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Inflammasomes in breast cancer: the ignition spark of progression and resistance?

Published online by Cambridge University Press:  20 June 2023

Sawsan Elgohary
Affiliation:
Clinical Pharmacology and Pharmacogenomics Research Group, Department of Pharmacology and Toxicology, Faculty of Pharmacy and Biotechnology, German University in Cairo, Cairo, Egypt
Hend M. El Tayebi*
Affiliation:
Clinical Pharmacology and Pharmacogenomics Research Group, Department of Pharmacology and Toxicology, Faculty of Pharmacy and Biotechnology, German University in Cairo, Cairo, Egypt
*
Corresponding author: Hend M. El Tayebi; Email: hend.saber@guc.edu.eg

Abstract

Inflammation and immune evasion are major key players in breast cancer (BC) progression. Recently, the FDA approved the use of anti-programmed death-ligand 1 antibody (anti-PD-L1) and phosphoinositide 3-kinase (PI3K) inhibitors against aggressive BC. Despite the paradigm shift in BC treatments, patients still suffer from resistance, recurrence and serious immune-related adverse events. These obstacles require unravelling of the hidden molecular contributors for such therapy failure hence yielding therapeutics that are at least as efficient yet safer. Inflammasome pathway is activated when the pattern recognition receptor senses danger signals (danger-associated molecular patterns) from damagedRdying cells or pathogen-associated molecular patterns found in microbes, leading to secretion of the active pro-inflammatory cytokines interleukin-1β (IL-1β) and interleukin-18 (IL-18). It has been shown throughout numerous studies that inflammasome pathway enhanced invasion, metastasis, provoked BC progression and therapy resistance. Additionally, inflammasomes upregulated the proliferative index ki67 and enhanced PD-L1 expression leading to immunotherapy resistance. IL-1β contributed to significant decrease in oestrogen receptor levels and promoted BC chemo-resistance. High levels of IL-18 in sera of BC patients were associated with worst prognosis. Stimulation of purinergic receptors and modulation of adipokines in obese subjects activated inflammasomes that evoked radiotherapy resistance and BC progression. The micro RNA miR-223-3p attenuated the inflammasome over-expression leading to lowered tumour volume and lessened angiogenesis in BC. This review sheds the light on the molecular pathways of inflammasomes and their impacts in distinct BC subtypes. In addition, it highlights novel strategies in treatment and prevention of BC.

Type
Review
Copyright
Copyright © The Author(s), 2023. Published by Cambridge University Press

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References

Sung, H et al. (2021) Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA: A Cancer Journal for Clinicians 71, 209249.Google ScholarPubMed
WHO (2020) Source: Globocan 2020. Globocan 2020.Google Scholar
Goldhirsch, A et al. (2011) Strategies for subtypes-dealing with the diversity of breast cancer: highlights of the St Gallen international expert consensus on the primary therapy of early breast cancer 2011. Annals of Oncology 22, 17361747.CrossRefGoogle ScholarPubMed
Cho, N (2016) Molecular subtypes and imaging phenotypes of breast cancer. Ultrasonography 35, 281288.CrossRefGoogle ScholarPubMed
Jiang, X and Shapiro, DJ (2014) The immune system and inflammation in breast cancer. Molecular and Cellular Endocrinology 382, 673682.CrossRefGoogle ScholarPubMed
Balkwill, F and Mantovani, A (2001) Inflammation and cancer: back to Virchow? Lancet 357, 539545.CrossRefGoogle ScholarPubMed
Dvorak, HF (1986) Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. New England Journal of Medicine 315, 16501659.Google Scholar
Coussens, LM and Werb, Z (2002) Inflammation and cancer. Nature 420, 860867.CrossRefGoogle ScholarPubMed
Brandão, RD et al. (2013) A randomised controlled phase II trial of pre-operative celecoxib treatment reveals anti-tumour transcriptional response in primary breast cancer. Breast Cancer Research: BCR 15, R29.CrossRefGoogle ScholarPubMed
Hussain, SP and Harris, CC (2007) Inflammation and cancer: an ancient link with novel potentials. International Journal of Cancer 121, 23732380.CrossRefGoogle ScholarPubMed
Dmitrieva, OS et al. (2016) Interleukins 1 and 6 as main mediators of inflammation and cancer. Biochemistry 81, 8090.Google ScholarPubMed
Hoesel, B and Schmid, JA (2013) The complexity of NF-κB signaling in inflammation and cancer. Molecular Cancer 12, 86.CrossRefGoogle ScholarPubMed
Serrano-del Valle, A et al. (2019) Immunogenic cell death and immunotherapy of multiple myeloma. Frontiers in Cell and Developmental Biology 7, 50.CrossRefGoogle ScholarPubMed
Matzinger, P (1994) Tolerance, danger, and the extended family. Annual Review of Immunology 12, 9911045.CrossRefGoogle ScholarPubMed
Matzinger, P (2002) The danger model: a renewed sense of self. Science 296, 301305.CrossRefGoogle Scholar
Obeid, M et al. (2007) Calreticulin exposure is required for the immunogenicity of γ-irradiation and UVC light-induced apoptosis [5]. Cell Death and Differentiation 14, 18481850.CrossRefGoogle ScholarPubMed
Zitvogel, L et al. (2008) Immunological aspects of cancer chemotherapy. Nature Reviews Immunology 8, 5973.CrossRefGoogle ScholarPubMed
Amin, J, Boche, D and Rakic, S (2017) What do we know about the inflammasome in humans? Brain Pathology 27, 192204.CrossRefGoogle ScholarPubMed
Sendler, M et al. (2020) NLRP3 inflammasome regulates development of systemic inflammatory response and compensatory anti-inflammatory response syndromes in mice with acute pancreatitis. Gastroenterology 158, 253269.CrossRefGoogle ScholarPubMed
Karki, R, Man, SM and Kanneganti, T-D (2017) Inflammasomes and cancer. Cancer Immunology Research [Internet] 5, 9499. Available at http://cancerimmunolres.aacrjournals.org/lookup/doi/10.1158/2326-6066.CIR-16-0269.CrossRefGoogle ScholarPubMed
Inoue, N et al. (2019) High serum levels of interleukin-18 are associated with worse outcomes in patients with breast cancer. Anticancer Research 39, 50095018.CrossRefGoogle ScholarPubMed
Krelin, Y et al. (2007) Interleukin-1β-driven inflammation promotes the development and invasiveness of chemical carcinogen-induced tumors. Cancer Research 67, 10621071.CrossRefGoogle ScholarPubMed
Jin, H, Shin Ko, Y and Kim, HJ (2018) P2Y2R-mediated inflammasome activation is involved in tumor progression in breast cancer cells and in radiotherapy-resistant breast cancer. International Journal of Oncology 53, 19531966.Google ScholarPubMed
Raut, PK et al. (2019) Growth of breast cancer cells by leptin is mediated via activation of the inflammasome: critical roles of estrogen receptor signaling and reactive oxygen species production. Biochemical Pharmacology 161, 7388.CrossRefGoogle ScholarPubMed
Zhang, L et al. (2019) NLRP3 inflammasome inactivation driven by miR-223-3p reduces tumor growth and increases anticancer immunity in breast cancer. Molecular Medicine Reports 19, 21802188.Google ScholarPubMed
Su, S et al. (2018) Immune checkpoint inhibition overcomes ADCP-induced immunosuppression by macrophages. Cell 175, 442457.CrossRefGoogle ScholarPubMed
