РОЛЬ СТРЕСОРНИХ ФАКТОРІВ У МОДУЛЯЦІЇ ЕКСПРЕСІЇ ТА ФУНКЦІОНАЛЬНОЇ АКТИВНОСТІ МАТРИКСНИХ МЕТАЛОПРОТЕЇНАЗ
DOI:
https://doi.org/10.15407/oncology.2025.02.111Ключові слова:
стрес, матриксні металопротеїнази, катехоламіни, глюкокортикоїдиАнотація
Матриксні металопротеїнази (matrix metalloproteinases, MMPs) відіграють ключову роль у ремоделюванні позаклітинного матриксу (extracellular matrix, ECM) та регуляції міжклітинних взаємодій. MMPs сприяють прогресії пухлин різного гістогенезу, впливаючи на деградацію ECM, ангіогенез, інвазію та метастазування пухлинних клітин. Сучасні дослідження свідчать, що стресорні фактори можуть модулювати експресію та активність MMPs. Катехоламіни та глюкокортикоїди, що вивільняються внаслідок активації гіпоталамо-гіпофізарно-наднирникової осі та симпатичної нервової системи, здатні стимулювати експресію низки MMPs, водночас підвищуючи рівні тканинних інгібіторів металопротеїназ (tissue inhibitor of metalloproteinases, TIMPs) або, навпаки, опосередковано активувати MMPs. Дисбаланс між активністю MMPs і рівнями TIMPs створює умови для інвазивного росту новоутворень та метастазування. Незважаючи на масив накопичених даних, механізми впливу стресу на регуляцію MMPs залишаються недостатньо з’ясованими та потребують подальших досліджень. Поглиблене вивчення цих процесів має потенціал для розробки нових прогностичних та терапевтичних підходів в онкології.
Посилання
Eckerling A, Ricon-Becker I, Sorski L, et al. Stress and cancer: mechanisms, significance and future directions. Nat Rev Cancer 2021; 21 (12): 7673–85. https://doi.org/10. 1038/s41568-021-00395-5.
Dai S, Mo Y, Wang Y, et al. Chronic stress promotes cancer development. Front Oncol 2020; 10: 1492. https://doi.org/ 10.3389/fonc.2020.01492.
Liu Y, Tian S, Ning B, et al. Stress and cancer: The mecha- nisms of immune dysregulation and management. Front Immunol 2022; 13: 1032294. https://doi.org/10.3389/ fi 1032294.
Lempesis IG, Georgakopoulou VE, Papalexis P, et al. Role of stress in the pathogenesis of cancer. Int J Oncol 2023; 63 (5): 124. https://doi.org/10.3892/ij 3.5572.
Zhou Q, Qian Z, Ding W, et al. Chronic psychological stress attenuates the efficacy of anti-PD-L1 immunotherapy for bladder cancer in immunocompetent mice. Cancer Invest 2021; 39 (6–7): 571–81. https://doi.org/10.1080/07357907. 2021.1943746.
Zhang R, Yao B, Li R, et al. Chronic epinephrine-induced endoplasmic reticulum and oxidative stress impairs pancrea- tic β-cells function and fate. Int J Mol Sci 2024; 25 (13): 7029. https://doi.org/10.3390/ij 137029.
Zhang W, Shi Y, Oyang L, et al. Endoplasmic reticulum stress—a key guardian in cancer. Cell Death Discov 2024; 10 (1): 343. https://doi.org/10.1038/s41420-024-02110-3.
Zheng Y, Wang N, Wang S, et al. Chronic psychological stress promotes breast cancer pre-metastatic niche for-
mation by mobilizing splenic MDSCs via TAM/CXCL1 signaling. J Exp Clin Cancer Res 2023; 42 (1): 129. https:// doi.org/10.1186/s13046-023-02696-z.
