RESEARCH PAPER
Serum and saliva levels of matrix metalloproteinase 3 and 9 in pharynx and larynx cancer
 
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1
Departament of Virology, Medical University of Lublin, Poland
2
Departament of Virology, Medical University of Lublin
CORRESPONDING AUTHOR
Paweł Macieląg   

Departament of Virology, Medical University of Lublin, Chodźki 1, 20-001 Lublin, Poland
 
J Pre Clin Clin Res. 2017;11(2):106–110
KEYWORDS
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ABSTRACT
Introduction and objective:
Matrix metalloproteinases (MMPs) are proteolytic enzymes responsible for the decomposition of extracellular matrix elements. They play an important role during embryogenesis, wound healing, endometrial epithelial exfoliation, the formation of new blood vessels, and also during cancer development. Throat and larynx tumours are included in a large group of head and neck cancers. These tumours are characterized by a poor prognosis. Despite advances in medical science, cancer treatment is difficult and often ineffective. The aim of the study was to evaluate the level of MMP-3 and MMP-9 in the serum and saliva of patients with pharynx and larynx tumours.

Material and methods:
Samples of saliva and serum were collected from 60 patients with larynx or throat cancer. Twenty patients without cancer comprised the control group. MMPs in saliva and serum were determined by the ELISA method.

Results:
In the study group, concentrations of MMP-3 in saliva were from 0.2 – 77.6 ng/ml. Patients with malignant tumours had higher saliva MMP-3 levels than healthy subjects. The concentration of MMP-3 in the serum of the study group ranged from 10.9 – 200.00 ng/ml, which was also higher than in the control group. There were no statistically significant difference in the MMP-9 level between the study and control groups (both in serum and saliva).

Conclusions:
This study is another element that shows the phenomena taking place at the cellular level during oncological disease. In serum and saliva samples, higher values of MMP3 were found in patients with cancer. The increase in the concentration of this enzyme in the risk group may be used for early detection of tumour transformation and evaluation of treatment.

 
REFERENCES (22)
1.
Kołaczkowska E. Metaloproteinaza 9 (MMP-9) jako szczególny przedstawiciel metaloproteinaz macierzy zewnątrzkomórkowej: rola w napływie i apoptozie neutrofili w trakcie reakcji zapalnej. Postępy Biol. Kom., 2010; 2: 471–499.
 
2.
Lipka D, Boratyński J. Metaloproteinazy MMP. Struktura i funkcja. Postępy Hig. Med. Dośw. 2008; 62: 328–336.
 
3.
Fink K, Boratyński J. Rola metaloproteinaz w modyfikacji macierzy zewnątrzkomórkowej w nowotworowym wzroście inwazyjnym, w przerzutowaniu i w angiogenezie. Postepy Hig Med Dosw. 2012; 66: 609–628.
 
4.
Deryugina EI, Quigley JP. Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 2006 Mar; 25(1): 9–34.
 
5.
Kawecki A, Nawrocki S i wsp. Nowotwory nabłonkowe narządów głowy i szyi. W: Zalecenia postępowania diagnostyczno-terapeutycznego w nowotworach złośliwych – 2013. Onkol. Prakt. Klin. Via Medica, Gdańsk, 2013: 2–32.
 
6.
Wojciechowska U, Didkowska J. Zachorowania i zgony na nowotwory złośliwe w Polsce. Krajowy Rejestr Nowotworów, Centrum Onkologii – Instytut im. Marii Skłodowskiej – Curie. Dostępne na stronie http://onkologia.org.pl/raport... dostęp z dnia 20.04.2017.
 
7.
Rzewnicki I, Biszewska J. Epidemiologia raka krtani i gardła dolnego w latach 1988–2012 w materiale Kliniki Otolaryngologii Uniwersytetu Medycznego w Białymstoku. Otolaryngologia Polska, 2013; 67(6): 265–273.
 
