Effect of IAPP on the Proteome of Cultured Rin-5F CellsCitation formats

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Effect of IAPP on the Proteome of Cultured Rin-5F Cells. / Miraee-Nedjad, Samaneh; Sims, Paul F G; Schwartz, Jean-Marc; Doig, Andrew.

In: BMC Biochemistry, Vol. 19, No. 9, 12.11.2018.

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Miraee-Nedjad, Samaneh ; Sims, Paul F G ; Schwartz, Jean-Marc ; Doig, Andrew. / Effect of IAPP on the Proteome of Cultured Rin-5F Cells. In: BMC Biochemistry. 2018 ; Vol. 19, No. 9.

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@article{2d3f2199557d4b4d9999a1a8e3838d58,
title = "Effect of IAPP on the Proteome of Cultured Rin-5F Cells",
abstract = "Background: Islet amyloid polypeptide (IAPP) or amylin deposits can be found in the islets of type 2 diabetes patients. The peptide is suggested to be involved in the etiology of the disease through formation of amyloid deposits and destruction of β islet cells, though the underlying molecular events leading from IAPP deposition to β cell death are still largely unknown.Results: We used OFFGEL™ proteomics to study how IAPP exposure affects the proteome of rat pancreatic insulinoma Rin-5F cells. The OFFGELTM methodology is highly effective at generating quantitative data on hundreds of proteins affected by IAPP, with its accuracy confirmed by In Cell Western and Quantitative Real Time PCR results. Combining data on individual proteins identifies pathways and protein complexes affected by IAPP. IAPP disrupts protein synthesis and degradation, and induces oxidative stress. It causes decreases in protein transport and localization. IAPP disrupts the regulation of ubiquitin-dependent protein degradation and increases catabolic processes. IAPP causes decreases in protein transport and localization, and affects the cytoskeleton, DNA repair and oxidative stress.Conclusions: Results is consistent with a model where IAPP aggregates overwhelm the ability of a cell to degrade proteins via the ubiquitin system. Ultimately this leads to apoptosis. IAPP aggregates may be also toxic to the cell by causing oxidative stress, leading to DNA damage or by decreasing protein transport. The reversal of any of these effects, perhaps by targeting proteins which alter in response to IAPP, may be beneficial for type II diabetes.",
keywords = "Amylin, Type 2 diabetes, Proteomics, Mass spectrometry, Pathway analysis, Protein-protein interactions",
author = "Samaneh Miraee-Nedjad and Sims, {Paul F G} and Jean-Marc Schwartz and Andrew Doig",
year = "2018",
month = "11",
day = "12",
doi = "10.1186/s12858-018-0099-3",
language = "English",
volume = "19",
journal = "BMC Biochemistry",
issn = "1471-2091",
publisher = "Springer Nature",
number = "9",

}

RIS

TY - JOUR

T1 - Effect of IAPP on the Proteome of Cultured Rin-5F Cells

AU - Miraee-Nedjad, Samaneh

AU - Sims, Paul F G

AU - Schwartz, Jean-Marc

AU - Doig, Andrew

PY - 2018/11/12

Y1 - 2018/11/12

N2 - Background: Islet amyloid polypeptide (IAPP) or amylin deposits can be found in the islets of type 2 diabetes patients. The peptide is suggested to be involved in the etiology of the disease through formation of amyloid deposits and destruction of β islet cells, though the underlying molecular events leading from IAPP deposition to β cell death are still largely unknown.Results: We used OFFGEL™ proteomics to study how IAPP exposure affects the proteome of rat pancreatic insulinoma Rin-5F cells. The OFFGELTM methodology is highly effective at generating quantitative data on hundreds of proteins affected by IAPP, with its accuracy confirmed by In Cell Western and Quantitative Real Time PCR results. Combining data on individual proteins identifies pathways and protein complexes affected by IAPP. IAPP disrupts protein synthesis and degradation, and induces oxidative stress. It causes decreases in protein transport and localization. IAPP disrupts the regulation of ubiquitin-dependent protein degradation and increases catabolic processes. IAPP causes decreases in protein transport and localization, and affects the cytoskeleton, DNA repair and oxidative stress.Conclusions: Results is consistent with a model where IAPP aggregates overwhelm the ability of a cell to degrade proteins via the ubiquitin system. Ultimately this leads to apoptosis. IAPP aggregates may be also toxic to the cell by causing oxidative stress, leading to DNA damage or by decreasing protein transport. The reversal of any of these effects, perhaps by targeting proteins which alter in response to IAPP, may be beneficial for type II diabetes.

AB - Background: Islet amyloid polypeptide (IAPP) or amylin deposits can be found in the islets of type 2 diabetes patients. The peptide is suggested to be involved in the etiology of the disease through formation of amyloid deposits and destruction of β islet cells, though the underlying molecular events leading from IAPP deposition to β cell death are still largely unknown.Results: We used OFFGEL™ proteomics to study how IAPP exposure affects the proteome of rat pancreatic insulinoma Rin-5F cells. The OFFGELTM methodology is highly effective at generating quantitative data on hundreds of proteins affected by IAPP, with its accuracy confirmed by In Cell Western and Quantitative Real Time PCR results. Combining data on individual proteins identifies pathways and protein complexes affected by IAPP. IAPP disrupts protein synthesis and degradation, and induces oxidative stress. It causes decreases in protein transport and localization. IAPP disrupts the regulation of ubiquitin-dependent protein degradation and increases catabolic processes. IAPP causes decreases in protein transport and localization, and affects the cytoskeleton, DNA repair and oxidative stress.Conclusions: Results is consistent with a model where IAPP aggregates overwhelm the ability of a cell to degrade proteins via the ubiquitin system. Ultimately this leads to apoptosis. IAPP aggregates may be also toxic to the cell by causing oxidative stress, leading to DNA damage or by decreasing protein transport. The reversal of any of these effects, perhaps by targeting proteins which alter in response to IAPP, may be beneficial for type II diabetes.

KW - Amylin

KW - Type 2 diabetes

KW - Proteomics

KW - Mass spectrometry

KW - Pathway analysis

KW - Protein-protein interactions

U2 - 10.1186/s12858-018-0099-3

DO - 10.1186/s12858-018-0099-3

M3 - Article

VL - 19

JO - BMC Biochemistry

JF - BMC Biochemistry

SN - 1471-2091

IS - 9

ER -