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Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
Open accessAbstract
Interleukin 1β (IL-1β) is an important inflammatory mediator of type 2 diabetes. Here we show that oligomers of islet amyloid polypeptide (IAPP), a protein that forms amyloid deposits in the pancreas during type 2 diabetes, triggered the NLRP3 inflammasome and generated mature IL-1β. One therapy for type 2 diabetes, glyburide, suppressed IAPP-mediated IL-1β production in vitro. Processing of IL-1β initiated by IAPP first required priming, a process that involved glucose metabolism and was facilitated by minimally oxidized low-density lipoprotein. Finally, mice transgenic for human IAPP had more IL-1β in pancreatic islets, which localized together with amyloid and macrophages. Our findings identify previously unknown mechanisms in the pathogenesis of type 2 diabetes and treatment of pathology caused by IAPP.
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“that induce interleukin (IL)-1β release to recruit macrophages and enhance local islet inflammation ( 45 ).”
From β-Cell Failure in Type 2 Diabetes: Postulated Mechanisms and Prospects for Prevention and Treatment (2014) · cites this paper as [45]
Experimental — accuracy not yet measuredIn the citing paper
“A potential role for NLRP3 in promoting elevated levels of IL-1β in type 2 diabetes was also implied by the observation of NLRP3-dependent IL-1β secretion by mouse bone marrow-derived macrophages and dendritic cells in response to islet amyloid polypeptide (IAPP), which is deposited in the pancreas and associated with loss of β-cell function in type 2 diabetes61.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [61]
In the citing paper
“Interestingly, the anti-diabetic drug glyburide (Glibenclamide; Roche/Sanofi-Aventis) has been shown to block glucose-mediated secretion of IL-1β by mouse pancreatic islets62, as well as IL-1β production by macrophages in response to IAPP61, and NLRP3-deficient mice were more glucose tolerant than wild-type mice62.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [61]
In the citing paper
“In a separate study, no differences in IL-1β secretion were observed between wild-type and TXNIP-deficient bone marrow-derived macrophages in response to several NLRP3 stimuli, including MSU crystals and ATP61.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [61]
In the citing paper
“However, the role of TXNIP and ROS in NLRP3 activation has been challenged.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [61]
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“Inflammasome activation in human-type diabetes Possible role of NLRP3 in human T2D also has been suggested in experiments showing the capability of human-type islet amyloid polypeptide (hIAPP) to activate NLRP3 inflammasome (29), which could be mechanistically similar to the NLRP3 activation by fibrillar Aβ oligomer (…”
BackgroundAbedini, A., Derk, J., & Schmidt, A. M. (2018) · Protein Science · doi:10.1002/pro.3425 · Cited by 25
Molli, A. E. I., Bergonzi, M. F., Spalvieri, M. P., Linari, M. A., Frechtel, G. D., & Cerrone, G. E. (2020) · Scientific Reports · doi:10.1038/s41598-020-66751-x · Cited by 25
The role of pyroptosis in metabolism and metabolic disease
Zheng, Z., Yang, S., Dai, W., Xue, P., Sun, Y., Wang, J., Zhang, X., Jiang, L., & Kong, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116863 · Cited by 28
Liu, F., Qu, H., Li, Y., Tang, Q. J., Yang, Z., Wang, H., & Deng, H. (2015) · Endocrine Journal · doi:10.1507/endocrj.ej15-0212 · Cited by 24
Amyloid fibrils activate B-1a lymphocytes to ameliorate inflammatory brain disease
Kurnellas, M. P., Ghosn, E., Schartner, J., Baker, J., Rothbard, J. J., Negrin, R. S., Herzenberg, L., Fathman, C., Steinman, L., & Rothbard, J. (2015) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1521206112 · Cited by 23
Duff, O., Walsh, D. M. J., Gill, S. M., McDermott, L., Furlong, B., O'Connor, N. E., Moran, K., & Woods, C. B. (2018) · JMIR Formative Research · doi:10.2196/formative.9550 · Cited by 23
Molecular biology of autoinflammatory diseases
Masumoto, J., Zhou, W., Morikawa, S., Hosokawa, S., Taguchi, H., Yamamoto, T., Kurata, M., & Kaneko, N. (2021) · Inflammation and Regeneration · doi:10.1186/s41232-021-00181-8 · Cited by 26
Li, B., Liu, Y., Zhang, L., Guo, X., Wen, C., Zhang, F., Luo, X., & Xia, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202100695rr · Cited by 24
Inflammasomes: a rising star on the horizon of COVID-19 pathophysiology
Wang, M., Yu, F., Chang, W., Zhang, Y., Zhang, L., & Li, P. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1185233 · Cited by 25
Huang, S., Zhao, L., Hong, C., Duo, C.-C., Guo, B., Zhang, L.-J., Gong, Z., Xiong, S., Gong, F., & Gao, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064951 · Cited by 24
Alvarado, R., O’Brien, B. A., Tanaka, A., Dalton, J. P., & Donnelly, S. (2014) · Immunobiology · doi:10.1016/j.imbio.2014.11.008 · Cited by 24
“…identified to date, inhibition of cathepsin B activty, or lysosomal acidification per se, prevents the activation of the lrp3 inflammasome, even in the presence of lysosomal rupture Gaide and Hoffman, 2008; Hornung et al., 2008; Hornung and Latz, 010; Masters et al., 2010; Rajamaki et al., 2010).”
