HHLA2 is expressed in pancreatic and ampullary cancers and increased expression is associated with better post-surgical prognosis.


Journal

British journal of cancer
ISSN: 1532-1827
Titre abrégé: Br J Cancer
Pays: England
ID NLM: 0370635

Informations de publication

Date de publication:
04 2020
Historique:
received: 19 04 2019
accepted: 31 01 2020
pubmed: 20 2 2020
medline: 31 12 2020
entrez: 20 2 2020
Statut: ppublish

Résumé

HHLA2 is a recently discovered member of the B7-family of immune checkpoint molecules with limited expression in normal tissues but overexpression in several types of cancer. The aim was to determine the expression, prevalence and biological relevance of HHLA2 protein expression in two closely related human cancer types, namely pancreatic cancer and ampullary cancer. HHLA2 expression levels were retrospectively determined by immunohistochemistry in tissue micro-arrays of surgically resected tumours of 122 pancreatic cancer patients and 72 patients with ampullary cancer of the pancreato-biliary subtype. HHLA2 was expressed at variable levels by tumour cells in 67% of pancreatic tumours and 93% of ampullary tumours. In the combined cohort high tumoural HHLA2 expression levels were significantly associated with delayed cancer recurrence and improved post-operative cancer-specific survival. The association of HHLA2 expression with cancer-specific survival and recurrence was statistically significant for the pancreatic cancer subgroup while a similar trend was found for the ampullary cancer subgroup. In multivariable analysis together with clinicopathologic characteristics, higher HHLA2 expression was an independent predictor of cancer-specific survival. The wide expression of HHLA2 in tumour cells and its association with cancer recurrence and patient survival suggest that HHLA2 represents a relevant immune checkpoint molecule in pancreatic and ampullary cancers.

Sections du résumé

BACKGROUND
HHLA2 is a recently discovered member of the B7-family of immune checkpoint molecules with limited expression in normal tissues but overexpression in several types of cancer. The aim was to determine the expression, prevalence and biological relevance of HHLA2 protein expression in two closely related human cancer types, namely pancreatic cancer and ampullary cancer.
METHODS
HHLA2 expression levels were retrospectively determined by immunohistochemistry in tissue micro-arrays of surgically resected tumours of 122 pancreatic cancer patients and 72 patients with ampullary cancer of the pancreato-biliary subtype.
RESULTS
HHLA2 was expressed at variable levels by tumour cells in 67% of pancreatic tumours and 93% of ampullary tumours. In the combined cohort high tumoural HHLA2 expression levels were significantly associated with delayed cancer recurrence and improved post-operative cancer-specific survival. The association of HHLA2 expression with cancer-specific survival and recurrence was statistically significant for the pancreatic cancer subgroup while a similar trend was found for the ampullary cancer subgroup. In multivariable analysis together with clinicopathologic characteristics, higher HHLA2 expression was an independent predictor of cancer-specific survival.
CONCLUSION
The wide expression of HHLA2 in tumour cells and its association with cancer recurrence and patient survival suggest that HHLA2 represents a relevant immune checkpoint molecule in pancreatic and ampullary cancers.

Identifiants

pubmed: 32071413
doi: 10.1038/s41416-020-0755-4
pii: 10.1038/s41416-020-0755-4
pmc: PMC7156757
doi:

Substances chimiques

HHLA2 protein, human 0
Immunoglobulins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1211-1218

