In tumors, certain genes related to proliferation
and invasion are upregulated in expression (1). In neurodegenerative diseases, there
are also a bulk of genes with abnormal expression, including genes
related to the autophagy-lysosomal pathway (2). These abnormally expressed genes may
not only serve as biomarkers for disease diagnosis, but also as
targets for treatment. Human endogenous retroviruses (HERVs) are
derived from ancient retroviruses, which infect and insert viral
genes into germline cells. HERVs constitute an estimated 8% of the
human genome (3). In general, a
complete HERV includes 5′ long terminal repeats (5′ LTR), a
primer-binding site, group-specific antigen gene (gag), a protease
gene, a polymerase gene (pol), an envelope gene and 3′ LTR elements
(4). Paternally expressed imprinted
gene 10 (PEG10) is an evolutionarily conserved HERV gene (5) belonging to the Ty3/Gypsy family of
retrotransposons. Evolutionarily, PEG10 is a therian-specific gene
(6,7), and differentially methylated regions
of PEG10 have emerged in the therian ancestor at least 160 million
years ago (8). During the evolution
of the placenta in mammals, PEG10 was inserted into the genome, as
it exists in marsupials but not in egg-laying monotreme species
(9). PEG10 is a paternally
expressed imprinting gene, which was reported to be located at
human chromosome 7q21 in 2001 for the first time (7). Importantly, PEG10 can be used for RNA
delivery (10–13). As an imprinting gene, PEG10 is
crucial for placental development and plays a key role in mouse
embryonic stem cell and trophoblast stem cell differentiation
(14–16). Ono et al (17) have reported that PEG10 maintains
placental function, and deletion of PEG10 in mice can lead to
embryonic lethality. Traditionally, PEG10 expression is limited to
the testes, adrenal gland and skin after adulthood (18). During the past few years, knowledge
of PEG10 being highly expressed in tumors and neurodegenerative
diseases has emerged. Thus, the present article reviewed the recent
findings on the roles of PEG10 in these diseases.
PEG10 contains 2 overlapping open reading frames
(RF1 and RF1/2), and the mRNA of PEG10 utilizes a typical
retroviral frameshift mechanism to encode two proteins: RF1
(encoding gag-like protein) and RF1/2 (encoding gag-pol-like
polyprotein) (19,20). The frameshifting efficiency of PEG10
is ~22% (19) and a study has
identified that the frameshift of PEG10 can be suppressed by a
small-molecule compound (21). The
ribosomal frameshift element of PEG10 consists of ‘slippery’ and
‘pseudoknot’. The slippery sequence is GGGAAAC, while pseudoknot is
composed of multiple stem-loop structures. When ribosomes encounter
the pseudoknot, the A- and P-site tRNAs detach from the zero frame
codons GGA-AAC, shifting back one nucleotide to GGG-AAA, causing
the original encoding of glycine-asparagine to change to
glycine-lysine (22). PEG10 has
multiple evolutionary conserved functional domains, including a
coiled-coil domain, retrotransposon-gag domain, retrovirus zinc
finger-like domain, retroviral asparytyl protease domain and
reverse transcriptase domain (5,7,23–26).
The structure of PEG10 is shown in Fig.
1.
LncRNA is a type of ncRNA with a length exceeding
200 nucleotides. LncRNAs are involved in the occurrence,
development and progression of cancer. PEG10 is an upregulated
lncRNA in patients with lymphoma (27). In diffuse large B-cell lymphoma
(DLBCL), lncRNA PEG10 inhibits microRNA (miR)-101-3p, while
miR-101-3p inhibits kinesin family member 2A (KIF2A). Therefore,
overexpression of PEG10 leads to an increase in KIF2A expression,
promoting DLBCL growth (28,29).
LncRNA PEG10 inhibits miR-449a, increases ribosomal protein S2
expression and increases the proliferation, invasion and migration
of neuroblastoma cells (30).
