logo
Menu

B7-H3 is expressed in certain tumor cells in a variety of cancers, but undetectable or low in normal tissue

  • B7-H3 expression is undetectable or low in normal tissue1–4
  • B7-H3 expression may be associated with a poor prognosis for a variety of tumor types4–13
Diagram of normal cells, tumor cells, and B7-H3 expressed in the tumor cells.

Diagram is for illustrative purpose only and does not represent a specific tumor type.

Was this informative?

B7-H3 expression is prevalent in certain human cancers

  • B7-H3 is a transmembrane protein that belongs to the B7 family that includes immune checkpoint molecules such as PD-L114-17
  • B7-H3 plays a role in antitumor immunity and regulating T cell activation17–20
  • The receptor for B7-H3 is currently unknown, but is thought to be expressed by T cells17,21
  • B7-H3 was expressed in 72% (n=1,342) of patients with certain cancers34,a
    • aIHC analysis using an anti-B7-H3 primary antibody (R&D Systems AF1027) of tumor cells from 1,342 commercially available human tumor tissues derived from a variety of cancer types. 72% of samples had detectable B7-H3 expression (IHC 1+, 16%; IHC 2+, 26%; IHC 3+, 30%)34

Click the buttons in the human body figure below to review certain cancers in which B7-H3 is expressed

The data shown in this section are from various publications derived from a review of the literature. Studies were only included if they used immunohistochemistry to measure B7-H3 protein expression. The details of each study can be found in the footnotes for each tumor type. The information shown comprises selected data and does not account for all evidence that may be available; therefore, no definitive conclusions should be drawn from these data.

​
Illustrative human body graphic showing tumor locations where B7-H3 protein expression has been reported across various solid cancers. Each site is clickable to display prevalence data.

Central nervous system

B7-H3 was expressed in 83% of glioma tissue samples34,a
B7-H3 was highly expressed in 76% of patients with glioblastoma35,b
aIHC analysis using an anti-B7-H3 primary antibody (R&D Systems AF1027) of tumor cells from 41 commercially available human glioma samples. 83% of samples had detectable B7-H3 expression (IHC 1+, 17%; IHC 2+, 17%; IHC 3+, 49%)34
bIHC analysis using an anti-B7-H3 primary antibody (R&D Systems AF1027) of 46 human glioblastoma specimen (low expression [22% or 10/46 samples] defined as 5-20% positive cells; high expression [76% or 35/46 samples] defined as ≥20% positive cells). B7-H3 was not detected in one specimen35

Head and neck

97.5% of head and neck squamous cell carcinoma patients expressed B7-H3 with a majority demonstrating strong staining36,a
aIHC analysis of 398 patient samples in tissue microarrays using an anti-B7-H3 primary antibody (Zytomed SP265). Samples were considered positive for B7-H3 if they had interpretable staining at an intensity of 1+, 2+, or 3+. Moderate staining was defined as a staining intensity of 1+ in >70% of tumor cells, a staining intensity of 2+ in ≤30% and ≤70% of tumor cells, or a staining intensity of 3 in ≤30% of tumor cells. Strong staining was defined as 2+ in >70% of tumor cells or a staining intensity of 3 in >30% of tumor cells36

Thyroid

B7-H3 was expressed in 61.5% of patients with papillary thyroid cancer51,a
aTissue samples from 343 papillary thyroid cancer tumors were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (Cell Signaling D9M2L). B7-H3 staining intensity was scored on a scale of 0-3 (0, no membranous staining or <1% tumor cells with faint/weak membranous staining; 1, ≥1% tumor cells with faint/weak membranous staining or <1% tumor cells with medium membranous staining; 2, ≥1% tumor cells with medium membranous staining or <1% tumor cells with strong membranous staining; 3, ≥1% tumor cells with strong membranous staining). Tissue samples with a staining score of 0 or 1 were assigned to the B7-H3-negative group (132/343, 38.5%), while those with a staining score of 2 or 3 were assigned to the B7-H3 positive group (211/343, 61.5%)51

Esophageal

B7-H3 was expressed in 87% of patients with esophageal squamous cell carcinoma34,a
aIHC analysis using an anti-B7-H3 primary antibody (R&D Systems AF1027) of tumor cells from 109 commercially available human ESCC samples. 87% of samples had detectable B7-H3 expression (IHC 1+, 8%; IHC 2+, 23%; IHC 3+, 56%)34