Références

Bray, F., Ferlay, J., Soerjomataram, I., Siegel, R. L., Torre, L. A. & Jemal, A. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J. Clin. 68, 394–424 (2018).
doi: 10.3322/caac.21492
Kamisawa, T., Wood, L. D., Itoi, T. & Takaori, K. Pancreatic cancer. Lancet. 388, 73–85 (2016).
doi: 10.1016/S0140-6736(16)00141-0
Chandrasegaram, M. D., Gill, A. J., Samra, J., Price, T., Chen, J., Fawcett, J. et al. Ampullary cancer of intestinal origin and duodenal cancer - A logical clinical and therapeutic subgroup in periampullary cancer. World J. Gastrointest. Oncol. 9, 407–415 (2017).
doi: 10.4251/wjgo.v9.i10.407
Chang, D. K., Jamieson, N. B., Johns, A. L., Scarlett, C. J., Pajic, M., Chou, A. et al. Histomolecular phenotypes and outcome in adenocarcinoma of the ampulla of vater. J. Clin. Oncol. 31, 1348–1356 (2013).
doi: 10.1200/JCO.2012.46.8868
Ahn D. H., Bekaii-Saab T. Ampullary cancer: an overview. Am. Soc. Clin. Oncol. Educ. Book. 112–115 (2014).
Yachida, S., Wood, L. D., Suzuki, M., Takai, E., Totoki, Y., Kato, M. et al. Genomic sequencing identifies ELF3 as a driver of ampullary carcinoma. Cancer Cell. 29, 229–240 (2016).
doi: 10.1016/j.ccell.2015.12.012
Conroy, T., Desseigne, F., Ychou, M., Bouche, O., Guimbaud, R., Becouarn, Y. et al. FOLFIRINOX versus gemcitabine for metastatic pancreatic cancer. N. Engl. J. Med. 364, 1817–1825 (2011).
doi: 10.1056/NEJMoa1011923
Von Hoff, D. D., Ervin, T., Arena, F. P., Chiorean, E. G., Infante, J., Moore, M. et al. Increased survival in pancreatic cancer with nab-paclitaxel plus gemcitabine. N. Engl. J. Med. 369, 1691–1703 (2013).
doi: 10.1056/NEJMoa1304369
Overman, M. J., Varadhachary, G. R., Kopetz, S., Adinin, R., Lin, E., Morris, J. S. et al. Phase II study of capecitabine and oxaliplatin for advanced adenocarcinoma of the small bowel and ampulla of Vater. J. Clin. Oncol. 27, 2598–2603 (2009).
doi: 10.1200/JCO.2008.19.7145
Ribas, A. & Wolchok, J. D. Cancer immunotherapy using checkpoint blockade. Science. 359, 1350–1355 (2018).
doi: 10.1126/science.aar4060
Royal, R. E., Levy, C., Turner, K., Mathur, A., Hughes, M., Kammula, U. S. et al. Phase 2 trial of single agent Ipilimumab (anti-CTLA-4) for locally advanced or metastatic pancreatic adenocarcinoma. J. Immunother. 33, 828–833 (2010).
doi: 10.1097/CJI.0b013e3181eec14c
Brahmer, J. R., Tykodi, S. S., Chow, L. Q., Hwu, W. J., Topalian, S. L., Hwu, P. et al. Safety and activity of anti-PD-L1 antibody in patients with advanced cancer. N. Engl. J. Med. 366, 2455–2465 (2012).
doi: 10.1056/NEJMoa1200694
Le, D. T., Durham, J. N., Smith, K. N., Wang, H., Bartlett, B. R., Aulakh, L. K. et al. Mismatch repair deficiency predicts response of solid tumors to PD-1 blockade. Science. 357, 409–413 (2017).
doi: 10.1126/science.aan6733
Hu, Z. I., Shia, J., Stadler, Z. K., Varghese, A. M., Capanu, M., Salo-Mullen, E. et al. Evaluating mismatch repair deficiency in pancreatic adenocarcinoma: challenges and recommendations. Clin. Cancer Res. 24, 1326–1336 (2018).
doi: 10.1158/1078-0432.CCR-17-3099
Zhao, R., Chinai, J. M., Buhl, S., Scandiuzzi, L., Ray, A., Jeon, H. et al. HHLA2 is a member of the B7 family and inhibits human CD4 and CD8 T-cell function. Proc Natl Acad Sci USA 110, 9879–9884 (2013).
doi: 10.1073/pnas.1303524110
Zhu, Y., Yao, S., Iliopoulou, B. P., Han, X., Augustine, M. M., Xu, H. et al. B7-H5 costimulates human T cells via CD28H. Nat. Commun. 4, 2043 (2013).
doi: 10.1038/ncomms3043
Cheng, H., Borczuk, A., Janakiram, M., Ren, X., Lin, J., Assal, A. et al. Wide expression and significance of alternative immune checkpoint molecules, B7x and HHLA2, in PD-L1-negative human lung cancers. Clin. Cancer Res. 24, 1954–1964 (2018).
doi: 10.1158/1078-0432.CCR-17-2924
Xiao, Y. & Freeman, G. J. A new B7:CD28 family checkpoint target for cancer immunotherapy: HHLA2. Clin. Cancer Res. 21, 2201–2203 (2015).
doi: 10.1158/1078-0432.CCR-14-2658
Janakiram, M., Chinai, J. M., Fineberg, S., Fiser, A., Montagna, C., Medavarapu, R. et al. Expression, clinical significance, and receptor identification of the newest B7 family member HHLA2 protein. Clin. Cancer Res. 21, 2359–2366 (2015).
doi: 10.1158/1078-0432.CCR-14-1495
Koirala, P., Roth, M. E., Gill, J., Piperdi, S., Chinai, J. M., Geller, D. S. et al. Immune infiltration and PD-L1 expression in the tumor microenvironment are prognostic in osteosarcoma. Sci. Rep. 6, 30093 (2016).
doi: 10.1038/srep30093
Cheng, H., Janakiram, M., Borczuk, A., Lin, J., Qiu, W., Liu, H. et al. HHLA2, a new immune checkpoint member of the B7 family, is widely expressed in human lung cancer and associated with EGFR mutational status. Clin. Cancer Res. 23, 825–832 (2017).
doi: 10.1158/1078-0432.CCR-15-3071
