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PARP7

From EverybodyWiki Bios & Wiki




PARP7 (Poly (ADP-ribose) polymerase 7), also known as TIPARP, is an enzyme of the PARP family that catalyzes the transfer of ADP-ribose from NAD+ to specific amino acids of itself and other substrate proteins.[1]. 17 PARP members are divided into polyPARPs, monoPARPs, and PARPs without catalytic activity according to different catalytic functions. PARP7 is a monoPARP that catalyzes the transfer of single units of ADP-ribose onto substrates to change their function [2][3]. PARP7 is closely related to tumor generation and immune function recovery [4].

PARP7 acts:

  • Amplified in many cancers and acts as a "brake" in the type I IFN response to cytosolic nucleic acid [6].

PARP7 is involved in [7]:

Structure of PARP7

PARP7 is characterized by a sequence consisting of 657 amino acids [8]. The protein contains a CCCH-type zinc finger domain for DNA/RNA binding, a protein−protein interaction domain mediating iso-ADP-ribose interaction, a conserved ADP-ribosyltransferase catalytic domain with ADP-ribosyl transferase activity, and an N-terminal nuclear localization signal (NLS) [9].

Role in viral infection

PARP7 plays a dual role in viral replication, with its specific function depending on the type of virus. With regard to infection with the coronavirus, there is a significant upregulation of PARP7 expression, suggesting that PARP7 expression levels substantially influence the host's antiviral response [10]. PARP7 directly enhances viral replication capabilities, so that modulating the expression and activity of PARP7 to strengthen the host's immune response represents a promising novel antiviral strategy [11]. PARP13 is an inactive member of the PARP family and plays a role in inhibiting the replication of a wide range of RNA viruses. PARP7 can modulate the antiviral activity of PARP13 through mono-ADP-ribosylation (MARylation) modification [12]. Conversely, it is hypothesized that high expression levels of PARP7 inhibit the replication of specific viruses, because PARP7 is identified as a potent inhibitors of Venezuelan equine encephalitis virus (VEEV), Getah virus(GETV), Sindbis virus (SINV), and other RNA viruses [13][14][15][16][17].

Role in tumor

Activation of the signaling pathway for type I interferon (IFN-I) release is an effective manner for the human body to clear tumor cells [18][19]. In the IFN-I signaling pathway, the activation of TANK-binding kinase 1 (TBK1) is essential for signal transduction. PARP7 inhibits TBK1 activation via mono-ADP-ribosylation, consequently suppressing the phosphorylation of interferon regulatory factor 3 (IRF3) [20].This process results in the disruption of the IFN-I pathway, ultimately contributing to immune escape in tumor cells [21]. Inhibition of PARP7 activity restores TBK1 phosphorylation function and activates the IFN-I signaling pathway [22]. This cascade subsequently activates the Janus kinase (JAK) Signal transducer and activator of transcription pathway, promoting the upregulation of CXCL10 expression and recruiting cytotoxic T cell to eliminate tumor cells.

PARP7 inhibits the IFN-I signaling pathway by blocking the degradation of FRA1 (FOSL1, an AP-1 transcription factor). Reducing the expression level of PARP7 promotes the degradation of FRA1 and restores the IFN-1 signaling. PARP7 inhibitors have clinical potential in treating FRA1-driven cancers, offering a new application strategy of PARP7 inhibitors for cancer therapy [23].

The upregulation of PD-1/PD-L1 immune checkpoints is demonstrated to obstruct the IFN-I signaling pathway, thereby impeding the recruitment of cytotoxic T lymphocytes. PARP7 inhibitors in combination with PD1/PD-L1 immune checkpoint inhibitor (ICIs) may improve tumor prognosis and provide synergistic anti-tumor effects [24]. It is found that the combination of RBN-2397 (a PARP7 inhibitor), MSA-2 (a STING agonist), and R848 (a Toll-like receptor 7/Toll-like receptor 8 agonist) is capable of increasing CXCL9 expression by approximately 8-fold [25], providing new insights into anti-tumor therapies using PARP7 inhibitors.

PARP7 inhibitors in cancer treatment

The expression of PARP7 varies across different tumor types, and its role differs accordingly. It is proven that down-regulating the expression level of PARP7 has excellent therapeutic effects on a variety of cancers. The use of PARP7 inhibitors is widely recognized as a novel approach to immune-mediated anti-tumor therapy.

In ovarian cancer, it is found that reducing the expression of PARP7 or mutating the sites responsible for modifying microtubule proteins increases microtubule stability and slows the growth of ovarian cancer cells. Knocking PARP7 gene leads to a decrease in cell growth, migration, and invasion, as well as an increase in microtubule content [26]. It is demonstrated that the coadministration of RBN-2397 (a PARP7 inhibitor) with paclitaxel exhibits activationic inhibitory effect on ovarian cancer. This strategy for coadministration can effectively decrease the invasive cellular phenotype associated with ovarian cancer [27].

In prostate cancer, the activation of the Androgen receptor (AR) signaling is important for tumor cell survival and growth [28]. PARP7 is a direct target gene of AR, whose protein stability is regulated by AR [29][30]. Upon activation of mutant ARs, PARP7 is significantly upregulated. PARP7 can influence AR signaling by modulating AR levels through a feedback regulatory mechanism. PARP7 modifies multiple cysteine residues of AR through ADP-ribosylation, thereby increasing the stability and signaling capacity of AR. This modification induces the formation of a complex between AR and the DTX3L-PARP9 complex, then regulates the expression of AR-regulated genes, thereby promoting the growth and survival of prostate cancer cells. The inhibition of PARP7 prevents AR from forming complexes with DTX3L and PARP9, limiting the growth and survival of prostate cancer cells [31][32][33][34].