Lung

52.4% of patients with metastatic or locally advanced non-small cell lung cancer exhibited strong membranous B7-H3 staining37,a
88.3% (189/214) of resected pulmonary squamous cell carcinoma cases expressed B7-H3; among these, 73% exhibited moderate or strong staining38,b
B7-H3 was expressed at moderate or strong levels in 64.5% of small cell lung cancer patient samples5,c
aTumor specimen from 82 patients with metastatic or locally advanced NSCLC underwent IHC analysis for membranous B7-H3 expression using an anti-B7-H3 primary antibody (Daiichi Sankyo Ltd BD/5A11). Strong staining was defined as IHC 2+ or 3+. IHC 1+ was defined as >10% tumor cells with faint/weak membranous staining; IHC 2+ was defined as >10% tumor cells with faint/weak membranous staining or ≤10% tumor cells with strong membranous staining; IHC 3+ was defined as >10% tumor cells with strong membranous staining. 32.9% (27/82) of tumor specimen were IHC 2+ and 19.5% (16/82) of tumor specimen were IHC 3+. 52.4% (43/82) of specimen were scored as IHC 2+ or 3+37
bIHC with an anti-B7-H3 primary antibody (R&D Systems AF1027) was used to evaluate B7-H3 expression in tissues from 214 patients with squamous cell carcinoma of the lung. Patients were positive if they had 5-100% of immunopositive cells (189/214 tissues; 88.3%) and if the staining was membranous and circumferential. Intensity was also estimated as weak (52/189 or 27% of tissues; faint brown staining), moderate (130/189 or 69% of tissues), or strong (7/189 or 4% of tissues; dark brown staining)38
cTissue microarrays constructed from resected tumor specimen from SCLC patients were subjected to IHC analysis using an anti-B7-H3 primary antibody (Cell Signaling D9M2L). Among the SCLC patients with complete follow-up data (n = 107), 69 (64.49%) expressed moderate or strong B7-H3 levels. B7-H3 expression was evaluated according to the intensity of epithelial tumor cell-specific cytoplasmic/membranous staining. Samples with a percentage of ≥1% cells with B7-H3 staining were considered positive (69/107 samples; 64.5%)5

Breast

B7-H3 was expressed in 50% of breast cancer samples39,a
a347 patients with breast cancer were evaluated for B7-H3 expression using IHC with an anti-B7-H3 primary antibody (Cell Signaling D9M2L). 226 patients were ER+, 45 patients were HER2+, and 63 patients had TNBC. A positive B7-H3 stain was defined as >1% of cells displaying unequivocal staining (174/347 samples; 50%), whereas a negative finding was defined as <1% positivity (173/347 samples; 50%). Cytoplasmic and membranous staining were analyzed. B7-H3 expression was elevated in HER2+ (32/45, 71%) and TNBC (39/63, 62%) breast cancer subtypes in comparison to the ER+ tumors39

Melanoma

B7-H3 was expressed in 78% of patients with melanoma34,a
aIHC analysis using an anti-B7-H3 primary antibody (R&D Systems AF1027) of tumor cells from 79 commercially available human melanoma samples. 78% of samples had detectable B7-H3 expression (IHC 1+, 6%; IHC 2+, 40%; IHC 3+, 32%)34

Gastric

B7-H3 was expressed in 78% of patients with gastric adenocarcinoma40,a
aResected gastric adenocarcinoma samples from 50 patients were subjected to IHC analysis using an anti-B7-H3 primary antibody (R&D Systems, clone not specified). Intensity of staining was scored on a scale of 0-3 (0, negative; 1, weak staining; 2, moderate staining; 3, intense staining). If <5% of cells stained positive for B7-H3 the staining result was considered negative. 39 /50 (78%) samples stained positive for B7-H340

Liver

B7-H3 was detected in 93.8% of hepatocellular carcinoma specimens and 70% of those showed moderate or strong expression41,a
aArchived tissues from 240 patients who received curative resection of HCC were incorporated into tissue microarrays and subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (Sigma, clone not specified). Sections were considered positive when tumor cells showed cytoplasmic or membranous B7-H3 immunostaining. The B7-H3 staining intensities were scored on a scale of 0-3 (0, negative; 1, weak; 2, moderate; 3, strong). A negative grade represented no tumor cells showing positive staining. 225/240 (93.8%) patient samples stained positive for B7-H3 expression. 89 (37.1%) patient samples exhibited moderate B7-H3 expression and 79 (32.9%) samples exhibited strong expression41