He XY, Gao Y, Ng, D, et al. Chronic stress increases metastasis via neutrophil-mediated changes to the micro- environment. Cancer cell 2024; 42 (3): 474–86. https:// doi.org/10.1016/j.ccell.2024.01.013.
Brown GT, Murray GI. Current mechanistic insights into the roles of matrix metalloproteinases in tumour invasion and metastasis. J Pathol 2015; 237 (3): 273–81. https://doi. org/10.1002/path.4586.
Szczygielski O, Dąbrowska E, Niemyjska, et al. Targeting matrix metalloproteinases and their inhibitors in melanoma. Int J Mol Sci 2024; 25 (24): 13558. https://doi.org/10.3390/ ij 13558.
Quintero-Fabián S, Arreola R, Becerril-Villanueva E, et al. Role of matrix metalloproteinases in angiogenesis and can- cer. Front Oncol 2019; 9: 1370. https://doi.org/10.3389/ fonc.2019.01370.
Laronha H, Caldeira J. Structure and Function of Human Matrix Metalloproteinases. Cells 2020; 9 (5): 1076. https:// doi.org/10.3390/cells9051076.
Cui N, Hu M, Khalil RA. Chapter one-biochemical and biological attributes of matrix metalloproteinases. Prog Mol Biol and Transl Sci 2017; 147: 1–73. https://doi.org/ 10.1016/bs.pmbts.2017.02.005.
Niland S, Riscanevo AX, Eble JA. Matrix metalloproteinases shape the tumor microenvironment in cancer progression. Int J Mol Sci 2022; 23 (1): 146. https://doi.org/10.3390/ ij 3010146.
Roy D, Walsh L. Candidate prognostic markers in breast cancer: focus on extracellular proteases and their inhibitors. Breast Cancer (Dove Med Press). 2014; 6: 81–91. https:// doi.org/10.2147/BCTT.S46020.
Liu J, Khalil RA. Matrix metalloproteinase inhibitors as investigational and therapeutic tools in unrestrained tissue remodeling and pathological disorders. Prog Mol Biol and Transl Sci 2017; 148: 355–420. https://doi.org/10.1016/ bs.pmbts.2017.04.003.
Gobin E, Bagwell K, Wagner J, et al. A pan-cancer perspec- tive of matrix metalloproteases (MMP) gene expression profile and their diagnostic/prognostic potential. BMC Cancer 2019; 19 (1): 581. https://doi.org/10.1186/s12885- 019-5768-0.
Benson CS, Babu SD, Radhakrishna S, et al. Expression of matrix metalloproteinases in human breast cancer tis- sues. Dis Markers 2013; 34 (6): 395–405. https://doi.org/ 10.3233/DMA-130986.
Davies KJ. The complex interaction of matrix metalloprotei- nases in the migration of cancer cells through breast tissue stroma. Int J Breast Cancer 2014; 2014: 839094. https:// doi.org/10.1155/2014/839094.
Radisky ES, Radisky DC. Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer. J Mam- mary Gland Biol Neoplasia 2010; 15 (2): 201–12. https:// doi.org/10.1007/s10911-010-9177-x.
Conlon G A, Murray GI. Recent advances in understanding the roles of matrix metalloproteinases in tumour invasion and metastasis. J Pathol 2019; 247 (5): 629–40. https:// doi.org/10.1002/path.5225.
Winer A, Adams S, Mignatti P. Matrix metalloproteinase inhibitors in cancer therapy: turning past failures into future successes. Mol Cancer Ther 2018; 17 (6): 1147–55. https:// doi.org/10.1158/1535-7163.MCT-17-0646.
Lukianova N, Mushii O, Borikun T, et al. Pattern of MMP2 and MMP9 expression depends on breast cancer patients’ age. Exp Oncol 2023; 45 (1): 17–27. https://doi.org/10. 15407/exp-oncology.2023.01.017.
Lukianova N, Mushii O, Zadvornyi T, et al. Features of col- lagenase gene expression in breast cancer tissue:an open databases analysis. Oncology 2024; 26 (1): 22–8. https:// doi.org/10.15407/oncology.2024.01.022.