8.
Chun-Ying Wu, Ming-Shiang Wu, En-Pei Chiang, et al. Plasma Matrix Metalloproteinase-9 Level Is Better than Serum Matrix Metalloproteinase-9 Level to Predict Gastric Cancer Evolution. Clin Cancer Res. 2007 Apr; 13(7): 20542060.
 
9.
Wilson S, Wakelam MJ, Hobbs RF, et al. Evaluation of the accuracy of serum MMP-9 as a test for colorectal cancer in a primary care population. BMC Cancer. 2006; 6: 258. doi:10.1186/1471–2407–6–258.
 
10.
Merdad A, Karim S, Schulten HJ, Dallol A, Buhmeida, et al. Expression of matrix metalloproteinases (MMPs) in primary human breast cancer: MMP-9 as a potential biomarker for cancer invasion and metastasis. Anticancer Res. 2014 Mar; 34(3): 1355–66.
 
11.
Jinga D C, Blidaru A, Condrea I i wsp. MMP-9 and MMP-2 gelatinases and TIMP1 and Timp-2 inhibitors in breast cancer: correlations with prognostic factors. J Cell Mol Med. 2006; 10: 499–510.
 
12.
Yokoyama K, Kamata N, Fujimoto R, Tsutsumi S. Increased invasion and matrix metalloproteinase-2 expression by Snail-induced mesenchymal transition in squamous cell carcinomas. Int J Oncol. 2003 Apr; 22(4): 891–8.
 
13.
Schütz A, Schneidenbach D, Aust G, Tannapfel A, Steinert M, Wittekind C. Differential expression and activity status of MMP-1, MMP-2 and MMP-9 in tumor and stromal cells of squamous cell carcinomas of the lung. Tumour Biol. 2002 MayJun; 23(3): 179–84.
 
14.
Popat R, Bhavsar NV, Popat PR. Gingival crevicular fluid levels of Matrix Metalloproteinase-1 (MMP-1) and Tissue Inhibitor of Metalloproteinase-1 (TIMP1) in periodontal health and disease. Singapore Dent J. 2014 Dec; 35:59–64.
 
15.
Gonçalves PF, Huang H, McAninley S, Alfant B, Harrison P, et al. Periodontal treatment reduces matrix metalloproteinase levels in localized aggressive periodontitis. J Periodontol. 2013 Dec; 84(12): 1801–8.
 
16.
Luukkaa H, Klemi P, Hirsimäki P, Vahlberg T. Matrix metalloproteinase (MMP)7 in salivary gland cancer. Acta Oncol. 2010; 49(1): 85–90.
 
17.
Shpitzer T, Hamzany Y, Bahar G, Feinmesser R, et al. Salivary analysis of oral cancer biomarkers. Br J Cancer. 2009 Oct 6; 101(7): 1194–1198.
 
18.
Ghallab NA, Shaker OG. Serum and salivary levels of chemerin and MMP-9 in oral squamous cell carcinoma and oral premalignant lesions. Clin Oral Investig. 2016 May 10. [Epub ahead of print].
 
19.
Kim H, Liu X, Kohyama T, Kobayashi T, et al. Cigarette smoke stimulates MMP1 production by human lung fibroblasts through the ERK1/2 pathway.COPD. 2004 Apr; 1(1): 13–23.
 
20.
Ozçaka O, Biçakci N, Pussinen P, Sorsa T, et al. Smoking and matrix metalloproteinases, neutrophil elastase and myeloperoxidase in chronic periodontitis. Oral Dis. 2011 Jan; 17(1): 68–76. doi: 10.1111/j.16010825.2010.01705.x.
 
21.
Rukkumani R, Priyanka A, Sankar P, Menon VP. Ferulic acid influences hepatic expression pattern of matrix metalloproteinases during alcohol and PUFA induced toxicity. Eur Rev Med Pharmacol Sci. 2012 Dec; 16(15):2147–53.
 
22.
Banerjee P, Jana S, Chakraborty S, Swarnakar S. Inflammation and MMPs in alcohol-induced liver diseases and protective action of antioxidants. Indian J. Biochem Biophys. 2013 Oct; 50(5): 377–86.
 
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