Biliary tract

B7-H3 was expressed in 57.8% of patients with resectable intrahepatic cholangiocarcinoma29,a
B7-H3 was expressed in 66.7% of patients with gallbladder cancer42,b
aICC specimen from 45 patients who received surgical resection were subjected to IHC analysis using an anti-B7-H3 primary antibody (Abcam, clone not specified). B7-H3-positive cancer cells were counted in 10 typical microscopic fields. A score was calculated by multiplying the staining intensity score by the staining area score. Staining intensity was scored on a scale of 0-3 (0, absent; 1, weak; 2, moderate; 3, strong) and staining area was measured by percentage of positive cells (1, ≤10% of cancer cells; 2, 10% to ≤50% of cancer cells; 3, >50% of cancer cells). The total final score ranged from 0-9. Final scores of ≤1 were considered as negative B7-H3 expression (19/45 cases; 42.2%) while scores ≥2 were classified as positive B7-H3 expression (26/45 cases; 57.8%)29
bGallbladder specimen from 126 patients who underwent cholecystectomy for gallbladder cancer were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (clone not specified). B7-H3 was expressed in 84/126 (66.7%) patient samples. B7-H3 expression was measured in 5 fields for each sample and judged according to the percentage of positive cells and given a score of negative (0% positive cells), 1+ (0% to <10% positive cells), 2+ (10% to <50% positive cells), 3+ (50% to <80% positive cells), or 4+ (≥80% positive cells). Negative or weakly positive patients were considered to be low expressing, while moderate or strong expressing were considered high expressing42

Pancreatic

B7-H3 was expressed in 81.3% of patients with pancreatic ductal adenocarcinoma43,a
aTissue microarrays were constructed from specimen from 240 PDAC patients and subjected to IHC for B7-H3 expression using an anti-B7-H3 primary antibody (R&D Systems AF1027). Samples were considered positive for B7-H3 expression on tumor cells when at least 5% of the tumor cells expressed B7-H3 (195/240 cases; 81.3%)43

Kidney

B7-H3 expression was detected in 69% of metastatic renal cell carcinoma patient samples45,a
aTissue microarrays were constructed from tumor tissues derived from radical or partial nephrectomy specimens from 84 patients with metastatic RCC. IHC analysis for B7-H3 expression was conducted using an anti-B7-H3 primary antibody (clone not specified), focusing on membranous expression of B7-H3. IHC was scored on a scale of 0-3+ (0, no staining; 1+, incomplete membranous staining and/or faint intensity; 2+, weak to moderate intensity; 3+, complete and intense membrane staining in at least 10% of tumor cells). B7-H3 was expressed at IHC 1+, 2+, or 3+ in 69% (58/84 patients). IHC 1+ staining was detected in 33.3% (n=28), IHC 2+ staining was detected in 31% (n=26), and IHC 3+ staining was detected in 4.8% (n=4) patients45

Colorectal

B7-H3 was expressed in 50.9% of colorectal cancer tumors44,a
aPrimary CRC tumors from 805 CRC patients were incorporated into a tissue microarray and subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (Cell Signaling D9M2L). The staining intensity of B7-H3 in tumor cells was evaluated as negative (no staining) or positive (weak to strong staining) expression. For different staining intensity in two spots from the same case, the higher score was recorded. B7-H3 was expressed in 50.9% (410/805) of CRC, including 30.9% (249/805) with weak staining, 12.4% (100/805) with medium staining, and 7.6% (61/805) with strong staining44

Ovarian

B7-H3 was expressed in 74% of patients with ovarian cancer and was expressed at moderate or strong levels in 40% of samples34,a
aIHC analysis using an anti-B7-H3 primary antibody (R&D Systems AF1027) of tumor cells from 68 commercially available human ovarian cancer samples. 74% of samples had detectable B7-H3 expression (IHC 1+, 34%; IHC 2+, 22%; IHC 3+, 18%). Moderate expression was defined as IHC 2+ and strong expression was defined as IHC 3+34

Prostate

Membranous B7-H3 expression was detected in 47% of patients with prostate cancer48,a
aTissue from 17,747 prostate cancer patients who had undergone radical prostatectomy were incorporated into tissue microarrays. Membranous B7-H3 expression was measured by IHC using an anti-B7-H3 primary antibody (Zytomed #M5650). 12,808 samples were interpretable in the analysis. The staining intensity (0, 1+, 2+, 3+) and the fraction of positive tumor cells were recorded for each tumor tissue spot and a final score was built of these two parameters: negative, staining intensity of 0; weak, staining intensity of 1+ in ≤70% of tumor cells or staining intensity of 2+ in ≤30% of tumor cells; moderate, staining intensity of 1+ in >70% of tumor cells, staining intensity of 2+ in >30% but in ≤70% of tumor cells or staining intensity of 3+ in ≤30% of tumor cells; strong, staining intensity of 2+ in >70% of tumor cells or staining intensity of 3+ in >30% of tumor cells. Out of the 6,014 samples expressing B7-H3, staining was considered weak in 12.3%, moderate in 21.1%, and strong in 13.5%48