Kwon MJ. Matrix metalloproteinases as therapeutic targets in breast cancer. Front Oncol 2023; 12: 1108695. https:// doi.org/10.3389/fonc.2022.1108695.
Mustafa S, Koran S, AlOmair L. Insights into the role of matrix metalloproteinases in cancer and its various thera- peutic aspects: a review. Front Mol Biosci 2022; 9: 896099. https://doi.org/10.3389/fmolb.2022.896099.
Sood AK, Bhatty R, Kamat AA, et al. Stress hormone-me- diated invasion of ovarian cancer cells. Clin Cancer Res 2006; 12 (2): 369–75. https://doi.org/10.1158/1078-0432. CCR-05-1698.
Yang EV, Sood AK, Chen M, et al. Norepinephrine up- regulates the expression of vascular. Endothelial growth factor, matrix metalloproteinase (MMP)-2, and MMP-9 in nasopharyngeal carcinoma tumor cells. Cancer Res 2006; 66 (21): 10357–364. https://doi.org/10.1158/0008-5472. CAN-06-2496.
Cury PR, Araújo VC, Canavez FC, et al. Hydrocortisone af- fects the expression of matrix metalloproteinases (MMP-1,
-2, -3, -7, and -11) and tissue inhibitor of matrix metallo- proteinases (TIMP-1) in human gingival fibroblasts. J Perio- dontol 2007; 78 (7): 1309–315. https://doi.org/10.1902/ jop.2007.060225.
Gilet A, Zou F, Boumenir M, et al. Aldosterone up-regulates MMP-9 and MMP-9/NGAL expression in human neu- trophils through p38, ERK1/2 and PI3K pathways. Exp Cell Res 2015; 331 (1): 152–63. https://doi.org/10.1016/j. yexcr.2014.11.004.
Li Y, Tang L, Duan Y, et al. Upregulation of MMP-13 and TIMP-1 expression in response to mechanical strain in MC3T3-E1 osteoblastic cells. BMC Res Notes 2010; 3: 309. https://doi.org/10.1186/1756-0500-3-309.
Alge-Priglinger CS, Kreutzer T, Obholzer K, et al. Oxidative stress-mediated induction of MMP-1 and MMP-3 in hu- man RPE cells. Invest Ophthalmol Vis Sci 2009; 50 (11): 5495–503.
Yu F, Kamada H, Niizuma K, et al. Induction of MMP-9 expression and endothelial injury by oxidative stress after spinal cord injury. J Neurotrauma 2008; 25 (3), 184–95. https://doi.org/10.1089/neu.2007.0438.
Das J, Agarwal T, Chakraborty S, Maiti TK. Compressive stress-induced autophagy promotes invasion of HeLa cells by facilitating protein turnover in vitro. Exp Cell Res 2019; 381 (2): 201–7. https://doi.org/10.1016/j.yexcr.2019.04.037.
Haage A, Nam DH, Ge X, Schneider IC. Matrix metallo- proteinase-14 is a mechanically regulated activator of se- creted MMPs and invasion. Biochem Biophys Res Com- mun 2014; 450 (1): 213–8. https://doi.org/10.1016/j.bbrc. 2014.05.086.
Wang P, Yang L, You X, et al. Mechanical stretch regulates the expression of matrix metalloproteinase in rheumatoid arthritis fibroblast-like synoviocytes. Connective Tis- sue Res 2009; 50 (2): 98–109. https://doi.org/10.1080/ 03008200802348625.
Cathomas F, Lin HY, Chan KL, et al. Circulating myeloid- derived MMP8 in stress susceptibility and depression. Na- ture 2024; 626 (8001): 1108–115. https://doi.org/10.1038/ s41586-023-07015-2.