LncRNA PEG10 and H19 are mutual upstream and downstream regulatory
factors, and PEG10 levels are constitutively associated with a high
lymph node ratio in gastric cancer (31). Furthermore, knockout of PEG10 causes
an increase in miR-3200 and inhibits the proliferation, migration
and invasion of gastric cancer cells (32) and glioma cells (33). LncRNA PEG10 inhibits miR-33a in
melanoma, thus inhibiting the PI3K/AKT and mTOR pathways (34). Furthermore, overexpression of lncRNA
PEG10 also has an essential role in promoting proliferation and
invasion in esophageal cancer cells (35) and hypopharyngeal squamous cell
carcinoma (36).
PEG10 contains 2 overlapping open reading frames,
RF1 and RF2. During embryonic development, PEG10-RF1 and
PEG10-RF1/2 proteins are expressed at different stages, suggesting
that PEG10-RF1 and PEG10-RF1/2 may have different functions.
PEG10-RF1/2 have an aspartate protease domain and new fragments can
be generated through self-cutting (19,22).
PEG10 is found in multiple cellular components, including the
nucleus (24), extracellular
vesicles and stress granules (25).
PEG10-RF1 has nuclear and cytoplasmic localization and does not
enter stress granules under stress conditions. However, PEG10-RF1/2
is only localized in the cytoplasm and enters stress granules under
stress conditions (25). PEG10-RF1
contains a retroviral zinc finger domain and is considered a
transcription factor, regulates the transcription of genes
participates in the progression of cancers and neurodegenerative
diseases; these genes include C9orf72-SMCR8 complex subunit,
doublecortin like kinase 1, plexin A4, semaphorin 5B, slit guidance
ligand 3 and Wnt family member 3A (24).
In addition, PEG10 is a secreted protein produced by
Dental-derived mesenchymal stem cells and bone marrow stem cells,
which is associated with adipose differentiation. PEG10 expression
is generally observed at the immediate early stage of adipocyte
differentiation (37).
The increase in PEG10 protein may be caused by
various ways, including DNA demethylation, gene duplication,
extended RNA half-life, transcriptional activation and inhibition
of protein degradation (Fig.
2).
In the mammalian genome, DNA methylation is an
important approach to govern gene expression (38,39).
DNA methylation usually inhibits gene expression by recruiting
repression proteins or inhibiting transcription factors to DNA. In
human parthenogenetic embryonic stem cells, activating
transcription factor 7 interacting protein increases PEG10
methylation and inhibits its transcription (40). In KrasG12D-induced T-cell
neoplasms, imprinting control regions (ICRs) of PEG10 are
significantly hypermethylated. Increased DNA methylation at the
ICRs of PEG10 is the earliest detectable change in lymphocytic
T-cell thymic lymphoma (41). Tet
methylcytosine dioxygenase 1 (TET1) is a maintenance DNA
demethylase, which promotes PEG10 expression by inhibiting DNA
methylation, and deleting TET1 results in an increase of
5-hydroxymethylcytosine in PEG10, leading to a decrease in PEG10
expression (42). Histone
methylation is another way to regulate PEG10 expression, and in
hepatocellular carcinoma (HCC), menin/mixed-lineage leukemia 1
(MLL) interaction inhibitor MI-503 prevents the display of the
menin-MLL1 complex from binding to the PEG10 promoter, reduces the
modification of trimethylated H3 lysine 4 in the promoter region
and inhibits PEG10 transcription (43).
Traditionally, gene amplification was identified as
one aspect of the genetic instability strongly associated with
malignantly transformed cells. Cancer cells use this mechanism to
mediate overexpression of certain oncogenes to promote
proliferation, anti-apoptosis and resistance to anticancer drugs
(44). For instance, genomic
amplification of PEG10 at the 7q21.3 locus was found in HCC samples
(45,46). In hepatitis B virus-associated HCC,
the increase in DNA copy number leads to an increased expression of
PEG10 (47).
The stability of mRNA plays an important role in the
control of gene expression (48).
PEG10 is a direct target of miRNA-574-5p (30). MiR-138-5p binds to the 3′UTR of
PEG10 mRNA, shortening the half-life of PEG10 mRNA (49). In regulating retinoblastoma (RB),
the circular RNA Circ:0075804 promotes PEG10 expression by
inhibiting miR-138-5p (49).