Kaplanov, I et al. (2019) Blocking IL-1β reverses the immunosuppression in mouse breast cancer and synergizes with anti-PD-1 for tumor abrogation. Proceedings of the National Academy of Sciences of the USA 116, 13611369.CrossRefGoogle ScholarPubMed
Marvastzas A, et al. (2019) FDA approves atezolizumab for PD-L1 positive unresectable locally advanced or metastatic triple-negative breast cancer. Case Medical Research 16, 44394453.Google Scholar
Schmid, P et al. (2020) Atezolizumab plus nab-paclitaxel as first-line treatment for unresectable, locally advanced or metastatic triple-negative breast cancer (IMpassion130): updated efficacy results from a randomised, double-blind, placebo-controlled, phase 3 trial. The Lancet. Oncology 21, 4459.CrossRefGoogle ScholarPubMed
Martinon, F, Burns, K and Tschopp, J (2002) The inflammasome: a molecular platform triggering activation of inflammatory {…}. Molecular Cell 10, 417426.CrossRefGoogle ScholarPubMed
Stutz, A et al. (2013) ASC speck formation as a readout for inflammasome activation. Methods in molecular biology .1040 91–101.CrossRefGoogle Scholar
Schroder, K and Tschopp, J (2010) The inflammasomes. Cell 140, 821832.CrossRefGoogle ScholarPubMed
Deets, KA and Vance, RE (2021) Inflammasomes and adaptive immune responses. Nature Immunology 22, 412422.CrossRefGoogle ScholarPubMed
Heilig, R and Broz, P (2018) Function and mechanism of the pyrin inflammasome. European Journal of Immunology 48, 230238.CrossRefGoogle ScholarPubMed
Lupfer, C, Malik, A and Kanneganti, TD (2015) Inflammasome control of viral infection. Current Opinion in Virology 12, 3846.CrossRefGoogle ScholarPubMed
Man, SM and Kanneganti, TD (2016) Converging roles of caspases in inflammasome activation, cell death and innate immunity. Nature Reviews Immunology 16, 721.CrossRefGoogle ScholarPubMed
Shi, J et al. (2014) Inflammatory caspases are innate immune receptors for intracellular LPS. Nature 514, 187192.CrossRefGoogle ScholarPubMed
Baker, PJ et al. (2015) NLRP3 inflammasome activation downstream of cytoplasmic LPS recognition by both caspase-4 and caspase-5. European Journal of Immunology 45, 29182926.CrossRefGoogle ScholarPubMed
Amarante-Mendes, GP et al. (2018) Pattern recognition receptors and the host cell death molecular machinery. Frontiers in Immunology 9, 2379.CrossRefGoogle ScholarPubMed
Kim, YK, Shin, JS and Nahm, MH (2016) NOD-like receptors in infection, immunity, and diseases. Yonsei Medical Journal 57, 514.CrossRefGoogle ScholarPubMed
Downs, KP et al. (2020) An overview of the non-canonical inflammasome. Molecular Aspects of Medicine 76, 100924.CrossRefGoogle ScholarPubMed
Hu, Q et al. (2017) Polymeric nanoparticles induce NLRP3 inflammasome activation and promote breast cancer metastasis. Macromolecular Bioscience 17. doi: 10.1002/mabi.201700273.CrossRefGoogle ScholarPubMed
Wei, Y et al. (2017) NLRP1 overexpression is correlated with the tumorigenesis and proliferation of human breast tumor. Biomed Research International 2017, 4938473.CrossRefGoogle ScholarPubMed
Kolb, R et al. (2016) Obesity-associated NLRC4 inflammasome activation drives breast cancer progression. Nature Communications 7, 13007.CrossRefGoogle ScholarPubMed
Hashmi, AA et al. (2019) Ki67 index in intrinsic breast cancer subtypes and its association with prognostic parameters. BMC Research Notes 12, 605.CrossRefGoogle ScholarPubMed
Zheng, Q et al. (2020) NLRP3 augmented resistance to gemcitabine in triple-negative breast cancer cells via EMT/IL-1β/Wnt/β-catenin signaling pathway. Bioscience Reports 40, BSR20200730.CrossRefGoogle ScholarPubMed
Yao, M et al. (2019) Berberine inhibits NLRP3 inflammasome pathway in human triple-negative breast cancer MDA-MB-231 cell. BMC Complementary and Alternative Medicine 19, 216.CrossRefGoogle ScholarPubMed
Deng, R et al. (2021) MAPK1/3 kinase-dependent ULK1 degradation attenuates mitophagy and promotes breast cancer bone metastasis. Autophagy 17, 30113029.CrossRefGoogle ScholarPubMed
Sarmiento-Salinas, FL et al. (2019) Breast cancer subtypes present a differential production of reactive oxygen species (ROS) and susceptibility to antioxidant treatment. Frontiers in Oncology 9, 480.CrossRefGoogle Scholar
Wang, T et al. (2019) Inhibition of murine breast cancer metastases by hydrophilic As4S4 nanoparticles is associated with decreased ROS and HIF-1α downregulation. Frontiers in Oncology 9, 333.CrossRefGoogle ScholarPubMed
Tang, J et al. (2021) Acute cadmium exposure induces GSDME-mediated pyroptosis in triple-negative breast cancer cells through ROS generation and NLRP3 inflammasome pathway activation. Environmental Toxicology and Pharmacology 87, 103686.CrossRefGoogle ScholarPubMed
Han, B et al. (2021) Elemene nanoemulsion inhibits metastasis of breast cancer by ROS scavenging. International Journal of Nanomedicine 16, 60356048.CrossRefGoogle ScholarPubMed
Si, L et al. (2020) Silibinin inhibits migration and invasion of breast cancer MDA-MB-231 cells through induction of mitochondrial fusion. Molecular and Cellular Biochemistry 463, 189201.CrossRefGoogle ScholarPubMed
Zhang, F et al. (2021) The antitriple negative breast cancer efficacy of Spatholobus suberectus Dunn on ROS-induced noncanonical inflammasome pyroptotic pathway. Oxidative Medicine and Cellular Longevity 2021, 5187569.CrossRefGoogle ScholarPubMed
Chen, IF et al. (2006) AIM2 suppresses human breast cancer cell proliferation in vitro and mammary tumor growth in a mouse model. Molecular Cancer Therapeutics 5, 17.CrossRefGoogle ScholarPubMed
Liu, ZY, Yi, J and Liu, FE (2015) The molecular mechanism of breast cancer cell apoptosis induction by absent in melanoma (AIM2). International Journal of Clinical and Experimental Medicine 8, 1475014758.Google ScholarPubMed
North, RJ et al. (1988) Interleukin 1-induced, T cell-mediated regression of immunogenic murine tumors: requirement for an adequate level of already acquired host concomitant immunity. Journal of Experimental Medicine 168, 20312043.CrossRefGoogle ScholarPubMed
Ben-Sasson, SZ et al. (2013) IL-1 enhances expansion, effector function, tissue localization, and memory response of antigen-specific CD8T cells. Journal of Experimental Medicine 210, 491502.CrossRefGoogle Scholar
Honma, S et al. (2002) The influence of inflammatory cytokines on estrogen production and cell proliferation in human breast cancer cells. Endocrine Journal 49, 371377.CrossRefGoogle ScholarPubMed
Todorović-Raković, N et al. (2018) The time-dependent prognostic value of intratumoral cytokine expression profiles in a natural course of primary breast cancer with a long-term follow-up. Cytokine 102, 1217.CrossRefGoogle Scholar
Paquette, B, Therriault, H and Wagner, JR (2013) Role of interleukin-1β in radiation-enhancement of MDA-MB-231 breast cancer cell invasion. Radiation Research 180, 292298.CrossRefGoogle ScholarPubMed
Mendoza-Rodríguez, MG et al. (2019) IL-1β inflammatory cytokine-induced TP63 isoform ΔNP63α signaling cascade contributes to cisplatin resistance in human breast cancer cells. International Journal of Molecular Sciences 20, 270.CrossRefGoogle ScholarPubMed
