Limits...
Modulator of apoptosis 1 (MOAP-1) is a tumor suppressor protein linked to the RASSF1A protein.

Law J, Salla M, Zare A, Wong Y, Luong L, Volodko N, Svystun O, Flood K, Lim J, Sung M, Dyck JR, Tan CT, Su YC, Yu VC, Mackey J, Baksh S - J. Biol. Chem. (2015)

Bottom Line: It is an integral partner to the tumor suppressor protein, Ras association domain family 1A (RASSF1A), and functions to activate the Bcl-2 family pro-apoptotic protein Bax.Although RASSF1A is now considered a bona fide tumor suppressor protein, the role of MOAP-1 as a tumor suppressor protein has yet to be determined.Overexpression of MOAP-1 in several cancer cell lines resulted in reduced tumorigenesis and up-regulation of genes involved in cancer regulatory pathways that include apoptosis (p53, Fas, and MST1), DNA damage control (poly(ADP)-ribose polymerase and ataxia telangiectasia mutated), those within the cell metabolism (IR-α, IR-β, and AMP-activated protein kinase), and a stabilizing effect on microtubules.

View Article: PubMed Central - PubMed

Affiliation: From the Departments of Biochemistry and.

Show MeSH

Related in: MedlinePlus

Protein expression of MOAP-1 in the indicated cancer cell lines (A–C). ERK1/2 is shown as a loading control for the lanes, and all lanes marked withan asterisk are normal cells. IB, immunoblot. Two forms of MOAP-1 can be observed blood cancers that migrate at ∼46 kDa instead of the normal 39 kDa. This result has been confirmed using the rabbit anti-MOAP-1 (from QED Biosciences) and rabbit anti-MOAP-1 from Sigma as indicated (B, right side).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4591801&req=5

Figure 3: Protein expression of MOAP-1 in the indicated cancer cell lines (A–C). ERK1/2 is shown as a loading control for the lanes, and all lanes marked withan asterisk are normal cells. IB, immunoblot. Two forms of MOAP-1 can be observed blood cancers that migrate at ∼46 kDa instead of the normal 39 kDa. This result has been confirmed using the rabbit anti-MOAP-1 (from QED Biosciences) and rabbit anti-MOAP-1 from Sigma as indicated (B, right side).

Mentions: In addition to detectable expression of MOAP-1 in NHBE, hTERT (immortalized with human telomerase), and MCF-10A, we can also detect MOAP-1 in other nontransformed cell lines such as HEMA-LP and PNT1A (Fig. 3, A–C). MOAP-1 protein was reduced or absent in many cancer cells as shown in Figs. 2D and 3. Noticeably, MOAP-1 expression was detected in the p53-positive cell lines (U2OS, HCT116, ZR-75, IMR-32, and PANC1) but was reduced/absent in p53- cells (SAOS-2 and SKOV3), p53 frameshift mutation or rearrangement cell lines (Caco-2 and CAPAN-2), and p53-mutant cell lines (SKBR3, MDA-MB-468, MDA MB-231,BT-549, and BT-20 (breast cancer cells) (Fig. 2D), and OVCAR-3 (ovarian cancer). However, the expression of MOAP-1 did not always correlate with the status of p53 as SW480 (p53-) has detectable MOAP-1, whereas the p53 wild type cell lines, A549, and the majority of the neuroblastoma cell lines do not have robust detection of MOAP-1. Among the cell lines that are p53+/+MOAP-1−/−, all have epigenetic silencing of RASSF1A (12). Therefore, we suspect that RASSF1A may influence the expression of MOAP-1, and we are currently exploring this unexpected observation. The dual loss of MOAP-1 and RASSF1A expression may contribute to malignant cell growth in the solid cancers.


Modulator of apoptosis 1 (MOAP-1) is a tumor suppressor protein linked to the RASSF1A protein.

Law J, Salla M, Zare A, Wong Y, Luong L, Volodko N, Svystun O, Flood K, Lim J, Sung M, Dyck JR, Tan CT, Su YC, Yu VC, Mackey J, Baksh S - J. Biol. Chem. (2015)

Protein expression of MOAP-1 in the indicated cancer cell lines (A–C). ERK1/2 is shown as a loading control for the lanes, and all lanes marked withan asterisk are normal cells. IB, immunoblot. Two forms of MOAP-1 can be observed blood cancers that migrate at ∼46 kDa instead of the normal 39 kDa. This result has been confirmed using the rabbit anti-MOAP-1 (from QED Biosciences) and rabbit anti-MOAP-1 from Sigma as indicated (B, right side).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4591801&req=5

Figure 3: Protein expression of MOAP-1 in the indicated cancer cell lines (A–C). ERK1/2 is shown as a loading control for the lanes, and all lanes marked withan asterisk are normal cells. IB, immunoblot. Two forms of MOAP-1 can be observed blood cancers that migrate at ∼46 kDa instead of the normal 39 kDa. This result has been confirmed using the rabbit anti-MOAP-1 (from QED Biosciences) and rabbit anti-MOAP-1 from Sigma as indicated (B, right side).
Mentions: In addition to detectable expression of MOAP-1 in NHBE, hTERT (immortalized with human telomerase), and MCF-10A, we can also detect MOAP-1 in other nontransformed cell lines such as HEMA-LP and PNT1A (Fig. 3, A–C). MOAP-1 protein was reduced or absent in many cancer cells as shown in Figs. 2D and 3. Noticeably, MOAP-1 expression was detected in the p53-positive cell lines (U2OS, HCT116, ZR-75, IMR-32, and PANC1) but was reduced/absent in p53- cells (SAOS-2 and SKOV3), p53 frameshift mutation or rearrangement cell lines (Caco-2 and CAPAN-2), and p53-mutant cell lines (SKBR3, MDA-MB-468, MDA MB-231,BT-549, and BT-20 (breast cancer cells) (Fig. 2D), and OVCAR-3 (ovarian cancer). However, the expression of MOAP-1 did not always correlate with the status of p53 as SW480 (p53-) has detectable MOAP-1, whereas the p53 wild type cell lines, A549, and the majority of the neuroblastoma cell lines do not have robust detection of MOAP-1. Among the cell lines that are p53+/+MOAP-1−/−, all have epigenetic silencing of RASSF1A (12). Therefore, we suspect that RASSF1A may influence the expression of MOAP-1, and we are currently exploring this unexpected observation. The dual loss of MOAP-1 and RASSF1A expression may contribute to malignant cell growth in the solid cancers.

Bottom Line: It is an integral partner to the tumor suppressor protein, Ras association domain family 1A (RASSF1A), and functions to activate the Bcl-2 family pro-apoptotic protein Bax.Although RASSF1A is now considered a bona fide tumor suppressor protein, the role of MOAP-1 as a tumor suppressor protein has yet to be determined.Overexpression of MOAP-1 in several cancer cell lines resulted in reduced tumorigenesis and up-regulation of genes involved in cancer regulatory pathways that include apoptosis (p53, Fas, and MST1), DNA damage control (poly(ADP)-ribose polymerase and ataxia telangiectasia mutated), those within the cell metabolism (IR-α, IR-β, and AMP-activated protein kinase), and a stabilizing effect on microtubules.

View Article: PubMed Central - PubMed

Affiliation: From the Departments of Biochemistry and.

Show MeSH
Related in: MedlinePlus