Z
inc
and
metalloproteinases
2
and
9: W
hat
is
their
relation
with
breast
cancer
?
R
ev
A
ssoc
M
ed
B
ras
2017; 63(1):78-84
83
matriz, as quais parecem estar envolvidas na propagação
de vários tipos de neoplasias, incluindo o câncer de mama.
Além disso, é provável que o zinco transportado seja utili-
zado para metalação do domínio catalítico das metalopro-
teinases recentemente sintetizadas antes de serem segrega-
das. Nesse sentido, o aumento das concentrações de zinco
em compartimentos celulares e a redução desse oligoele-
mento no sangue de pacientes com câncer de mama pare-
cem alterar a atividade das metaloproteinases 2 e 9, con-
tribuindo para a ocorrência de tumor maligno. Assim,
faz-se necessária a realização de novos estudos na perspec-
tiva de esclarecer o papel do zinco e das metaloproteinases
2 e 9 na patogênese do câncer de mama.
Palavras-chave
: zinco, metaloproteinases da matriz, neo-
plasias da mama.
R
eferences
1.
Silva AG, Ewald IP, Sapienza M, Pinheiro M, Peixoto A, Nóbrega AF, et al.
Li-Fraumeni-like syndrome associated with a large BRCA1 intragenic deletion.
BMC Cancer. 2012; 12:237.
2.
Peto J, Houlston RS. Genetics and the common cancers. Eur. J. Cancer 2001;
37(Suppl.8):S88-96.
3.
Harris HR, Bergkvist L, Wolk A. Vitamin C intake and breast cancer mortality
in a cohort of Swedish women. Br J Cancer. 2013; 109(1):257-64.
4.
Lowe NM, Fekete K, Decsi T. Methods of assessment of zinc status in humans:
a systematic review. Am J Clinical Nutrition. 2009; 89(6):2040S-51S.
5.
Lin CY, Tsai PH, Kandaswami CC, Lee P, Huang CJ, Hwang JJ, et al. Matrix
metalloproteinase-9 cooperates with transcription factor Snail to induce
epithelial-mesenchymal transition. Cancer Sci. 2011; 102(4):815-27.
6.
Shuman Moss LA, Jensen-Taubman S, Stetler-Stevenson WG. Matrix
metalloproteinases: changing roles in tumor progression and metastasis.
Am J Pathol. 2012; 181(6):1895-9.
7.
Lindsey ML, Zamilpa R. Temporal and spatial expression of matrix
metalloproteinases and tissue inhibitors of metalloproteinases following
myocardial infarction. Cardiovasc Ther. 2012; 30(1):31-41.
8.
Delabio-Ferraz E, Aguiar Neto JP, Takiya CM, Lacombe DP. Rana catesbeiana,
pólvora e modulação supramolecular cicatrização intestinal e prognóstico
no câncer de cólon: uma mesma origem biológica para o insucesso? Rev
Bras Colo-proctol. 2010; 30(2):141-51.
9.
Perches CS, Brandão CVS, Ranzani JJT, Rocha NS, Sereno MG, Fonzar JF.
Matriz metaloproteinases na reparação corneal. Revisão de literatura. Vet
Zootec. 2012; 19(4):480-9.
10.
Mani SK, Kern CB, Kimbrough D, Addy B, Kasiganesan H, Rivers H, et al.
Inhibition of class I histone deacetylase activity represses matrix
metalloproteinase-2 and -9 expression and preserves LV function
postmyocardial infarction. Am J Physiol Heart Circ Physiol. 2015;
308(11):H1391-401.
11.
Fu MM, Fu E, Kuo PJ, Tu HP, Chin YT, Chiang CY, et al. Gelatinases and
extracellular matrix metalloproteinase inducer are associated with
cyclosporin-A-induced attenuation of periodontal degradation in rats. J
Periodontol. 2015; 86(1):82-90.
12. Freise C, Querfeld U. The lignan (+)-episesamin interferes with TNF-
α
-induced
activation of VSMC via diminished activation of NF-
κ
B, ERK1/2 and AKT
and decreased activity of gelatinases. Acta Physiol. 2015; 213(3):642-52.
13. Ala-Aho R, Kähäri VM. Collagenases in cancer. Biochimie. 2005; 87(3-
4):273-86.
14.
Hadler-Olsen E, Fadnes B, Sylte I, Uhlin-Hansen L, Winberg JO. Regulation
of matrix metalloproteinase activity in health and disease. FEBS J. 2011;
278(1):28-45.
15. Coussens LM, Werb Z. Matrix metalloproteinases and the development of
cancer. Chem Biol. 1996; 3(11):895-904.
16.
Liotta LA, Thorgeirsson UP, Garbisa S. Role of collagenases in tumor cell
invasion. Cancer Metastasis Rev. 1982; 1(4):277-88.
17.
Noël A, Jost M, Maquoi E. Matrix metalloproteinases at cancer tumor-host
interface. Semin Cell Dev Biol. 2008; 19(1):52-60.
18.
Sternlicht MD, Lochter A, Sympson CJ, Huey B, Rougier JP, Gray JW, et al.
The stromal proteinase MMP3/stromelysin-1 promotes mammary
carcinogenesis. Cell. 1999; 98(2):137-46.