Mendoza-Rodríguez, M et al. (2017) IL-1β induces up-regulation of BIRC3, a gene involved in chemoresistance to doxorubicin in breast cancer cells. Cancer Letters 390, 3944.CrossRefGoogle ScholarPubMed
Jiménez-Garduño, AM et al. (2017) IL-1β induced methylation of the estrogen receptor ERα gene correlates with EMT and chemoresistance in breast cancer cells. Biochemical and Biophysical Research Communications 409, 780785.CrossRefGoogle Scholar
De La Cruz, LM et al. (2018) Impact of neoadjuvant chemotherapy on breast cancer subtype: does subtype change and, if so, how? IHC profile and neoadjuvant chemotherapy. Annals of Surgical Oncology 25, 35353540.CrossRefGoogle ScholarPubMed
Lim, SK et al. (2016) Impact of molecular subtype conversion of breast cancers after neoadjuvant chemotherapy on clinical outcome. Cancer Research and Treatment 48, 133141.CrossRefGoogle ScholarPubMed
Zhao, W et al. (2021) Receptor conversion impacts outcomes of different molecular subtypes of primary breast cancer. Therapeutic Advances in Medical Oncology 13, 17588359211012982.CrossRefGoogle ScholarPubMed
Al-Saleh, K et al. (2021) Prognostic significance of estrogen, progesterone and HER2 receptors’ status conversion following neoadjuvant chemotherapy in patients with locally advanced breast cancer: results from a tertiary cancer center in Saudi Arabia. PLoS ONE 16, e0247802.CrossRefGoogle ScholarPubMed
Nakamura, K et al. (1989) Endotoxin-induced serum factor that stimulates gamma interferon production. Infection and Immunity 57, 590595.CrossRefGoogle ScholarPubMed
Kuppala, MB et al. (2012) Immunotherapeutic approach for better management of cancer – role of IL-18. Asian Pacific Journal of Cancer Prevention 13, 53535361.CrossRefGoogle ScholarPubMed
Fabbi, M, Carbotti, G and Ferrini, S (2015) Context-dependent role of IL-18 in cancer biology and counter-regulation by IL-18BP. Journal of Leukocyte Biology 97, 665675.CrossRefGoogle ScholarPubMed
Nakata, A et al. (1999) Inhibition by interleukin 18 of osteolytic bone metastasis by human breast cancer cells. Anticancer Research 19, 41314138.Google ScholarPubMed
Okano, F and Yamada, K (2000) Canine interleukin-18 induces apoptosis and enhances fas ligand mRNA expression in a canine carcinoma cell line. Anticancer Research 20, 34113415.Google Scholar
Liu, X et al. (2015) Mesenchymal stem cells expressing interleukin-18 suppress breast cancer cells in vitro. Experimental and Therapeutic Medicine 9, 11921200.CrossRefGoogle ScholarPubMed
Autenshlyus, AI et al. (2021) Cytokine production by tumor bioptate at different pathological prognostic stages in breast cancer. Doklady Biochemistry and Biophysics 497, 8689.CrossRefGoogle ScholarPubMed
Li, K et al. (2016) Leptin promotes breast cancer cell migration and invasion via IL-18 expression and secretion. International Journal of Oncology 48, 24792487.CrossRefGoogle ScholarPubMed
Bel'skaya, LV, Loginova, AI and Sarf, EA (2022) Pro-inflammatory and anti-inflammatory salivary cytokines in breast cancer: relationship with clinicopathological characteristics of the tumor. Current Issues in Molecular Biology [Internet] 44, 46764691. Available at https://www.mdpi.com/1467-3045/44/10/319CrossRefGoogle ScholarPubMed
Merendino, RA et al. (2001) Serum levels of interleukin-18 and sICAM-1 in patients affected by breast cancer: preliminary considerations. International Journal of Biological Markers 16, 126129.CrossRefGoogle ScholarPubMed
Ma, T and Kong, M (2021) Interleukin-18 and -10 may be associated with lymph node metastasis in breast cancer. Oncology Letters 21, 253.CrossRefGoogle ScholarPubMed
Kunts, TA et al. (2016) Effect of polyclonal activators on cytokine production by blood cells and by malignant breast cancer cells. Doklady Biological Sciences 466, 4547.CrossRefGoogle ScholarPubMed
El-Deeb, MMK, El-Sheredy, HG and Mohammed, AF (2019) The possible role of interleukin (IL)-18 and nitrous oxide and their relation to oxidative stress in the development and progression of breast cancer. Asian Pacific Journal of Cancer Prevention 20, 26592665.CrossRefGoogle ScholarPubMed
Yang, Y et al. (2015) Interleukin-18 enhances breast cancer cell migration via down-regulation of claudin-12 and induction of the p38 MAPK pathway. Biochemical and Biophysical Research Communications 459, 379386.CrossRefGoogle ScholarPubMed
Park, S et al. (2009) Interleukin-18 induces transferrin expression in breast cancer cell line MCF-7. Cancer Letters 286, 189.CrossRefGoogle ScholarPubMed
Jung, MY et al. (2009) Analysis of the expression profiles of cytokines and cytokine-related genes during the progression of breast cancer growth in mice. Oncology Reports 22, 11411147.Google ScholarPubMed
Metwally, FM, El-Mezayen, HA and Ahmed, HH (2011) Significance of vascular endothelial growth factor, interleukin-18 and nitric oxide in patients with breast cancer: correlation with carbohydrate antigen 15.3. Medical Oncology 28, 1521.CrossRefGoogle ScholarPubMed
Eissa, SAL et al. (2005) Importance of serum IL-18 and RANTES as markers for breast carcinoma progression. Journal of the Egyptian National Cancer Institute 17, 5155.Google ScholarPubMed
Perel'muter, VM et al. (2008) Genetic and clinical and pathological characteristics of breast cancer in premenopausal and postmenopausal women. Advances in Gerontology 21, 643653.Google ScholarPubMed
Qader, G et al. (2020) Cardiac, hepatic and renal dysfunction and IL-18 polymorphism in breast, colorectal, and prostate cancer patients. Asian Pacific Journal of Cancer Prevention 22, 131137.CrossRefGoogle Scholar
Xu, G and Wang, F (2020) Associations of polymorphisms in interleukins with susceptibility to breast cancer: evidence from a meta-analysis. Cytokine 130, 154988.CrossRefGoogle ScholarPubMed
Li, X et al. (2015) Increased cancer risk associated with the -607C/A polymorphism in interleukin-18 gene promoter: an updated meta-analysis including 12,502 subjects. Journal of B.U.ON. 20, 902917.Google ScholarPubMed
Back, LKDC et al. (2014) Functional polymorphisms of interleukin-18 gene and risk of breast cancer in a Brazilian population. Tissue Antigens 84, 229233.CrossRefGoogle Scholar
Zhou, Y et al. (2022) Effect of pyroptosis-related genes on the prognosis of breast cancer. Frontiers in Oncology [Internet]. 12, 948169.CrossRefGoogle ScholarPubMed
Srabović, N et al. (2011) Interleukin 18 expression in the primary breast cancer tumour tissue. Medicinski Glasnik 8, 109115.Google ScholarPubMed
Turchaninova, MA et al. (2011) [Characterization of circulating RNA in plasma as potential tool for breast cancer diagnostics]. Bioorganicheskaya Khimiya 37, 393398.Google ScholarPubMed
Günel, N et al. (2003) Prognostic value of serum IL-18 and nitric oxide activity in breast cancer patients at operable stage. American Journal of Clinical Oncology 26, 416421.CrossRefGoogle ScholarPubMed
Wang, Z et al. (2022) A pyroptosis-related gene signature predicts prognosis and immune microenvironment for breast cancer based on computational biology techniques. Frontiers in Genetics [Internet]. 13, 801056.CrossRefGoogle ScholarPubMed
