Thesis

Novel Role of Pellino1 Ubiquitin Ligase in B Cell Lymphoma

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Ubiquitination is a post translational modification (PTM) process that plays a role in protein
degradation by the addition of ubiquitin groups to target protein. In the ubiquitination process, E3
ubiquitin ligase is responsible to mediate the bridge between E2 ubiquitin-conjugating enzymes and
substrate for ubiquitin conjugation. Pellino1 or PELI1, one of the ubiquitin ligases, was found to
reduce antigen uptake in the adaptive immune system. PELI1 also has been associated with the
progression of Burkitt Lymphoma (BL), the most aggressive B cell non-Hodgkin lymphoma. However,
the exact role of PELI1 in the BL remains unclear. Thus, this project aims to investigate the role of
PELI1 in BL. PELI1 knockout and control Ramos cell line were treated with antigen to determine the
level of Syk signaling activation level using western blot and phosflow. The oxygen consumption rate
of PELI1 was quantified in PELI1 knockout and control Ramos cell line using three drugs for
mitochondrial inhibitors, Oligomycin, FCCP, and Rotenone. Furthermore, calcium flux analysis was
performed in PELI1 knockout and control Ramos cell line by the addition of FuraRed as the calcium
dyes and antigen for triggering the calcium influx. As a result, PELI1 knockout cells show non
significant changes in the level of Syk activation level. PELI1 knockout cells show significant changes in
oxygen consumption rate of the cells and calcium flux of the cells. This finding suggests that PELI1 has
a regulatory role in metabolism as well as calcium ions in the cells.

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Availability

Detail Information

Series Title

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Call Number

BM 23-002

Publisher

i3L, Jakarta : i3L, Jakarta., 2023

Collation

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Language

English

ISBN/ISSN

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Classification

NONE

Content Type

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Media Type

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Carrier Type

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Edition

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Subject(s)

PELI1
E3 Ubiquitin Ligase
Burkitt Lymphoma

Specific Detail Info

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Statement of Responsibility

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