N6-methyladenosine residues on the PEG10 3′UTR are recognized and
bind by insulin like growth factor 2 mRNA binding protein 1 to
recruit poly (A) Binding Protein Cytoplasmic 1 and enhance the
stability of PEG10 mRNA, thereby increasing the protein content of
PEG10 (50). In neural progenitor
cells, TET3 increases the DNA methylation levels of PEG10 and
maintains neural stem cell identity (51). In HCC, miR-122 binds to the PEG10
3′UTR and inhibits PEG10 expression (52). LncRNA SNAI3 antisense RNA 1
increases PEG10 expression through competing endogenous RNA
spreading of miR-27a-3p and miR-34a-5p, thereby promoting cancer
cell proliferation (53). In human
colon cancer cells, miR-491 binds to the 3′UTR of PEG10 mRNA and
inhibits PEG10 expression (54). In
colorectal cancer, NOTCH1-associated lncRNA in T-cell acute
lymphoblastic leukemia 1 increases PEG10 expression to promote
tumor progression by sponging miR-574-5p (55).
Transcription factors can bind to the promoter
region of PEG10 and activate its transcription. Myc promotes
tumor-cell proliferation by activating PEG10 transcription
(56,57). In addition, the E2F family of
transcription factors (E2Fs) are transcription factors that promote
the transcription of PEG10 and thereby enhance the proliferation of
HCC cells (58). Glycogen synthase
kinase 3β can phosphorylate and activate E2F transcriptional factor
1 (E2F1). Phosphorylated E2F1 binds to ubiquitin specific peptidase
11, leading to reduced degradation of E2F1 due to deubiquitination.
E2F-1 has also been recently shown to be crucial for PEG10
activation in pancreatic cancer, and to further promote cell
proliferation, migration and invasion (59). Similarly, in HCC, the expression of
PEG10 is positively correlated with lymph node metastasis.
Overexpression of PEG10 promotes epithelial-mesenchymal transition,
and the expression of PEG10 is influenced by the transforming
growth factor β (TGF-β) signaling (60). Furthermore, transcription factor
CTR9 homolog, Paf1/RNA polymerase II complex component promotes
PEG10 transcription (61).
Although TGF-β promotes PEG10 expression in HCC
tissues, in other cancer tissues, the expression of PEG10 is
inhibited by TGF-β, e.g. in chondrosarcoma cells (62). Furthermore, the upregulated PEG10
activity in turn inhibits TGF-β and bone morphogenetic protein
signaling (63). The transcription
factor one cut homeobox 2 binds to the PEG10 promoter and increases
the mRNA levels of PEG10 in lethal prostate cancer (64,65),
and recent studies demonstrated that androgen receptor (AR)
inhibits the transcription of PEG10 (66–68).
RB inhibits PEG10 transcription by inhibiting E2F1 activity
(26,58). Interestingly, the expression of
PEG10 can be regulated by small molecule compounds. For instance,
curcumin inhibits the expression of PEG10 in an unknown mechanism,
thereby inhibiting the growth of breast cancer cells (69). Exposure to cadmium (Cd) can cause a
decrease in the expression of Cd-exposed placentas PEG10 (70).
PEG10 has a C-terminal polyproline repeat domain,
which may be recognized by human ubiquilin 2 (UBQLN2) and
facilitates its proteasomal degradation (24,71).
The deficiency of UBQLN2 leads to an increase in PEG10 protein.