Yao, L et al. (2011) Discovery of IL-18 as a novel secreted protein contributing to doxorubicin resistance by comparative secretome analysis of MCF-7 and MCF-7/Dox. PLoS ONE 6, e24684.CrossRefGoogle ScholarPubMed
Tiainen, L et al. (2019) Low plasma IL-8 levels during chemotherapy are predictive of excellent long-term survival in metastatic breast cancer. Clinical Breast Cancer 19, e522e533.CrossRefGoogle ScholarPubMed
Gicquel, T et al. (2017) Purinergic receptors: new targets for the treatment of gout and fibrosis. Fundamental and Clinical Pharmacology 31, 136146.CrossRefGoogle ScholarPubMed
Burnstock, G (2020) Introduction to purinergic signalling in the brain. Advances in Experimental Medicine and Biology 1202, 112.CrossRefGoogle ScholarPubMed
Ralevic, V and Dunn, WR (2015) Purinergic transmission in blood vessels. Autonomic Neuroscience: Basic and Clinical 191, 4866.CrossRefGoogle ScholarPubMed
Sriram, K and Insel, PA (2021) Inflammation and thrombosis in covid-19 pathophysiology: proteinase-activated and purinergic receptors as drivers and candidate therapeutic targets. Physiological Reviews 101, 545567.CrossRefGoogle ScholarPubMed
Schäfer, R et al. (2003) ATP- and UTP-activated P2Y receptors differently regulate proliferation of human lung epithelial tumor cells. The American Journal of Physiology-Lung Cellular and Molecular Physiology 285, L376L385.CrossRefGoogle ScholarPubMed
Shabbir, M et al. (2008) Purinergic receptor-mediated effects of ATP in high-grade bladder cancer. BJU International 101, 106112.Google ScholarPubMed
Janssens, R and Boeynaems, JM (2001) Effects of extracellular nucleotides and nucleosides on prostate carcinoma cells. British Journal of Pharmacology 132, 536546.CrossRefGoogle ScholarPubMed
Kim, DC et al. (2020) P2Y2R has a significant correlation with Notch-4 in patients with breast cancer. Oncology Letters 20, 647654.CrossRefGoogle Scholar
Burnstock, G (2007) Purine and pyrimidine receptors. Cellular and Molecular Life Sciences 64, 14711483.CrossRefGoogle ScholarPubMed
Reed, JC (1999 Jan) Mechanisms of apoptosis avoidance in cancer. Current Opinion in Oncology 11, 6875.CrossRefGoogle ScholarPubMed
Suganuma, M et al. (1999) Essential role of tumor necrosis factor α (TNF-α) in tumor promotion as revealed by TNF-α-deficient mice. Cancer Research 59, 45164518.Google ScholarPubMed
Egberts, JH et al. (2008) Anti-tumor necrosis factor therapy inhibits pancreatic tumor growth and metastasis. Cancer Research 68, 14431450.CrossRefGoogle ScholarPubMed
Duan, S et al. (2021) Extracellular vesicle-mediated purinergic signaling contributes to host microenvironment plasticity and metastasis in triple negative breast cancer. International Journal of Molecular Sciences 22, 597.CrossRefGoogle ScholarPubMed
Azimi, I et al. (2016) Altered purinergic receptor-Ca2+ signaling associated with hypoxia-induced epithelial-mesenchymal transition in breast cancer cells. Molecular Oncology 10, 166178.CrossRefGoogle ScholarPubMed
Yokdang, N et al. (2015) Blockade of extracellular NM23 or its endothelial target slows breast cancer growth and metastasis. Integrative Cancer Science and Therapeutics 2, 192200.CrossRefGoogle ScholarPubMed
Yokdang, N et al. (2011) A role for nucleotides in support of breast cancer angiogenesis: heterologous receptor signalling. British Journal of Cancer 104, 16281640.CrossRefGoogle ScholarPubMed
Bilbao, PS, Santillán, G and Boland, R (2010) ATP stimulates the proliferation of MCF-7 cells through the PI3K/Akt signaling pathway. Archives of Biochemistry and Biophysics 499, 4048.CrossRefGoogle ScholarPubMed
Liu, X et al. (2021) Atp inhibits breast cancer migration and bone metastasis through down-regulation of cxcr4 and purinergic receptor p2y11. Cancers 13, 4293.CrossRefGoogle ScholarPubMed
Wright, JR et al. (2020) The TICONC (Ticagrelor-Oncology) study: implications of P2Y12 inhibition for metastasis and cancer-associated thrombosis. JACC CardioOncology 2, 236250.CrossRefGoogle ScholarPubMed
Cantley, LC (2002) The phosphoinositide 3-kinase pathway. Science 296, 16551657.CrossRefGoogle ScholarPubMed
Jin, H et al. (2014) P2Y2 receptor activation by nucleotides released from highly metastatic breast cancer cells increases tumor growth and invasion via crosstalk with endothelial cells. Breast Cancer Research: BCR 16, R77.CrossRefGoogle ScholarPubMed
Joo, YN et al. (2014) P2Y2R activation by nucleotides released from the highly metastatic breast cancer cell contributes to pre-metastatic niche formation by mediating lysyl oxidase secretion, collagen crosslinking, and monocyte recruitment. Oncotarget 5, 93229334.CrossRefGoogle ScholarPubMed
Eun, SY et al. (2015) P2Y2 nucleotide receptor-mediated extracellular signal-regulated kinases and protein kinase C activation induces the invasion of highly metastatic breast cancer cells. Oncology Reports 34, 195202.CrossRefGoogle ScholarPubMed
Jin, H and Kim, HJ (2020) NLRC4, ASC and Caspase-1 are inflammasome components that are mediated by P2Y2R activation in breast cancer cells. International Journal of Molecular Sciences 21, 3337.CrossRefGoogle ScholarPubMed
Korcok, J et al. (2004) Extracellular nucleotides act through P2X7 receptors to activate NF-κB in osteoclasts. Journal of Bone and Mineral Research 19, 642651.CrossRefGoogle ScholarPubMed
Ferrari, D et al. (1997) Extracellular ATP activates transcription factor NF-κB through the P2Z purinoreceptor by selectively targeting NF-κB p65 (RelA). Journal of Cell Biology 139, 16351643.CrossRefGoogle Scholar
Oida, K et al. (2014) Nuclear factor-κB plays a critical role in both intrinsic and acquired resistance against endocrine therapy in human breast cancer cells. Scientific Reports 4, 4057.CrossRefGoogle Scholar
Pantschenko, AG et al. (2003) The interleukin-1 family of cytokines and receptors in human breast cancer: implications for tumor progression. International Journal of Oncology 23, 269284.Google ScholarPubMed
Radisky, ES and Radisky, DC (2010) Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer. Journal of Mammary Gland Biology and Neoplasia 15, 201212.CrossRefGoogle ScholarPubMed
Yokoo, T and Kitamura, M (1996) Dual regulation of IL-1β-mediated matrix metalloproteinase-9 expression in mesangial cells by NF-KB and AP-1. American Journal of Physiology 270, F123F130.Google Scholar
Ruhul Amin, ARM et al. (2003) Secretion of matrix metalloproteinase-9 by the proinflammatory cytokine, IL-1β: a role for the dual signalling pathways, Akt and Erk. Genes to Cells 8, 515523.CrossRefGoogle ScholarPubMed
Ferrara, N (2004) Vascular endothelial growth factor: basic science and clinical progress. Endocrine Reviews 25, 581611.CrossRefGoogle ScholarPubMed
Allavena, P et al. (2008) The Yin-Yang of tumor-associated macrophages in neoplastic progression and immune surveillance. Immunological Reviews 222, 155161.CrossRefGoogle ScholarPubMed
Claesson-Welsh, L and Welsh, M (2013) VEGFA and tumour angiogenesis. Journal of Internal Medicine 273, 114127.CrossRefGoogle ScholarPubMed