BackgroundThe human serum protein C4b-binding protein inhibits pancreatic IAPP-induced inflammasome activation
Kułak, K. B., Westermark, G. T., Papac-Miličević, N., Renström, E., Blom, A. M., & King, B. C. (2017) · Diabetologia · doi:10.1007/s00125-017-4286-3 · Cited by 24
“Islet amyloid polypeptide (IAPP), which is co-secreted with insulin [5], forms oligomers that induce inflammasome activation [6].”
BackgroundNeuroprotective Effects of Amylin Analogues on Alzheimer’s Disease Pathogenesis and Cognition
Grizzanti, J., Corrigan, R. R., & Casadesús, G. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180433 · Cited by 24
Compound C Protects Mice from HFD-Induced Obesity and Nonalcoholic Fatty Liver Disease
Wang, F., Liu, Y., Yuan, J., Yang, W., & Mo, Z. (2019) · International Journal of Endocrinology · doi:10.1155/2019/3206587 · Cited by 24
“In this aspect, it is interesting to note that compound C reduces the inflammatory gene expression in the liver, including IL-1β, IL-18, IL-6, and TNF-α.”
BackgroundInfluentialJensen, D. M., Hendricks, K. V., Mason, A. T., & Tessem, J. S. (2020) · Metabolites · doi:10.3390/metabo10120485 · Cited by 24
Role of the AMP kinase in cytokine-induced human EndoC-βH1 cell death
Fred, R. G., Krizhanovskii, C., Ameur, A., Cen, J., Bergsten, P., Ravassard, P., Scharfmann, R., & Welsh, N. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.07.015 · Cited by 24
Mao, Y., Liu, J., Han, B., & Wang, L. (2019) · Medical Science Monitor · doi:10.12659/msm.913788 · Cited by 23
“The pathogenesis of T2D is closely associated with inflammatory processes, and cellular stress which may cause T2D which also induces or exacerbates inflammatory responses [46].”
BackgroundChen, Y., Zhou, Y., Deng, B., Wu, D., Quan, Y., & Min, Z. (2020) · Oncology Reports · doi:10.3892/or.2020.7475 · Cited by 23
“response, and is involved in a variety of cellular activities, including cell proliferation, differentiation and apoptosis (5).”
BackgroundVinaik, R., Barayan, D., & Jeschke, M. G. (2020) · Endocrinology · doi:10.1210/endocr/bqaa116 · Cited by 23
Jiao, J., Wang, Z., Guo, Y., Liu, J., Huang, X., Ni, X., Gao, D., Sun, L., Zhu, X., Zhou, Q., et al. (2021) · PeerJ · doi:10.7717/peerj.12384 · Cited by 26
“The IL-1B (-511) and IL-1RN (VNTR) polymorphisms have been reported to be related to the pathogenesis of T2DM (Ehses et al., 2009; Masters et al., 2010), and many case-control studies have illustrated the association of IL-1B (-511) and IL-1RN (VNTR) polymorphisms with T2DM risk.”
