Subcellular localization and functional characterization of paraneoplastic Ma Antigen 3 (PNMA3)
PNMA (Paraneoplastic Ma Antigens) family consists of nineteen family members that are encoded by human genome (Pang et al., 2018). Gene expression studies showed that many of the family members are expressed in human brain and testes tissues. Furthermore, subset of the family members were reported t...
Saved in:
| Main Author: | |
|---|---|
| Format: | Thesis |
| Published: |
2023
|
| Subjects: | |
| Online Access: | http://eprints.sunway.edu.my/2425/ |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | PNMA (Paraneoplastic Ma Antigens) family consists of nineteen family members that are encoded by human genome (Pang et al., 2018). Gene expression studies showed that many of the family members are expressed in human brain and testes tissues. Furthermore, subset of the family members were reported to show abberant protein expression in tumors, including PNMA1, 2 and 3 proteins which have been found to express in breast, lung, and testicular cancers (Dalmau et al., 1999; Schüller et al., 2005) that are associated with Paraneoplastic Disorder in which the patients developed neurological conditions such as limbic, hypothalamic, and brainstem encephalitis. Other than their association with Paraneoplastic Disorder, the physiological functions of the PNMA family members remain elusive. However, few members of the PNMA family are known to be involved in the regulation of apoptosis signaling pathway. Among the family members that are known to positively regulate the apoptosis process are PNMA1, PNMA4 and PNMA5. In contrast, PNMA2 has been shown to be able to inhibit the apoptotic activity of PNMA4. However, the physiological function of PNMA3 remains unclear although bio-informative analysis has identified the presence of C2HC zinc finger domain at C-terminus of PNMA3 unique only to PNMA3 and not to the other PNMA family. In order to investigate the physiological function of PNMA3, the research project focuses on the cloning and expression of PNMA3 to determine the impact of overexpressed PNMA3 on cancer cells. Results from this investigation showed that PNMA3 similar to PNMA2 promotes cell viability and also its nuclear localization through the presence of a nucleus Socalization domain found at C-terminus of PNMA3 similar to that found on PNMA5. Interaction studies also have shown self-dimerization of PNMA3 which was prevalent in other PNMA families such as PNMA4 and PNMA5. Our interaction studies also identified the interaction of PNMA3 with PNMA2 and PNMA5 and we observed an increase in cell viability of PNMA2 and PNMA5 when co-transfected with PNMA3. |
|---|