Takahashi, T et al. (2001) A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-γ and DNA synthesis in vascular endothelial cells. EMBO Journal 20, 27682778.CrossRefGoogle ScholarPubMed
Guerrero-Zotano, A, Mayer, IA and Arteaga, CL (2016) PI3K/AKT/mTOR: role in breast cancer progression, drug resistance, and treatment. Cancer and Metastasis Reviews 35, 515524.CrossRefGoogle ScholarPubMed
Papa, A and Pandolfi, PP (2019) The pten–pi3k axis in cancer. Biomolecules 9, 153.CrossRefGoogle ScholarPubMed
Park, JH et al. (2020) Cigarette smoke extract stimulates mmp-2 production in nasal fibroblasts via ros/pi3k, akt, and nf-κb signaling pathways. Antioxidants 9, 739.CrossRefGoogle ScholarPubMed
Chen, JS et al. (2009) Involvement of PI3K/PTEN/AKT/mTOR pathway in invasion and metastasis in hepatocellular carcinoma: association with MMP-9. Hepatology Research: The Official Journal of the Japan Society of Hepatology 39, 177186.CrossRefGoogle ScholarPubMed
Markham, A (2019) Alpelisib: first global approval. Drugs 79, 12491253.CrossRefGoogle ScholarPubMed
Marín-Aguilar, F et al. (2020) NLRP3 inflammasome suppression improves longevity and prevents cardiac aging in male mice. Aging Cell 19, e13050.CrossRefGoogle ScholarPubMed
Müller, CE, Baqi, Y and Namasivayam, V (2020) Agonists and antagonists for purinergic receptors. Methods in Molecular Biology (Clifton, N.J.) 2041, 4564.CrossRefGoogle ScholarPubMed
Chou, WC et al. (2022) Impact of intracellular innate immune receptors on immunometabolism. Cellular and Molecular Immunology 19, 337351.CrossRefGoogle ScholarPubMed
Cai, Y et al. (2021) Genomic alterations in PIK3CA-mutated breast cancer result in mTORC1 activation and limit the sensitivity to PI3Ka inhibitors. Cancer Research 81, 24702480.CrossRefGoogle Scholar
Thangavel, C et al. (2011) Therapeutically activating RB: reestablishing cell cycle control in endocrine therapy-resistant breast cancer. Endocrine-Related Cancer 18, 333345.CrossRefGoogle ScholarPubMed
Pi, S et al. (2021) The P2RY12 receptor promotes VSMC-derived foam cell formation by inhibiting autophagy in advanced atherosclerosis. Autophagy 17, 9801000.CrossRefGoogle ScholarPubMed
Fuller, RA and Chavez, B (2012) Ticagrelor (brilinta), an antiplatelet drug for acute coronary syndrome. P & T 37, 562568.Google ScholarPubMed
Nieswandt, B et al. (1999) Lysis of tumor cells by natural killer cells in mice is impeded by platelets. Cancer Research 59, 12951300.Google ScholarPubMed
Gareau, AJ et al. (2018) Ticagrelor inhibits platelet–tumor cell interactions and metastasis in human and murine breast cancer. Clinical & Experimental Metastasis 35, 2535.CrossRefGoogle ScholarPubMed
Denslow, A et al. (2017) Clopidogrel in a combined therapy with anticancer drugs – effect on tumor growth, metastasis, and treatment toxicity: studies in animal models. PLoS ONE 12, e0188740.CrossRefGoogle Scholar
Borges-Rodriguez, M et al. (2021) Platelet inhibition prevents nlrp3 inflammasome activation and sepsis-induced kidney injury. International Journal of Molecular Sciences 22, 10330.CrossRefGoogle ScholarPubMed
Huang, B et al. (2021) Ticagrelor inhibits the NLRP3 inflammasome to protect against inflammatory disease independent of the P2Y12 signaling pathway. Cellular & Molecular Immunology 18, 12781289.CrossRefGoogle ScholarPubMed
Slater, M et al. (2004) Differentiation between cancerous and normal hyperplastic lobules in breast lesions. Breast Cancer Research and Treatment 83, 110.CrossRefGoogle ScholarPubMed
Davis, FM et al. (2011) Remodeling of purinergic receptor-mediated Ca 2+ signaling as a consequence of EGF-induced epithelial-mesenchymal transition in breast cancer cells. PLoS ONE 6, e23464.CrossRefGoogle ScholarPubMed
Tan, C et al. (2015) Expression of P2X7R in breast cancer tissue and the induction of apoptosis by the gene-specific shRNA in MCF-7 cells. Experimental and Therapeutic Medicine 10, 14721478.CrossRefGoogle ScholarPubMed
Zheng, L et al. (2014) Regulation of the P2X7R by microRNA-216b in human breast cancer. Biochemical and Biophysical Research Communications 452, 197204.CrossRefGoogle ScholarPubMed
Jelassi, B et al. (2011) P2X 7 receptor activation enhances SK3 channels- and cystein cathepsin-dependent cancer cells invasiveness. Oncogene 30, 21082122.CrossRefGoogle ScholarPubMed
Tafani, M et al. (2011) Hypoxia-increased RAGE and P2X7R expression regulates tumor cell invasion through phosphorylation of Erk1/2 and Akt and nuclear translocation of NF-κB. Carcinogenesis 32, 11671175.CrossRefGoogle Scholar
Dolcet, X et al. (2005) NF-kB in development and progression of human cancer. Virchows Archiv 446, 475482.CrossRefGoogle ScholarPubMed
Xia, J et al. (2015) P2X7 receptor stimulates breast cancer cell invasion and migration via the AKT pathway. Oncology Reports 34, 103110.CrossRefGoogle ScholarPubMed
Brisson, L et al. (2020) P2X7 receptor promotes mouse mammary cancer cell invasiveness and tumour progression, and is a target for anticancer treatment. Cancers 12, 2342.CrossRefGoogle ScholarPubMed
Jelassi, B et al. (2013) Anthraquinone emodin inhibits human cancer cell invasiveness by antagonizing P2X7 receptors. Carcinogenesis 34, 14871496.CrossRefGoogle ScholarPubMed
Avanzato, D et al. (2016) Activation of P2X7 and P2Y11 purinergic receptors inhibits migration and normalizes tumor-derived endothelial cells via cAMP signaling. Scientific Reports 6, 32602.CrossRefGoogle ScholarPubMed
Wu, P et al. (2022) P2X7 receptor-induced bone cancer pain by regulating microglial activity via NLRP3/IL-1beta signaling. Pain Physician 25, E1199E1210.Google ScholarPubMed
Ghiringhelli, F et al. (2009) Activation of the NLRP3 inflammasome in dendritic cells induces IL-1Β-dependent adaptive immunity against tumors. Nature Medicine 15, 11701178.CrossRefGoogle ScholarPubMed
Lebreton, F et al. (2018) NLRP3 inflammasome is expressed and regulated in human islets article. Cell Death & Disease 9, 726.CrossRefGoogle Scholar
Kinoshita, T et al. (2015) NLRP3 mediates NF-κB activation and cytokine induction in microbially induced and sterile inflammation. PLoS ONE 10, e0119179.CrossRefGoogle ScholarPubMed
Chen, K et al. (2013) ATP-P2X4 signaling mediates NLRP3 inflammasome activation: a novel pathway of diabetic nephropathy. International Journal of Biochemistry & Cell Biology 45, 932943.CrossRefGoogle ScholarPubMed
Wiedemar, N, Hauser, DA and Mäser, P (2020) 100 Years of suramin. Antimicrobial Agents and Chemotherapy 64, e01168-19.CrossRefGoogle ScholarPubMed
Sahu, D et al. (2012) Suramin ameliorates collagen induced arthritis. International Immunopharmacology 12, 288293.CrossRefGoogle ScholarPubMed
Oda, K et al. (2022) Suramin prevents the development of diabetic kidney disease by inhibiting {NLRP3} inflammasome activation in {KK-Ay} mice. Journal of Diabetes Investigation 14, 205220.CrossRefGoogle ScholarPubMed
Menze, ET et al. (2021) Simvastatin mitigates depressive-like behavior in ovariectomized rats: possible role of NLRP3 inflammasome and estrogen receptors’ modulation. International Immunopharmacology 95, 107582.CrossRefGoogle ScholarPubMed
Rezano, A et al. (2021) Cytotoxicity of simvastatin in human breast cancer MCF-7 and MDA-MB-231 cell lines. Asian Pacific Journal of Cancer Prevention 22, 3342.CrossRefGoogle ScholarPubMed