Yang EV, Bane CM, MacCallum RC, et al. Stress-related modulation of matrix metalloproteinase expression. J Neuroimmunol 2002; 133 (1–2): 144–50. https://doi.org/10. 1016/S0165-5728(02)00270-9.
Lundberg AK, Jönsson S, Stenmark J, et al. Stress-induced release of matrix metalloproteinase-9 in patients with co- ronary artery disease: The possible influence of cortisol. Psychoneuroendocrinol 2016; 73: 117–24. https://doi.org/ 10.1016/j.psyneuen.2016.07.219.
Gajendrareddy PK, Engeland CG, Junges R, et al. MMP-8 overexpression and persistence of neutrophils relate to stress-impaired healing and poor collagen architecture in mice. Brain Behav Immun 2013; 28: 44–8. https://doi. org/10.1016/j.bbi.2012.10.016.
Cheng Y, Gao XH, Li XJ, et al. Depression promotes prostate cancer invasion and metastasis via a sympathetic-cAMP- FAK signaling pathway. Oncogene 2018; 37 (22): 2953–966. https://doi.org/10.1038/s41388-018-0177-4.
Wu X, Liu BJ, Ji S, et al. Social defeat stress promotes tumor growth and angiogenesis by upregulating vascular endothe- lial growth factor/extracellular signal-regulated kinase/ matrix metalloproteinase signaling in a mouse model of lung carcinoma. Mol Med Rep 2015; 12 (1): 1405–12. https:// doi.org/10.3892/mmr.2015.3559.
Thaker P, Han L, Kamat A, et al. Chronic stress promotes tumor growth and angiogenesis in a mouse model of ova- rian carcinoma. Nat Med 2006; 12 (8): 939–44. https:// doi.org/10.1038/nm1447.
Zhou P, Yang C, Zhang S, et al. The imbalance of MMP-2/ TIMP-2 and MMP-9/TIMP-1 contributes to collagen de- position disorder in diabetic non-injured skin. Front En- docrinol 2021; 12: 734485. https://doi.org/10.3389/fendo. 2021.734485.
Hartmann C, El-Gindi J, Lohmann C, et al. TIMP-3: a novel target for glucocorticoid signaling at the blood–brain barrier. Biochem Biophys Res Commun 2009; 2: 182–6. https://doi.org/10.1016/j.bbrc.2009.08.158.
Shiomi T, Inoki I, Kataoka F, et al. Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151. Lab Invest 2005; 85 (12): 1489–506. https://doi. org/10.1038/labinvest.3700351.
Förster C, Kahles T, Kietz S, Drenckhahn D. Dexametha- sone induces the expression of metalloproteinase inhibitor TIMP-1 in the murine cerebral vascular endothelial cell line cEND. The J Physiol 2007; 580 (3): 937–49. https:// doi.org/10.1113/jphysiol.2007.129007.
Andersson T, af Klint E, Strobel S, et al. Differential gene expression and protein expression levels of MMP and TIMP molecules in response to glucocorticoid treatment in arthritic patients. Arthritis Res Ther 2004; 6 (Suppl 1): 53. https://doi.org/10.1186/ar1095.
Bian F, Pelegrino FS, Henriksson JT, et al. Diff rential ef- fects of dexamethasone and doxycycline on infl tion and MMP production in murine alkali-burned corneas associated with dry eye. Ocul Surf 2016; 14 (2): 242–54. https://doi.org/10.1016/j.jtos.2015.11.006.
Gonzalez-Avila G, Sommer B, Garcia-Hernandez AA, et al. Matrix metalloproteinases and stress hormones in lung cancer progression. J Oncol 2022; 2022: 5349691. https:// doi.org/10.1155/2022/5349691.
Kameda K, Matsunaga T, Abe N, et al. Correlation of oxi- dative stress with activity of matrix metalloproteinase in patients with coronary artery disease: Possible role for left ventricular remodelling. Eur Heart J 2003; 24 (24): 2180–5. https://doi.org/10.1016/j.ehj.2003.09.022.