Ribon Therapeutics reported the first PARP7 inhibitor RBN-2397. This compound has progressed to clinical phase II trials for the treatment of advanced and metastatic solid tumors. RBN-2397 exhibited extremely high inhibitory potency against PARP7 with an IC50 value of 5.0 nM and significant growth inhibition of CT-26 tumor cells in a mouse xenograft model [35].

Role in stroke

Overactivation of astrocyte can exacerbate brain damage and impair the recovery of brain function following a stroke. It is demonstrated that the circHectd1-mir142 axis promotes astrocyte activation by inducing downstream PARP7 expression. CircRNA Hectd1 (circHectd1) functions as a sponge for microRNA 142 (mir142), inhibiting its activity and consequently reducing its binding to the untranslated region (3'UTR) of PARP7. The process enhances the transcription and translation of PARP7, which subsequently activates autophagy and stimulates astrocyte activation [36]. By inhibiting PARP7 expression, the activation of astrocytes can be reduced, thereby positively influencing stroke treatment.

Role in other physiological functions

PARP7 expression may impact hepatic energy metabolism and inflammatory response by decreasing NAD+ levels, consequently affecting glucose regulation and promoting the development of nonalcoholic fatty liver disease (NAFLD) [37]. PARP7 is associated with blood glucose [38][39] , blood pressure [40][41], oral cancer [42], uveal melanoma [43][44], meningioma [45], inflammatory bowel disease [46], bone disease, obesity, and intraocular pressure [47]

References

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  2. ↑ Vyas, Sejal; Chesarone-Cataldo, Melissa; Todorova, Tanya; Huang, Yun-Han; Chang, Paul (2013-08-06). "A systematic analysis of the PARP protein family identifies new functions critical for cell physiology". Nature Communications. 4 (1). Bibcode:2013NatCo...4.2240V. doi:10.1038/ncomms3240. ISSN 2041-1723. PMC 3756671. PMID 23917125. Unknown parameter |article-number= ignored (help)
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  4. ↑ Palavalli Parsons, Lavanya H; Challa, Sridevi; Gibson, Bryan A; Nandu, Tulip; Stokes, MiKayla S; Huang, Dan; Lea, Jayanthi S; Kraus, W Lee (2020-12-24). "Author response: Identification of PARP-7 substrates reveals a role for MARylation in microtubule control in ovarian cancer cells". Biochemistry and Chemical Biology. doi:10.7554/elife.60481.sa2.
  5. ↑ Yamada, Taisho; Horimoto, Hiromasa; Kameyama, Takeshi; Hayakawa, Sumio; Yamato, Hiroaki; Dazai, Masayoshi; Takada, Ayato; Kida, Hiroshi; Bott, Debbie; Zhou, Angela C; Hutin, David; Watts, Tania H; Asaka, Masahiro; Matthews, Jason; Takaoka, Akinori (2016-04-18). "Constitutive aryl hydrocarbon receptor signaling constrains type I interferon–mediated antiviral innate defense". Nature Immunology. 17 (6): 687–694. doi:10.1038/ni.3422. ISSN 1529-2908. PMID 27089381.
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  44. ↑ Tang, Zhongjun; Cai, Kebo (2021-08-14). "A Novel 8-Gene Prognostic Signature for Survival Prediction of Uveal Melanoma". Analytical Cellular Pathology. 2021: 1–18. doi:10.1155/2021/6693219. ISSN 2210-7185. PMID 34434692 Check |pmid= value (help).
  45. ↑ Prakash Babu, Phanithi; Noble Kumar, Talari; Manas, Panigrahi; Sailaja, Madigubba (2016). "Aryl hydrocarbon receptor (AHR) signalling pathway is activated and involved in tumor progression of human meningioma". Frontiers in Cellular Neuroscience. 10. doi:10.3389/conf.fncel.2016.36.00113. ISSN 1662-5102.
  46. ↑ Hutin, David; Hagen, Karoline Alvik; Shao, Peng; Sugamori, Kim; Grant, Denis M.; Matthews, Jason (2022-01-15). "Reduced Colonic Mucosal Injury in 2,3,7,8-Tetrachlorodibenzo-p-Dioxin Poly ADP-Ribose Polymerase (TIPARP/PARP7)-Deficient Mice". International Journal of Molecular Sciences. 23 (2): 920. doi:10.3390/ijms23020920. ISSN 1422-0067. PMC 8779828 Check |pmc= value (help). PMID 35055106 Check |pmid= value (help).
  47. ↑ Zhang, Youjia; Song, Maomao; Bi, Yingwen; Lei, Yuan; Sun, Xinghuai; Chen, Yuhong (2022-12-19). "TIPARP is involved in the regulation of intraocular pressure". Communications Biology. 5 (1). doi:10.1038/s42003-022-04346-0. ISSN 2399-3642. PMC 9763400 Check |pmc= value (help). PMID 36536086 Check |pmid= value (help). Unknown parameter |article-number= ignored (help)


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