Ribeiro, DE et al. (2021) Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology. Molecular Psychiatry 26, 10441059.CrossRefGoogle ScholarPubMed
Ghiringhelli, F et al. (2009) Activation of the NLRP3 inflammasome in dendritic cells induces IL-1β-dependent adaptive immunity against tumors. Nature Medicine 15, 11701178.CrossRefGoogle ScholarPubMed
Zhou, JZ et al. (2014) Differential impact of adenosine nucleotides released by osteocytes on breast cancer growth and bone metastasis. Oncogene 34, 18311842.CrossRefGoogle ScholarPubMed
Fiorillo, M et al. (2021) High ATP production fuels cancer drug resistance and metastasis: implications for mitochondrial ATP depletion therapy. Frontiers in Oncology 11, 740720.CrossRefGoogle ScholarPubMed
Pardoll, DM (2012) The blockade of immune checkpoints in cancer immunotherapy. Nature Reviews Cancer 12, 252264.CrossRefGoogle ScholarPubMed
Schütz, F et al. (2017) PD-1/PD-L1 pathway in breast cancer. Oncology Research and Treatment 40, 294297.CrossRefGoogle ScholarPubMed
Kwa, MJ and Adams, S (2018) Checkpoint inhibitors in triple-negative breast cancer (TNBC): where to go from here. Cancer 124, 20862103.CrossRefGoogle Scholar
Ballas, ZK (2018) The 2018 Nobel Prize in physiology or medicine: an exemplar of bench to bedside in immunology. Journal of Allergy and Clinical Immunology 142, 17521753.CrossRefGoogle ScholarPubMed
Esteva, FJ et al. (2019) Immunotherapy and targeted therapy combinations in metastatic breast cancer. The Lancet Oncology 20, e175e186.CrossRefGoogle ScholarPubMed
Katz, H and Alsharedi, M (2018) Immunotherapy in triple-negative breast cancer. Medical Oncology 35, 13.CrossRefGoogle Scholar
O'Donnell, JS et al. (2017) Resistance to PD1/PDL1 checkpoint inhibition. Cancer Treatment Reviews 52, 7181.CrossRefGoogle ScholarPubMed
Postow, MA, Callahan, MK and Wolchok, JD (2015) Immune checkpoint blockade in cancer therapy. Journal of Clinical Oncology 33, 19741982.CrossRefGoogle ScholarPubMed
Chen, L et al. (2018) Blockage of the NLRP3 inflammasome by MCC950 improves anti-tumor immune responses in head and neck squamous cell carcinoma. Cellular and Molecular Life Sciences 75, 20452058.CrossRefGoogle ScholarPubMed
Theivanthiran, B et al. (2020) A tumor-intrinsic PD-L1/NLRP3 inflammasome signaling pathway drives resistance to anti-PD-1 immunotherapy. Journal of Clinical Investigation 130, 25702586.CrossRefGoogle ScholarPubMed
Bar, N et al. (2020) Differential effects of PD-L1 versus PD-1 blockade on myeloid inflammation in human cancer. JCI Insight 5, e129353.CrossRefGoogle ScholarPubMed
Sabatier, R et al. (2015) Prognostic and predictive value of PDL1 expression in breast cancer. Oncotarget 6, 54495464.CrossRefGoogle ScholarPubMed
Cimino-Mathews, A et al. (2016) PD-L1 (B7-H1) expression and the immune tumor microenvironment in primary and metastatic breast carcinomas. Human Pathology 47, 5263.CrossRefGoogle ScholarPubMed
Kim, HM, Lee, J and Koo, JS (2017) Clinicopathological and prognostic significance of programmed death ligand-1 expression in breast cancer: a meta-analysis. BMC Cancer 17, 690.CrossRefGoogle ScholarPubMed
Tsang, JYS et al. (2017) PD-L1 expression and tumor infiltrating PD-1+ lymphocytes associated with outcome in HER2+ breast cancer patients. Breast Cancer Research and Treatment 162, 1930.CrossRefGoogle ScholarPubMed
Muenst, S et al. (2013) The presence of programmed death 1 (PD-1)-positive tumor-infiltrating lymphocytes is associated with poor prognosis in human breast cancer. Breast Cancer Research and Treatment 139, 667676.CrossRefGoogle ScholarPubMed
Zhou, T et al. (2018) Expression of programmed death ligand-1 and programmed death-1 in samples of invasive ductal carcinoma of the breast and its correlation with prognosis. Anti-Cancer Drugs 29, 904910.CrossRefGoogle ScholarPubMed
Mao, H et al. (2010) New insights of CTLA-4 into its biological function in breast cancer. Current Cancer Drug Targets 10, 728736.CrossRefGoogle ScholarPubMed
Gu-Trantien, C et al. (2017) CXCL13-producing TFH cells link immune suppression and adaptive memory in human breast cancer. JCI Insight 2, e91487.CrossRefGoogle ScholarPubMed
Najjar, YG et al. (2017) Myeloid-derived suppressor cell subset accumulation in renal cell carcinoma parenchyma is associated with intratumoral expression of IL1b, IL8, CXCL5, and Mip-1α. Clinical Cancer Research 23, 23462355.CrossRefGoogle Scholar
Theivanthiran, B et al. (2022) Tumor-intrinsic {NLRP3-HSP70-TLR4} axis drives premetastatic niche development and hyperprogression during {anti-PD-1} immunotherapy. Science Translational Medicine 14, eabq7019.CrossRefGoogle ScholarPubMed
Hou, J et al. (2020) Author correction: PD-L1-mediated gasdermin C expression switches apoptosis to pyroptosis in cancer cells and facilitates tumour necrosis. Nature Cell Biology 22, 12641275.CrossRefGoogle ScholarPubMed
Park, IH et al. (2017) Tumor-derived IL-18 induces PD-1 expression on immunosuppressive NK cells in triple-negative breast cancer. Oncotarget 8, 3272232730.CrossRefGoogle ScholarPubMed
Zhao, Y et al. (2018) Regulatory B cells induced by pancreatic cancer cell-derived interleukin-18 promote immune tolerance via the PD-1/PD-L1 pathway. Oncotarget 9, 1480314814.CrossRefGoogle ScholarPubMed
Khandekar, D et al. (2022) Low-salt diet reduces {anti-CTLA4} mediated systemic immune-related adverse events while retaining therapeutic efficacy against breast cancer. O Biologico 11, 810.Google ScholarPubMed
Lim, SO et al. (2016) Deubiquitination and stabilization of PD-L1 by CSN5. Cancer Cell 30, 925939.CrossRefGoogle ScholarPubMed
Bertrand, F et al. (2017) TNFα blockade overcomes resistance to anti-PD-1 in experimental melanoma. Nature Communications 8, 2256.CrossRefGoogle ScholarPubMed
Li, C et al. (2018) PINK1 and PARK2 suppress pancreatic tumorigenesis through control of mitochondrial iron-mediated immunometabolism. Developmental Cell 46, 441455.CrossRefGoogle ScholarPubMed
Li, S et al. (2020) Cisplatin promotes the expression level of PD-L1 in the microenvironment of hepatocellular carcinoma through YAP1. Molecular and Cellular Biochemistry 475, 7991.CrossRefGoogle ScholarPubMed
Juric, V et al. (2018) MMP-9 inhibition promotes anti-tumor immunity through disruption of biochemical and physical barriers to T-cell trafficking to tumors. PLoS ONE 13, e0207255.CrossRefGoogle ScholarPubMed
Frigola, X et al. (2011) Identification of a soluble form of B7-H1 that retains immunosuppressive activity and is associated with aggressive renal cell carcinoma. Clinical Cancer Research 17, 19151923.CrossRefGoogle ScholarPubMed
Chen, Y et al. (2011) Development of a sandwich ELISA for evaluating soluble PD-L1 (CD274) in human sera of different ages as well as supernatants of PD-L1+ cell lines. Cytokine 56, 231238.CrossRefGoogle ScholarPubMed
Li, Y et al. (2019) Serum sPD-1 and sPD-L1 as biomarkers for evaluating the efficacy of neoadjuvant chemotherapy in triple-negative breast cancer patients. Clinical Breast Cancer 19, 326332.CrossRefGoogle ScholarPubMed