Bladder

B7-H3 expression was detected in 70.7% of urothelial carcinoma patient samples46,a
aTumor samples from 314 urothelial carcinoma patients who had undergone radical cystectomy were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (R&D Systems, clone not specified). B7-H3 expression was quantified in tumor cells and cases with <10% of cells staining for B7-H3 were considered negative. B7-H3 was expressed by 222 /314 (70.7%) of bladder tumors evaluated46

Cervical

B7-H3 was expressed in 63% of patients with primary cervical cancer and 78.5% of patients with recurrent cervical cancer47,a
aSamples derived from 605 primary cervical cancer patient tumors who underwent cervical conization (n=16) or hysterectomy (n=590) and 65 recurrent cervical cancer patients who underwent either pelvic exenteration or metastasectomy were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (Cell Signaling D9M2L). Only patients diagnosed with squamous cell carcinoma or usual-type adenocarcinoma were included. B7-H3 was expressed in 380/605 (63%) primary cervical cancer tumors and 51/65 (78.5%) recurrent cervical cancer tumors. Samples were considered positive for B7-H3 expression when ≥5% of tumor cells expressed B7-H3 at any intensity. B7-H3 was also considered positive when observed in stromal cells47

Endometrial

B7-H3 expression was detected in 75.7% of endometrial cancer patient samples6,a
aTumor tissue from 99 patient specimens (81 endometrioid carcinomas and 18 type II carcinomas) were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (R&D Systems, clone not specified). B7-H3 was expressed in 75/99 (75.7%) of patients with endometrial cancer. Evaluation of B7-H3 expression in tumor cells was based on staining intensity and quantity throughout the whole slide. Staining quantity was scored as follows: 0-10% positive cells, >10-50% positive cells, >50-80% positive cells, and >80-100% positive cells. Staining intensity was scored as faint (1+), moderate (2+), or strong (3+). The quantity score was multiplied by the intensity score to yield an immunohistochemical score of 1-12. Scores ≥9 were determined to represent B7-H3 overexpression6

Orthopedic

B7-H3 was expressed in 97.3% of soft tissue sarcoma samples49,a
B7-H3 was expressed in 73.3% of patients with osteosarcoma50,b
aB7-H3 was measured by IHC in tissue samples from 153 patients with soft tissue sarcoma using an anti-B7-H3 primary antibody (clone RBT-B7-H3). IHC B7-H3 expression was initially scored on a scale of 0-5, with a score of 0 representing negative staining and scores 1-5 representing increasing levels of tumor expression with respect to frequency. 149/153 (97.3%) of tissue samples expressed B7-H349
bPathological specimen from 60 osteosarcoma patients were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (Sino Biological, Inc, clone not specified). Tissues were considered positive for B7-H3 expression if they had ≥5% of tumor cells stain positive for B7-H3. 44/60 (73.3%) samples stained positive for B7-H3 expression50

Orthopedic

B7-H3 was expressed in 97.3% of soft tissue sarcoma samples49,a 49,a
B7-H3 was expressed in 73.3% of patients with osteosarcoma50,b
aB7-H3 was measured by IHC in tissue samples from 153 patients with soft tissue sarcoma using an anti-B7-H3 primary antibody (clone RBT-B7-H3). IHC B7-H3 expression was initially scored on a scale of 0-5, with a score of 0 representing negative staining and scores 1-5 representing increasing levels of tumor expression with respect to frequency. 149/153 (97.3%) of tissue samples expressed B7-H349
bbPathological specimen from 60 osteosarcoma patients were subjected to IHC analysis for B7-H3 expression using an anti-B7-H3 primary antibody (Sino Biological, Inc, clone not specified). Tissues were considered positive for B7-H3 expression if they had ≥5% of tumor cells stain positive for B7-H3. 44/60 (73.3%) samples stained positive for B7-H3 expression50

Was this informative?

