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Investigation of the role of NLRP13 in cell death

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dc.contributor Graduate Program in Molecular Biology and Genetics.
dc.contributor.advisor Özören, Nesrin.
dc.contributor.author Çakır, Elif Öykü.
dc.date.accessioned 2024-03-12T14:59:21Z
dc.date.available 2024-03-12T14:59:21Z
dc.date.issued 2022
dc.identifier.other BIO 2022 C34
dc.identifier.uri http://digitalarchive.boun.edu.tr/handle/123456789/21477
dc.description.abstract NLRP13 is an intracellular protein that is included in the NOD- like receptor family. It contains the N-terminal pyrin domain, central NOD domain, and leucine-rich repeats, LRR at C terminus. Stably NLRP13 expressing THP-1 cells induced a higher pro-inflammatory response upon LPS/ATP treatment and P. Aeruginosa infection. Moreover, the activation of procaspase-8 is relatively increased in the stably NLRP13 expressing THP-1 cell. NLRP13 can interact with caspase-8 according to Co-IP results. Besides these, NLRP3 inflammasome components are significantly higher in the stably NLRP13 expressing THP-1 cells upon inflammasome activation. This thesis study aimed to investigate whether NLRP13 has a role in cell death via the caspase-8 activation complex after inflammasome activation. To elucidate this, Annexin V-PI staining and LDH release assay were performed after pyroptosis induction via inflammasome activation.No significant difference was observed between stably NLRP13 expressing THP-1 cells and control cells. Furthermore, Gasdermin D cleavage was shown to be similar for each group while PARP-1 cleavage in stably NLRP13 expressing THP-1 cells was slightly higher than control. The experiments were repeated after caspase-8 was inhibited. There was no significant difference in Annexin V-PI staining, LDH release assay, and gasdermin D cleavage. However, PARP-1 cleavage was slightly decreased in stably NLRP13 expressing THP-1 cells when caspase-8 was inhibited.It was shown that NLRP13 is not involved directly in pyroptosis via induction of the caspase-8 activation complex; however, it could be involved in the molecular switch mechanism between apoptosis and pyroptosis with the caspase-8 activation complex.
dc.format.extent 111:001:PDF:b2795719:038417:0:0:0:0:0:0tFull text electronic versionvn
dc.publisher Thesis (M.S.) - Bogazici University. Institute for Graduate Studies in Science and Engineering, 2022.
dc.subject.lcsh Cell death.
dc.subject.lcsh Inflammation -- Mediators.
dc.title Investigation of the role of NLRP13 in cell death
dc.format.pages xvi, 53 leaves


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