Protein-protein interactions with and within the NLRP3 inflammasome : Evidence from STRING and literature studies

University essay from Högskolan i Skövde/Institutionen för biovetenskap

Author: Ralph Monte; [2020]

Keywords: ;

Abstract: Inflammasomes are multiprotein complexes that play a role in the innate immune system. One inflammasome is the NLRP3 inflammasome, which can be activated and primed by different stimuli that bind to pattern recognition receptors (PRRs). There are many theories of how the NLRP3 inflammasome can be regulated, one of which is deubiquitination by deubiquitinating enzymes (DUBs). The NLRP3 inflammasome is also involved in many diseases, for example, diabetes, cancer and neurodegenerative diseases. The main aim of this study is to increase knowledge of the protein-protein interactions with and within the NLRP3 inflammasome. Thus, this study will give further insight into NLRP3 inflammasome pathways and can lead to novel treatment targets for different NLRP3-associated diseases in the future. The NLRP3 inflammasome and its regulation were described in this study and protein-protein interaction (PPI) networks of the individual NLRP3 inflammasome key components (NLRP3, PYCARD, caspase-1) were obtained from STRING for human, mouse and macaque orthologs. The obtained PPI networks were then compared. The types of PPI in all PPI networks, either functional or physical, were verified by KEGG or research literature, respectively. Mass spectrometry data of unstimulated and stimulated THP-1 cells were also analyzed. During this study the BRISC complex and its members, a DUB, was also further explored. All in all, the study increased the knowledge about the protein-protein interactions with and within the NLRP3 inflammasome. Further research can aid in the discovery of novel treatment targets of diseases related to inflammasomes.

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