B7-H3 may exert pro-tumorigenic effects

  • The function of B7-H3 remains under investigation; however, some data support that B7-H3 may exert pro-tumorigenic effects17
  • Although the receptor for B7-H3 is unknown, there are several signaling pathways mediated by B7-H3 that have been identified17
  • Preclinical models suggest that B7-H3 may initiate signaling through investigated cancer-associated pathways, such as PI3K/AKT/mTOR, Jak/STAT3, MVP/Raf/MEK, and NF-kB/VEGF17
+ SHOW MORE
  • Upregulation of B7-H3 may activate PI3K and Jak/STAT3 signaling pathways to promote tumor cell migration and invasion, proliferation, and treatment resistance17,22–24
  • B7-H3 has been shown to initiate signaling through Raf/MEK through associations with major vault protein (MVP) and induce cancer stem cell and tumor formation25
  • Signaling through NF-kB activates VEGF to stimulate angiogenesis, which promotes cell survival and proliferation17,26
  • Through these signaling pathways, B7-H3 may exert pro-tumorigenic effects including promotion of cell proliferation, migration and invasion, immune evasion, and angiogenesis17
+ SHOW MORE
  • Immune evasion – B7-H3 expression is enriched within certain tumor microenvironments, where it facilitates immune evasion through various mechanisms and promotes an immunosuppressive microenvironment17,27,28
  • Cell proliferation – B7-H3 has been reported to activate signaling pathways such as ERK, PI3K, and STAT3 in certain cancer cells, which may lead to accelerated cell proliferation and tumor growth17
  • Angiogenesis – B7-H3 is shown to be implicated in angiogenesis in certain cancers. B7-H3 promotes angiogenesis by stimulating the secretion of VEGF17,26,29,30
  • Invasion and migration (metastasis) – B7-H3 function in tumor biology is linked to its ability to induce increased metastasis-promoting cell migration and invasion27,31-33

Click the buttons in the figure below to learn more about each investigational pathway.

Interactive diagram of signaling pathways potentially linked to B7-H3, including PI3K/AKT/mTOR, Jak/STAT3, Raf/MEK, and NF-kB/VEGF. Figure adapted from Getu AA, et al. Mol Cancer. 2023;22(1):43.

Upregulation of B7-H3 may activate PI3K and Jak/STAT3 signaling pathways to promote tumor cell migration and invasion, sustained tumor cell proliferation, and treatment resistance17,22–24

Upregulation of B7-H3 may activate PI3K and Jak/STAT3 signaling pathways to promote tumor cell migration and invasion, sustained tumor cell proliferation, and treatment resistance17,22–24

B7-H3 has been shown to initiate signaling through Raf/MEK through associations with major vault protein (MVP) and induce cancer stem cell and tumor formation25

Signaling through NF-kB activates VEGF to stimulate angiogenesis, which promotes cell survival and proliferation17,26

Cell proliferation – B7-H3 has been reported to activate signaling pathways such as ERK, PI3K, and STAT3 in certain cancer cells, which may lead to accelerated cell proliferation and tumor growth17

Angiogenesis – B7-H3 is shown to be implicated in angiogenesis in certain cancers. B7-H3 promotes angiogenesis by stimulating the secretion of VEGF17,26,29,30

Invasion and migration (metastasis) – B7-H3 function in tumor biology is linked to its ability to induce increased metastasis-promoting cell migration and invasion27,31-33

Immune evasion – B7-H3

expression is enriched within certain tumor microenvironments, where it facilitates immune evasion through various mechanisms and promotes an immunosuppressive microenvironment17,27,28

Was this informative?

Abbreviations

Akt, protein kinase B; B7-H3, B7 homolog 3; CNS, central nervous system; CRC, colorectal cancer; ER, estrogen receptor; ERK, extracellular signal-regulated kinase; ESCC, esophageal squamous cell carcinoma; HCC, hepatocellular carcinoma; HER2, human epidermal growth factor receptor; HNSCC, head and neck squamous cell carcinoma; ICC, intrahepatic cholangiocarcinoma; IHC, immunohistochemistry; Jak, Janus kinase; MEK, mitogen-activated protein kinase kinase; mNSCLC, metastatic non-small cell lung cancer; mTOR, mammalian target of rapamycin; MVP, major vault protein; NF-kB, nuclear factor kappa-light-chain-enhancer of activated B cells; NSCLC, non-small cell lung cancer; PDAC, pancreatic ductal adenocarcinoma; PD-L1, programmed cell death ligand 1; PI3K, phosphoinositide 3-kinase; Raf, rapidly accelerating fibrosarcoma protein; RCC, renal cell carcinoma; STAT3, signal transducer and activator of transcription 3; TME, tumor microenvironment; TNBC, triple negative breast cancer; VEGF, vascular endothelial growth factor.