Han, B et al. (2021) The clinical implication of soluble PD-L1 (sPD-L1) in patients with breast cancer and its biological function in regulating the function of T lymphocyte. Cancer Immunology Immunotherapy 70, 28932909.CrossRefGoogle ScholarPubMed
Berkson, JD et al. (2020) Inflammatory cytokines induce sustained CTLA-4 cell surface expression on human MAIT cells. ImmunoHorizons 4, 1422.CrossRefGoogle ScholarPubMed
Reeves, GK et al. (2007) Cancer incidence and mortality in relation to body mass index in the Million Women Study: cohort study. British Medical Journal 335, 1134.CrossRefGoogle ScholarPubMed
Rose, DP and Vona-Davis, L (2009) Influence of obesity on breast cancer receptor status and prognosis. Expert Review of Anticancer Therapy 9, 10911101.CrossRefGoogle ScholarPubMed
Colditz, GA and Lindsay, L (2018) Obesity and cancer: evidence, impact, and future directions. Clinical Chemistry 64, 154162.CrossRefGoogle ScholarPubMed
Kolb, R, Sutterwala, FS and Zhang, W (2016) Obesity and cancer: inflammation bridges the two. Current Opinion in Pharmacology 29, 7789.CrossRefGoogle ScholarPubMed
Unamuno, X et al. (2018) Adipokine dysregulation and adipose tissue inflammation in human obesity. European Journal of Clinical Investigation 48, e12997.CrossRefGoogle ScholarPubMed
Grossmann, ME et al. (2009) Role of the adiponectin leptin ratio in prostate cancer. Oncology Research 18, 269277.CrossRefGoogle ScholarPubMed
Mechanick, JI, Zhao, S and Garvey, WT (2018) Leptin, an adipokine with central importance in the global obesity problem. Global Heart 13, 113127.CrossRefGoogle ScholarPubMed
Campfield, LA, Smith, FJ and Burn, P (1996) The OB protein (leptin) pathway – a link between adipose tissue mass and central neural networks. Hormone and Metabolic Research 28, 619632.CrossRefGoogle ScholarPubMed
Arita, Y et al. (1999) Paradoxical decrease of an adipose-specific protein, adiponectin, in obesity. Biochemical and Biophysical Research Communications 257, 7983.CrossRefGoogle ScholarPubMed
Xiong, H et al. (2019) Elevated leptin levels in temporomandibular joint osteoarthritis promote proinflammatory cytokine IL-6 expression in synovial fibroblasts. Journal of Oral Pathology & Medicine 48, 251259.CrossRefGoogle ScholarPubMed
Lee, SM et al. (2014) Leptin increases TNF-α expression and production through phospholipase D1 in raw 264.7 cells. PLoS ONE 9, e102373.Google ScholarPubMed
Fang, H and Judd, RL (2018) Adiponectin regulation and function. Comprehensive Physiology 8, 10311063.CrossRefGoogle ScholarPubMed
Jardé, T et al. (2009) Involvement of adiponectin and leptin in breast cancer: clinical and in vitro studies. Endocrine-Related Cancer 16, 1197–210.CrossRefGoogle ScholarPubMed
Katira, A and Tan, PH (2016) Evolving role of adiponectin in cancer-controversies and update. Cancer Biology and Medicine 13, 101119.CrossRefGoogle ScholarPubMed
Dalamaga, M, Diakopoulos, KN and Mantzoros, CS (2012) The role of adiponectin in cancer: a review of current evidence. Endocrine Reviews 33, 547594.CrossRefGoogle Scholar
Beales, ILP et al. (2014) Adiponectin inhibits leptin-induced oncogenic signalling in oesophageal cancer cells by activation of PTP1B. Molecular and Cellular Endocrinology 382, 150158.CrossRefGoogle ScholarPubMed
Pham, DV et al. (2020) Globular adiponectin inhibits breast cancer cell growth through modulation of inflammasome activation: critical role of sestrin2 and AMPK signaling. Cancers 12, 613.CrossRefGoogle ScholarPubMed
Illiano, M et al. (2017) Adiponectin down-regulates CREB and inhibits proliferation of A549 lung cancer cells. Pulmonary Pharmacology & Therapeutics 45, 114120.CrossRefGoogle ScholarPubMed
Ghantous, CM et al. (2015) Differential role of leptin and adiponectin in cardiovascular system. International Journal of Endocrinology 2015, 534320.CrossRefGoogle ScholarPubMed
Okoh, V, Deoraj, A and Roy, D (2011) Estrogen-induced reactive oxygen species-mediated signalings contribute to breast cancer. Biochimica et Biophysica Acta – Reviews on Cancer 1815, 115133.CrossRefGoogle ScholarPubMed
Catalano, S et al. (2004) Leptin induces, via ERK1/ERK2 signal, functional activation of estrogen receptor alpha in MCF-7 cells. Journal of Biological Chemistry 279, 19.CrossRefGoogle ScholarPubMed
Magnani, F and Mattevi, A (2019) Structure and mechanisms of ROS generation by NADPH oxidases. Current Opinion in Structural Biology 59, 9197.CrossRefGoogle ScholarPubMed
Juhasz, A et al. (2009) Expression of NADPH oxidase homologues and accessory genes in human cancer cell lines, tumours and adjacent normal tissues. Free Radical Research 43, 523532.CrossRefGoogle ScholarPubMed
Eyre, R et al. (2019) Microenvironmental IL1β promotes breast cancer metastatic colonisation in the bone via activation of Wnt signalling. Nature Communications 10, 5016.CrossRefGoogle ScholarPubMed
Liu, T et al. (2017) NF-κB signaling in inflammation. Signal Transduction and Targeted Therapy 2, e17023.CrossRefGoogle ScholarPubMed
Catalano, S et al. (2015) A novel leptin antagonist peptide inhibits breast cancer growth in vitro and in vivo. Journal of Cellular and Molecular Medicine 19, 11221132.CrossRefGoogle ScholarPubMed
Fang, X and Sweeney, G (2006) Mechanisms regulating energy metabolism by adiponectin in obesity and diabetes. Biochemical Society Transactions 34, 798801.CrossRefGoogle ScholarPubMed
Divella, R et al. (2016) Obesity and cancer: the role of adipose tissue and adipo-cytokines-induced chronic inflammation. Journal of Cancer 7, 23462359.CrossRefGoogle ScholarPubMed
Rajala, MW and Scherer, PE (2003) Minireview: the adipocyte – at the crossroads of energy homeostasis, inflammation, and atherosclerosis. Endocrinology 144, 37653773.CrossRefGoogle ScholarPubMed
Shrestha, A et al. (2016) Critical role of AMPK/FoxO3A axis in globular adiponectin-induced cell cycle arrest and apoptosis in cancer cells. Journal of Cellular Physiology 231, 357369.CrossRefGoogle ScholarPubMed
Cui, E et al. (2018) Adiponectin inhibits migration and invasion by reversing epithelial-mesenchymal transition in non-small cell lung carcinoma. Oncology Reports 40, 13301338.Google ScholarPubMed
Nigro, E et al. (2018) Adiponectin and colon cancer: evidence for inhibitory effects on viability and migration of human colorectal cell lines. Molecular and Cellular Biochemistry 448, 125135.CrossRefGoogle ScholarPubMed
Waki, H et al. (2005) Generation of globular fragment of adiponectin by leukocyte elastase secreted by monocytic cell line THP-1. Endocrinology 146, 790796.CrossRefGoogle ScholarPubMed
Kim, MJ et al. (2017) Globular adiponectin inhibits lipopolysaccharide-primed inflammasomes activation in macrophages via autophagy induction: the critical role of AMPK signaling. International Journal of Molecular Sciences 18, 1275.CrossRefGoogle ScholarPubMed
Wang, F et al. (2018) Adiponectin inhibits NLRP3 inflammasome by modulating the AMPK-ROS pathway. International Journal of Clinical and Experimental Pathology 11, 33383347.Google ScholarPubMed
Raut, PK and Park, PH (2020) Globular adiponectin antagonizes leptin-induced growth of cancer cells by modulating inflammasomes activation: critical role of HO-1 signaling. Biochemical Pharmacology 180, 114186.CrossRefGoogle ScholarPubMed