BackgroundWang, J.-W., Xiu-ying, Y., Wei, N., Wu, S.-S., Zhang, Z., Luo, G.-H., Li, X., Li, J., & Cao, H. (2022) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000006117 · Cited by 23
King, B. C., & Blom, A. M. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.12.009 · Cited by 23
“It has been identified that islet amyloid polypeptide (IAPP) is able to act as an inflammasome activator (Masters et al., 2010).”
BackgroundRibeiro, I. S., Pereira, Í. S., dos Santos, D. P., Lopes, D. N., Prado, A. O., Calado, S. P. D. M., Gonçalves, C. V., Galantini, M. P. L., Muniz, I. P. R., dos Santos, G. G. A., et al. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110734 · Cited by 25
Witkowski, A., Carta, S., Lu, R., Yokoyama, S., Rubartelli, A., & Cavigiolio, G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005663 · Cited by 22
Alpha1-antitrypsin ameliorates islet amyloid-induced glucose intolerance and β-cell dysfunction
Rodríguez‐Comas, J., Moreno‐Vedia, J., Obach, M., Castaño, C., Pablo, S., Alcarraz‐Vizán, G., Díaz-Catalán, D., Mestre, A., Horrillo, R., Costa, M., et al. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.100984 · Cited by 22
T cells accumulate in non-diabetic islets during ageing
Denroche, H. C., Miard, S., Sallé-Lefort, S., Picard, F., & Verchere, C. B. (2021) · Immunity & Ageing · doi:10.1186/s12979-021-00221-4 · Cited by 25
RhoGTPases and inflammasomes: Guardians of effector-triggered immunity
Dufies, O., & Boyer, L. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009504 · Cited by 24
Cholesterol, Inflammasomes, and Atherogenesis
Ordovás, J. M., & Ordovás-Montañés, J. (2011) · Current Cardiovascular Risk Reports · doi:10.1007/s12170-011-0212-2 · Cited by 22
Metadata
- Authors
- Masters, S. L., Dunne, A., Subramanian, S. L., Hull, R. L., Tannahill, G. M., Sharp, F. A., Becker, C., Franchi, L., Yoshihara, E., Chen, Z., Mullooly, N., Mielke, L. A., Harris, J., Coll, R. C., Mills, K. H. G., Mok, K. H., Newsholme, P., Nuñez, G., Yodoi, J., Kahn, S. E., Lavelle, E. C., & O'Neill, L. A. J.
- Affiliations
- Trinity College Dublin (IE)
- University of Washington (US)
- University of Michigan (US)
- Kyoto University (JP)
- University College Dublin (IE)
- Corresponding author
- Masters, Seth L
- ORCID
- Venue
- Nature Immunology
- Published
- 2010-09-12
- Volume
- 11
- Issue
- 10
- Pages
- 897-904
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- PMC
- PMC3103663
- OpenAlex
- W2034946303
- Cited by
- 1,330
- References
- 55
- Citations by year
- 2026: 58 · 2025: 57 · 2024: 64 · 2023: 75 · 2022: 71 · 2021: 99 · 2020: 100 · 2019: 95 · 2018: 82 · 2017: 83 · 2016: 73 · 2015: 101 · 2014: 95 · 2013: 112 · 2012: 83
- FWCI
- 35.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion, other-oa)
- eSpace (Curtin University) (submittedVersion)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI063331, R56AI063331, R01AI063331, R37AI063331)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-75998, R01DK075998)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Diabetes and associated disorders
- Keywords
- NLRP3 inflammasome, amylin, IL-1β, type 2 diabetes, beta cell destruction, glibenclamide, LDL oxidation, glucose metabolism, inflammasome priming, pancreatic islets, macrophages, amyloid deposition
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Amyloid, Animals, Carrier Proteins, Cells, Cultured, Dendritic Cells, Diabetes Mellitus, Type 2, Glyburide, Humans, Hypoglycemic Agents, Islets of Langerhans, Macrophages, Mice, Inbred C57BL, Mice, Transgenic, Receptors, Cytoplasmic and Nuclear, Mice, Rats, Interleukin-1beta, Islet Amyloid Polypeptide
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