19.
Polette M, Gilbert N, Stas I, Nawrocki B, Noël A, Remacle A, et al. Gelatinase
A expression and localization in human breast cancers. An in situ
hybridization study and immunohistochemical detection using confocal
microscopy. Virchows Arch. 2004; 424(6):641-5.
20.
Egeblad M, Werb Z. New functions for the matrix metalloproteinases in
cancer progression. Nat Rev Cancer. 2002; 2(3):161-74.
21.
van ’t Veer LJ, Dai H, van de Vijver MJ, He YD, Hart AA, Mao M, et al. Gene
expression profiling predicts clinical outcome of breast cancer. Nature. 2002;
415(6871):530-6.
22.
Koshikawa N, Giannelli G, Cirulli V, Miyazaki K, Quaranta V. Role of cell
surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5.
J Cell Biol. 2000; 148(3):615-24.
23. Patel BP, Shah SV, Shukla SN, Shah PM, Patel PS. Clinical significance of MMP-
2 and MMP-9 in patients with oral cancer. Head Neck. 2007; 29(6):564-72.
24.
Jinga DC, Blidaru A, Condrea I, Ardeleanu C, Dragomir C, Szegli G, et
al. MMP-9 and MMP-2 gelatinases and TIMP-1 and TIMP-2 inhibitors
in breast cancer: correlations with prognostic factors. J Cell Mol Med.
2006; 10(2):499-510.
25.
Daniele A, Zito AF, Giannelli G, Divella R, Asselti M, Mazzocca A, et al.
Expression of metalloproteinases MMP-2 and MMP-9 in sentinel lymph
node and serum of patients with metastatic and non-metastatic breast
cancer. Anticancer Res. 2010; 30(9):3521-7.
26.
Somiari SB, Somiari RI, Heckman CM, Olsen CH, Jordan RM, Russell SJ, et
al. Circulating MMP2 and MMP9 in breast cancer – potential role in
classification of patients into low risk, high risk, benign disease and breast
cancer categories. Int J Cancer. 2006; 119(6):1403-11.
27. Vasaturo F, Solai F, Malacrino C, Nardo T, Vincenzi B, Modesti M, et al.
Plasma levels of matrix metalloproteinases 2 and 9 correlate with histological
grade in breast cancer patients. Oncol Lett. 2013; 5(1):316-20.
28. Č
upi
ć
DF, Tešar EC, Ilijaš KM, Nemrava J, Kova
č
evi
ć
M, Musta
ć
E. Expression
of matrix metalloproteinase 9 in primary and recurrent breast carcinomas.
Coll Antropol. 2011; 35(Suppl 2):7-10.
29.
Zucker S, Hymowitz M, Conner C, Zarrabi HM, Hurewitz AN, Matrisian L,
et al. Measurement of matrix metalloproteinases and tissue inhibitors of
metalloproteinases in blood and tissues. Clinical and experimental
applications. Ann N Y Acad Sci. 1999; 878:212-27.
30.
Hwang BM, Chae HS, Jeong YJ, Lee YR, Noh EM, Youn HZ, et al. Protein
tyrosine phosphatase controls breast cancer invasion through the expression
of matrix metalloproteinase-9. BMB Rep. 2013; 46(11):533-8.
31. Gong Y, Chippada-Venkata UD, Oh WK. Roles of matrix metalloproteinases
and their natural inhibitors in prostate cancer progression. Cancers (Basel).
2014; 6(3):1298-327.
32.
Benson CS, Babu SD, Radhakrishna S, Selvamurugan N, Ravi Sankar B.
Expression of matrix metalloproteinases in human breast cancer tissues.
Dis Markers. 2013; 34(6):395-405.
33.
Klein T, Bischoff R. Physiology and pathophysiology of matrix
metalloproteases. Amino Acids. 2011; 41(2):271-90.
34.
Kambe T. An overview of a wide range of functions of ZnT and Zip zinc
transporters in the secretory pathway. Biosci Biotechnol. Biochem. 2011;
75(6):1036-43.
35.
Morcos NY, Zakhary NI, Said MM, Tadros MM. Postoperative simple
biochemical markers for prediction of bone metastases in Egyptian breast
cancer patients. Ecancermedicalscience. 2013; 7:305.
36.
Holanda AON. Relação entre os parâmetros bioquímicos do zinco e as
concentrações das metaloproteinases 2 e 9 em mulheres com câncer de
mama. [Dissertation]. Teresina: Universidade Federal do Piauí; 2014.
37. Taylor KM, Morgan HE, Smart K, Zahari NM, Pumford S, Ellia IO, et al.
The emerging role of the LIV-1 subfamily of zinc transporters in breast
cancer. Mol Med. 2007; 13(7-8):396-406.
38.
Kelleher SL, Seo YA, Lopez V. Mammary gland zinc metabolism: regulation
and dysregulation. Genes Nutr. 2009; 4(2):83-94.
39.
Kelleher SL, McCormick NH, Velasquez V, Lopez V. Zinc in specialized
secretory tissues: roles in the pancreas, prostate, and mammary gland. Adv
Nutr. 2011; 2(2):101-11.