Furthermore, the ubiquitin protein ligase E3A (UBE3A) is another
PEG10 regulating gene. UBE3A inhibits the expression of PEG10 via
the proteasome (25)
Nuclear localized PEG10 functions as a transcription
factor, mediating the transcription of numerous downstream target
genes. Kruppel-like factor 2 (KLF2) is an inhibitory factor of
NF-κB and PEG10 activates NF-κB signaling by inhibiting KLF2
expression (23). Upregulated PEG10
expression activates NOTCH signaling and promotes metastatic cancer
stem cell self-renewal (72). PEG10
was reported to bind to TGF-β receptor ALK1 and to inhibit ALK1 as
well as ALK5 signaling (73). In
HCC, TSG101 binds to PEG10 to prevent its degradation, thereby
enhancing PEG10 expression and downstream target genes p53, p21 and
matrix metalloproteinases (MMPs), leading to cell proliferation,
invasion and migration (74). After
overexpression of PEG10 in human colon cancer cells, the
Wnt1/β-catenin pathway is activated, promoting cell proliferation
and inhibiting cell apoptosis (54). In Burkitt's lymphoma cells, PEG10
promotes tumor cell invasion and metastasis by upregulating the
expression of MMP-2 and −9 (18,26,59,75).
PEG10 promotes the proliferation of endometrial cancer cells by
inhibiting the transcription of p16 and p18 genes. PEG10 tends to
bind to the TGGGAYTACA and CTCNGCCTCC motifs (50). Of note, it was recently found that
PEG10 is an RNA binding protein, promoting trophoblast stem cell
differentiation into placental lineages (14).
PEG10 is considered an oncogene and PEG10 protein
has been found to be significantly increased in various cancer
types to date. Exogenous PEG10 expression leads to increased
cellular proliferation and increased cell viability (76).
The relationship between PEG10 and cancer was first
studied in liver cancer. PEG10 is strongly expressed in HCC
(77). A machine learning study
found that PEG10 is highly expressed in patients unresponsive to
transarterial chemotherapy (78).
Expression of PEG10 is significantly correlated with poor survival
and tumor recurrence in HCC, making PEG10 an independent predictor
of early recurrence of HCC (79).
However, other studies found that PEG10 has an inhibitory effect on
tumor cell growth by activating immune response. For instance,
transduction of dendritic cells with PEG10 recombinant adenovirus
induced anti-tumor immunity against HCC (80). Another study also identified that
androgens activate PEG10 (81).
Thereby, PEG10 is the potential biomarker of HCC (82,83).
An increase in PEG10 content is closely related to
the prognosis of lung cancer; therefore, PEG10 is a diagnostic and
prognostic gene for lung adenocarcinoma and squamous cell carcinoma
(84). E2Fs activate MMPs by
upregulating PEG10, leading to lung cancer progression, prognosis
and metastasis (85,86). E2F1 activates PEG10 gene
transcription, promoting proliferation of lung epithelial cells
(87). Furthermore, transcription
termination factor 1 activates receptor tyrosine kinase like orphan
receptor 1 (ROR1), which activates PEG10 transcription. Inhibition
of ROR1 by small inhibitory (si)RNA in the human lung cancer cell
line PC-9 leads to a decrease in the transcription level of PEG10
(88). On the contrary, the
expression of PEG10 is also inhibited by certain transcription
factors. The expression of PEG10 is inhibited by PI3K/AKT, which
leads to a decrease in PEG10 protein levels in lung cancer cells
(89).
The expression of PEG10 in prostate cancer is
usually suppressed, as AR inhibits the transcription of PEG10
(26). However, during the
treatment of prostate cancer, AR inhibitors drive cancer cells to
evolve into neuroendocrine prostate cancer (NEPC) and the
expression of PEG10 gradually increases during the transition from
adenocarcinoma to NEPC. Therefore, PEG10 can be used as a
predictive indicator for biochemical recurrence of prostate cancer
(90). As a characteristic gene of
NEPC, silencing PEG10 inhibits the in vitro growth of
prostate cancer cells (91). In AR
activated adenocarcinoma type prostate cancer, full-length RF1/2 is
the dominant form, while in NEPC cells, RF1 and RF1/2 are both
highly expressed (26). Full-length
PEG10 (RF1/2) drive the proliferation of NEPC, while short-length
PEG10 (RF1) promotes invasion (26). The expression of PEG10 is associated
with short survival of patients with prostate adenocarcinoma
(92). Importantly, studies have
highlighted the crucial role of PEG10 in promoting the malignant
transformation of the highly lethal AR-negative phenotype prostate
cancer (93). Silencing PEG10
reduced the expression of neuroendocrine markers and inhibited cell
proliferation (94).