Villalpando-Rodriguez, GE et al. (2019) Lysosomal destabilizing drug siramesine and the dual tyrosine kinase inhibitor lapatinib induce a synergistic ferroptosis through reduced heme oxygenase-1 (HO-1) levels. Oxidative Medicine and Cellular Longevity 2019, 9561281.CrossRefGoogle ScholarPubMed
Yamauchi, T et al. (2003) Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423, 762769.CrossRefGoogle ScholarPubMed
Verfaillie, T et al. (2012) PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress. Cell Death & Differentiation 19, 18801891.CrossRefGoogle ScholarPubMed
Li, Y et al. (2014) New insights into the roles of CHOP-induced apoptosis in ER stress structure and properties of C/EBP homologous protein roles of CHOP in ER stress-mediated apoptosis. Acta Biochimica et Biophysica Sinica 46, 629640.CrossRefGoogle Scholar
Rozpedek, W et al. (2016) The role of the PERK/eIF2α/ATF4/CHOP signaling pathway in tumor progression during endoplasmic reticulum stress. Current Molecular Medicine 16, 533544.CrossRefGoogle ScholarPubMed
Pasha, M et al. (2017) Sestrin2 as a novel biomarker and therapeutic target for various diseases. Oxidative Medicine and Cellular Longevity 2017, 3296294.CrossRefGoogle ScholarPubMed
Zulato, E et al. (2018) LKB1 loss is associated with glutathione deficiency under oxidative stress and sensitivity of cancer cells to cytotoxic drugs and γ-irradiation. Biochemical Pharmacology 156, 479490.CrossRefGoogle ScholarPubMed
Ren, Y and Shen, HM (2019) Critical role of AMPK in redox regulation under glucose starvation. Redox Biology 25, 101154.CrossRefGoogle ScholarPubMed
Zimmermann, K et al. (2015) Activated AMPK boosts the Nrf2/HO-1 signaling axis – a role for the unfolded protein response. Free Radical Biology & Medicine 88, 417426.CrossRefGoogle Scholar
Sapio, L et al. (2020) AdipoRon affects cell cycle progression and inhibits proliferation in human osteosarcoma cells. Journal of Oncology 2020, 7262479.CrossRefGoogle ScholarPubMed
Ramzan, AA et al. (2019) Adiponectin receptor agonist AdipoRon induces apoptotic cell death and suppresses proliferation in human ovarian cancer cells. Molecular and Cellular Biochemistry 461, 3746.CrossRefGoogle ScholarPubMed
Wang, SJ et al. (2020) Adiponectin receptor agonist AdipoRon inhibits the proliferation of myeloma cells via the AMPK/autophagy pathway. Zhongguo shi yan xue ye xue za zhi 28, 171176.Google ScholarPubMed
Xu, J et al. (2020) Roles of miRNA and IncRNA in triple-negative breast cancer. Journal of Zhejiang University: Science B 21, 673689.CrossRefGoogle Scholar
Panoutsopoulou, K, Avgeris, M and Scorilas, A (2018) miRNA and long non-coding RNA: molecular function and clinical value in breast and ovarian cancers. Expert Review of Molecular Diagnostics 18, 963979.CrossRefGoogle ScholarPubMed
Klinge, CM (2018) Non-coding RNAs in breast cancer: intracellular and intercellular communication. Non-Coding RNA 4, 40.CrossRefGoogle ScholarPubMed
O'Brien, J et al. (2018) Overview of microRNA biogenesis, mechanisms of actions, and circulation. Frontiers in Endocrinology 9, 402.CrossRefGoogle ScholarPubMed
Venkatesh, J et al. (2021) LncRNA-miRNA axes in breast cancer: novel points of interaction for strategic attack. Cancer Letters 509, 8188.CrossRefGoogle ScholarPubMed
Li, XY et al. (2014) MiRNA-107 inhibits proliferation and migration by targeting CDK8 in breast cancer. International Journal of Clinical and Experimental Medicine 7, 3240.Google ScholarPubMed
Zhou, W et al. (2018) MicroRNA-223 suppresses the canonical NF-κB pathway in basal keratinocytes to dampen neutrophilic inflammation. Cell Reports 22, 18101823.CrossRefGoogle ScholarPubMed
Wu, Y and Zhou, BP (2010) Snail: more than EMT. Cell Adhesion and Migration 4, 199203.CrossRefGoogle ScholarPubMed
Cheng, H-Y et al. (2022) Snail-regulated exosomal {microRNA-21} suppresses {NLRP3} inflammasome activity to enhance cisplatin resistance. Journal for Immunotherapy of Cancer 10, e004832.CrossRefGoogle ScholarPubMed
Lv, W et al. (2021) Identification of pyroptosis-related lncRNAs for constructing a prognostic model and their correlation with immune infiltration in breast cancer. Journal of Cellular and Molecular Medicine 25, 1040310417.CrossRefGoogle ScholarPubMed
Liang, Y et al. (2020) LncRNA BCRT1 promotes breast cancer progression by targeting miR-1303/PTBP3 axis. Molecular Cancer 19, 85.CrossRefGoogle ScholarPubMed
Terme, M et al. (2011) IL-18 induces PD-1-dependent immunosuppression in cancer. Cancer Research [Internet] 71, 53935399. Available at http://cancerres.aacrjournals.org/cgi/doi/10.1158/0008-5472.CAN-11-0993.CrossRefGoogle ScholarPubMed
Yin, Y et al. (2018) MiR-144 suppresses proliferation, invasion, and migration of breast cancer cells through inhibiting CEP55. Cancer Biology & Therapy 19, 306315.CrossRefGoogle ScholarPubMed
Pan, Y et al. (2016) miR-144 functions as a tumor suppressor in breast cancer through inhibiting ZEB1/2-mediated epithelial mesenchymal transition process. OncoTargets and Therapy 9, 62476255.CrossRefGoogle ScholarPubMed
Yu, L et al. (2015) MicroRNA-144 affects radiotherapy sensitivity by promoting proliferation, migration and invasion of breast cancer cells. Oncology Reports 34, 18451852.CrossRefGoogle ScholarPubMed
Ren, N et al. (2020) LncRNA ADAMTS9-AS2 inhibits gastric cancer (GC) development and sensitizes chemoresistant GC cells to cisplatin by regulating miR-223-3p/NLRP3 axis. Aging 12, 1102511041.CrossRefGoogle ScholarPubMed
Samir, A, Salama, E and El-Tayebi, HM (2018) The long non-coding RNA XIST: a new cornerstone in carcinogenesis. Journal of Molecular and Genetic Medicine 12, 1000356.Google Scholar
Salama, EA, Adbeltawab, RE and El Tayebi, HM (2020) XIST and TSIX: novel cancer immune biomarkers in PD-L1-overexpressing breast cancer patients. Frontiers in Oncology 9, 1459.CrossRefGoogle ScholarPubMed
Liu, J et al. (2019) Downregulation of LncRNA-XIST inhibited development of non-small cell lung cancer by activating miR-335/SOD2/ROS signal pathway mediated pyroptotic cell death. Aging 11, 78307846.CrossRefGoogle ScholarPubMed
Li, J et al. (2018) LncRNA GAS5 suppresses ovarian cancer by inducing inflammasome formation. Bioscience Reports 38, BSR20171150.CrossRefGoogle ScholarPubMed
Zhang, P et al. (2019) The lncRNA Neat1 promotes activation of inflammasomes in macrophages. Nature Communications 10, 1495.CrossRefGoogle ScholarPubMed
Zhang, M et al. (2019) Knockdown of NEAT1 induces tolerogenic phenotype in dendritic cells by inhibiting activation of NLRP3 inflammasome. Theranostics 9, 34253442.CrossRefGoogle ScholarPubMed
Yi, H et al. (2017) LincRNA-Gm4419 knockdown ameliorates NF-κB/NLRP3 inflammasome-mediated inflammation in diabetic nephropathy. Cell Death & Disease 8, e2583.CrossRefGoogle ScholarPubMed
Wen, Y, Yu, Y and Fu, X (2017) LncRNA Gm4419 contributes to OGD/R injury of cerebral microglial cells via IκB phosphorylation and NF-κB activation. Biochemical and Biophysical Research Communications 487, 923929.CrossRefGoogle ScholarPubMed