References

1. Yang S, et al. Int J Biol Sci. 2020;16(11):1767-1773. 2. Dong P, et al. Front Oncol. 2018;8:264. 3. Yamato M, et al. Mol Cancer Ther. 2022;21:635-46. 4. Wang L, et al. Tumour Biol. 2016;37(3):2961-71. 5. Qiu M, et al. Front Oncol. 2021;11:600238. 6. Brunner A, et al. Gynecol Oncol. 2012;124(1):105-11. 7. Chen S, et al. J Cancer Res Clin Oncol. 2023;149(18):16609-16621. 8. Cong F, et al. Oncol Lett. 2017;14(6):7185-7190. 9. Song J, et al. Onco Targets Ther. 2016:9:6257-6263. 10. Katayama A, et al. Int J Oncol. 2011;38:1219-1226. 11. Wang L, et al. PLoS One. 2013;8(8):e70689. 12. Amori G. Prostate Cancer Prostatic Dis. 2021;24(3):767-774. 13. Inamura K, et al. Lung Cancer. 2017;103:44-51. 14. Zhong C, et al. Clin Exp Immunol. 2020;200(1):12-21. 15. Khan M, et al. Front Immunol. 2021;12:651634. 16. Pardoll DM. Nat Rev Cancer. 2012;12(4):252-64. 17. Getu AA, et al. Mol Cancer. 2023;22(1):43. 18. Kobori H, et al. Immunology. 2010;130(3):363-373. 19. Luo L, et al. J Immunol. 2004;173:5445-50. 20. Leitner J, et al. Eur J Immunol. 2009;39:1754-1764. 21. Chapoval AI, et al. Nat Immunol. 2001;2(3):269-274. 22. Wu X, et al. Transl Cancer Res. 2024;13(2):833-846. 23. Sun M, et al. J Cancer. 2021;12(24):7518-7526. 24. Zhou L and Zhao Y. Cancer Manag Res. 2019:11:10205. 25. Liu Z, et al. Oncogene. 2019;38(1):88-102. 26. Wang R, et al. Cell Death Dis. 2020;11(1):55. 27. Kanchan RK, et al. Biochim Biophys Acta Rev Cancer. 2022;1877(5):188783. 28. Gay CM, et al. Clin Cancer Res. 2025;31(16):3476-3482. 29. Cheng R, et al. APMIS. 2018;126(5):396-402. 30. Cheng N, et al. Biochem Pharmacol. 2021:183:114298. 31. Chen YW, et al. Curr Cancer Drug Targets. 2008;8(5):404-41. 32. Li Y, et al. Oncotarget. 2017;8(42):71725-71735. 33. Liu F, et al. Mol Med Rep. 2015;12(4):5455-5460. 34. Seaman S, et al. Cancer Cell. 2017;31(4):501-515. 35. Nehama D, et al. eBioMedicine. 2019;47:33-43. 36. Borgmann M, et al. J Cancer Res Clin Oncol. 2023;149(7):3383-3393. 37. Yonesaka K, et al. Clin Cancer Res. 2018;24(11):2653-2664. 38. Boland JM, et al. Clin Lung Cancer. 2013;14(2):157-63. 39. Joshi V, et al. Int J Mol Sci. 2024;25(7):3976. 40. Guo L, et al. Medicine (Baltimore). 2019;98(8):e14663. 41. Sun TW, et al. Cancer Immunol Immunother. 2012;61(11):2171-82. 42. Liu CL, et al. Eur Rev Med Pharmacol Sci. 2016;20(21):4466-4473. 43. Chen X, et al. Arch Pathol Lab Med. 2023;147(4):465-473. 44. Lu Z, et al. Mod Pathol. 2020;33(11):2330-2340. 45. Özalp FR, et al. BMC Cancer. 2024;24(1):1471. 46. Boorjian SA, et al. Clin Cancer Res. 2008;14(15):4800-8. 47. Zong L, et al. Mod Pathol. 2022;35(6):786-793. 48. Bonk S, et al. Pathol Int. 2020;70(10):733-742. 49. Lynch MM, et al. BMC Cancer. 2024;24:1336. 50. Zhang Q, et al. BMC Cancer. 2022;22:1124. 51. Zhao B, et al. Front Cell Dev Biol. 2022;10:819236.

Click to review reference list