Driven by genomic gains and promoter demethylation,
PEG10 is highly expressed and is associated with poor patient
prognosis in mycosis fungoides-large-cell transformation (23). Furthermore, PEG10 overexpression was
observed in B-cell acute lymphoblastic leukemia and B-cell chronic
lymphocytic leukemia (95,96). Reducing PEG10 expression leads to a
decrease in cell volume and a weakened colony-formation ability in
large transformed cutaneous T-cell lymphoma cells; consequently,
PEG10 inhibition may be a promising treatment for advanced invasive
T-cell lymphoma (23). In thymoma,
the DNA methylation level of the promoter region of PEG10 is higher
than that of T-cell lymphoblastic leukemia (97,98).
Abnormal DNA methylation in PEG10 ICRs is expected to become a
prognostic marker for T-cell neoplasm and B-cell chronic
lymphocytic leukemia (41,99).
To date, PEG10 has been shown to be crucial in
several types of cancer, such as Ewing sarcoma (ES), esophageal
squamous cell carcinoma (ESCC) and metastatic thymic
adenocarcinoma. In ES, PEG10 inhibits the TGF-β pathway and reduces
cell growth. In the human skin epidermoid carcinoma cell line A431,
miR-145, miR-432 and miR-1972 inhibit PEG10 expression (100). Besides, genetic mutations can also
affect PEG10 activity. In metastatic thymic adenocarcinoma, PEG10
was found to have a somatic p.R207H mutation (101). LncRNA PEG10 is elevated in serum
exosomes of patients with ESCC (102). Higher PEG10 levels are associated
with unfavorable overall and progression-free survival (103). Therefore, PEG10 can serve as a
marker of carcinogenesis, progression and poor prognosis, as well
as a putative drug target in ovarian cancer (72,104,105), rectal adenocarcinoma (106), early-onset colorectal cancer
(107), neuroendocrine
muscle-invasive bladder cancer (108), bladder cancer (108), adenosquamous carcinomas (109), gallbladder adenocarcinoma
(110), breast cancer (111,112), adenocarcinoma (113), oral squamous cell carcinoma
(114) and glioma (115).
ALS is a chronic neurodegenerative disease that
mainly causes damage to upper and lower motor neurons. Mutations in
the ubiquitin-adaptor protein UBQLN2 is considered one of the
causes of ALS (116,117). PEG10 is a substrate of UBQLN2
(118); UBQLN2 binds to the
C-terminus of PEG10 and initiates its degradation (24).
Angelman syndrome is caused by UBE3A defect;
patients with Angelman syndrome often experience developmental
delay, balance disorders, limb incoordination and gait instability.
The UBE3A mutation causes PEG10 aggregation, alters neuronal
migration and ultimately leads to Angelman syndrome (25).
Although no targeted small-molecule inhibitors to
block PEG10 have been developed, there are still numerous ways to
inhibit PEG10, including inhibitors that target its transcription
factors, siRNAs, shRNAs or miRNAs that target PEG10 mRNA, as well
as using PEG10 as an antigen to develop vaccines (119). PEG10-related treatment methods are
listed in Table I. The functional
diversity of PEG10 poses multiple challenges to drug development,
and ensuring target specificity is key in drug development to avoid
unnecessary damage to embryo development or normal tissue
function.
Not applicable.
This work was supported by the National Science Foundation of
Sichuan Province (grant no. 2023NSFSC1555), the National Clinical
Research Center for Geriatrics, West China Hospital, Sichuan
University (grant no. Z20192008), the special fund in West China
Hospital, Sichuan University (grant no. 008420415031) and the 1·3·5
project for disciplines of excellence, West China Hospital, Sichuan
University (grant no. ZYJC18003).
Not applicable.
DM, SB and XB were involved in the conceptualization
of the study. SW and YC wrote the original draft. YW and YD
prepared the figures. MT and XT reviewed and revised the
manuscript. All authors reviewed the manuscript and have read and
approved the final version. Data authentication is not
applicable.
Not applicable.
Not applicable.
The authors declare that they have no competing
interests.
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