Zhu, Z. & Dong, W. Overexpression of HHLA2, a member of the B7 family, is associated with worse survival in human colorectal carcinoma. Onco Targets Ther. 11, 1563–1570 (2018).
doi: 10.2147/OTT.S160493
Lin, G., Ye, H., Wang, J., Chen, S., Chen, X. & Zhang, C. Immune checkpoint human endogenous Retrovirus-H long terminal repeat-associating protein 2 is upregulated and independently predicts unfavorable prognosis in bladder urothelial carcinoma. Nephron 141, 256–264 (2019).
doi: 10.1159/000495887
Chen, D., Chen, W., Xu, Y., Zhu, M., Xiao, Y., Shen, Y. et al. Upregulated immune checkpoint HHLA2 in clear cell renal cell carcinoma: a novel prognostic biomarker and potential therapeutic target. J. Med. Genet. 56, 43–49 (2019).
doi: 10.1136/jmedgenet-2018-105454
Byers, J. T., Paniccia, A., Kaplan, J., Koenig, M., Kahn, N., Wilson, L. et al. Expression of the novel costimulatory molecule B7-H5 in pancreatic cancer. Ann. Surg Oncol. 22(Suppl 3), S1574–S1579 (2015).
doi: 10.1245/s10434-014-4293-2
Yan, H., Qiu, W., Koehne de Gonzalez, A. K., Wei, J. S., Tu, M., Xi, C. H. et al. HHLA2 is a novel immune checkpoint protein in pancreatic ductal adenocarcinoma and predicts post-surgical survival. Cancer Lett. 442, 333–340 (2019).
doi: 10.1016/j.canlet.2018.11.007
Sideras, K., Biermann, K., Yap, K., Mancham, S., Boor, P. P. C., Hansen, B. E. et al. Tumor cell expression of immune inhibitory molecules and tumor-infiltrating lymphocyte count predict cancer-specific survival in pancreatic and ampullary cancer. Int. J. Cancer 141, 572–582 (2017).
doi: 10.1002/ijc.30760
Sideras, K., Biermann, K., Verheij, J., Takkenberg, B. R., Mancham, S., Hansen, B. E. et al. PD-L1, Galectin-9 and CD8(+) tumor-infiltrating lymphocytes are associated with survival in hepatocellular carcinoma. Oncoimmunology. 6, e1273309 (2017).
doi: 10.1080/2162402X.2016.1273309
Zang, X. & Allison, J. P. The B7 family and cancer therapy: costimulation and coinhibition. Clin. Cancer Res. 13(18 Pt 1), 5271–5279 (2007).
doi: 10.1158/1078-0432.CCR-07-1030
Massi, D., Brusa, D., Merelli, B., Ciano, M., Audrito, V., Serra, S. et al. PD-L1 marks a subset of melanomas with a shorter overall survival and distinct genetic and morphological characteristics. Ann. Oncol. 25, 2433–2442 (2014).
doi: 10.1093/annonc/mdu452
Choueiri, T. K., Fay, A. P., Gray, K. P., Callea, M., Ho, T. H., Albiges, L. et al. PD-L1 expression in nonclear-cell renal cell carcinoma. Ann. Oncol. 25, 2178–2184 (2014).
doi: 10.1093/annonc/mdu445
Taube, J. M., Anders, R. A., Young, G. D., Xu, H., Sharma, R., McMiller, T. L. et al. Colocalization of inflammatory response with B7-h1 expression in human melanocytic lesions supports an adaptive resistance mechanism of immune escape. Sci. Transl. Med. 4, 127ra37 (2012).
doi: 10.1126/scitranslmed.3003689
Bertucci, F., Finetti, P., Mamessier, E., Pantaleo, M. A., Astolfi, A., Ostrowski, J. et al. PDL1 expression is an independent prognostic factor in localized GIST. Oncoimmunology 4, e1002729 (2015).
doi: 10.1080/2162402X.2014.1002729
Spranger, S., Spaapen, R. M., Zha, Y., Williams, J., Meng, Y., Ha, T. T. et al. Up-regulation of PD-L1, IDO, and T(regs) in the melanoma tumor microenvironment is driven by CD8(+) T cells. Sci. Transl. Med. 5, 200ra116 (2013).
doi: 10.1126/scitranslmed.3006504
Ribas, A. & Hu-Lieskovan, S. What does PD-L1 positive or negative mean? J. Exp. Med. 213, 2835–2840 (2016).
doi: 10.1084/jem.20161462

Auteurs

Patrick P C Boor (PPC)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands.

Kostandinos Sideras (K)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands.
Erasmus MC-University Medical Center, Department of Surgery, Rotterdam, The Netherlands.

Katharina Biermann (K)

Erasmus MC-University Medical Center, Department of Pathology, Rotterdam, The Netherlands.

M Hosein Aziz (M)

Erasmus MC-University Medical Center, Department of Surgery, Rotterdam, The Netherlands.

Iris J M Levink (IJM)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands.

Shanta Mancham (S)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands.

Nicole S Erler (NS)

Erasmus MC-University Medical Center, Department of Biostatistics, Rotterdam, The Netherlands.

Xudong Tang (X)

Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, USA.

Casper H van Eijck (CH)

Erasmus MC-University Medical Center, Department of Surgery, Rotterdam, The Netherlands.

Marco J Bruno (MJ)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands.

Dave Sprengers (D)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands.

Xingxing Zang (X)

Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, USA.

Jaap Kwekkeboom (J)

Erasmus MC-University Medical Center, Department of Gastroenterology and Hepatology, Rotterdam, The Netherlands. j.kwekkeboom@erasmusmc.nl.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH