPA not only dose-dependently promotes the aggregation of hIAPP and enhances the membrane disruption effects of hIAPP, but also promotes the extent of hIAPP aggregation related oxidative stress. Taken together, our results suggest that BPA exposure increased T2DM risk may involve the exacerbated toxic aggregation of hIAPP.

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“…27 2.8. Samples were detected by using a JASCO-810 circular dichroism spectropolarimeter (JASCO, Japan) under continuous N 2 flow.…”

Section: Far-uv Circular Dichroism (Cd) and Data Analysismentioning

confidence: 99%

Inhibition effects of tanshinone on the aggregation of α-synuclein

Zhao

et al. 2016

Food Funct.

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Parkinson's disease (PD) is one of the most common neurodegenerative diseases. Lewy bodies that are formed by the aggregated α-synuclein are a major pathological feature of PD. Salvia miltiorrhiza has been used as food and as a traditional medicine for centuries in China, with tanshinone I (TAN I) and tanshinone IIA (TAN IIA) as its major bioactive ingredients. Here, we investigated the effects of TAN I and TAN IIA on α-synuclein aggregation both in vitro and in a transgenic Caenorhabditis elegans PD model (NL5901). We demonstrated that TAN I and TAN IIA inhibited the aggregation of α-synuclein as demonstrated by the prolonged lag time and the reduced thioflavin-T fluorescence intensity; TAN I and TAN IIA also disaggregated preformed mature fibrils in vitro. Moreover, the presence of TAN I or TAN IIA affected the secondary structural transformation of α-synuclein from unstructured coils to β-sheets, and alleviated the membrane disruption caused by aggregated α-synuclein in vitro. Besides, the immuno-dot-blot assay indicated that TAN I and TAN IIA reduce the formation of oligomers and fibrils. We further found that TAN I and TAN IIA extended the life span of NL5901, a strain of transgenic C. elegans that expresses human α-synuclein, possibly by attenuating the aggregation of α-synuclein. Taken together, our results suggested that TAN I and TAN IIA may be explored further as potential candidates for the prevention and treatment of PD.

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Porcine islet amyloid polypeptide fragments are refractory to amyloid formation

Cited by 40 publications

References 40 publications

Effects of several quinones on insulin aggregation

Effects of several quinones on insulin aggregation

Bisphenol A Accelerates Toxic Amyloid Formation of Human Islet Amyloid Polypeptide: A Possible Link between Bisphenol A Exposure and Type 2 Diabetes

Inhibition effects of tanshinone on the aggregation of α-synuclein

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