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Table of Contents    
TOPIC OF THE ISSUE-EDITORIAL
Year : 2011  |  Volume : 59  |  Issue : 2  |  Page : 224-225

Matrix metalloproteinases


Department of Neurological Sciences and Pathology, Section of Neuropathology, Christian Medical College, Vellore, India

Date of Submission06-Feb-2011
Date of Decision07-Feb-2011
Date of Acceptance07-Feb-2011
Date of Web Publication7-Apr-2011

Correspondence Address:
Geeta Chacko
Department of Neurological Sciences and Pathology, Christian Medical College, Vellore - 632 004
India
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/0028-3886.79123

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How to cite this article:
Chacko G. Matrix metalloproteinases. Neurol India 2011;59:224-5

How to cite this URL:
Chacko G. Matrix metalloproteinases. Neurol India [serial online] 2011 [cited 2019 Dec 9];59:224-5. Available from: http://www.neurologyindia.com/text.asp?2011/59/2/224/79123


Matrix metalloproteinases (MMPs) are a family of enzymes that regulate the extracellular matrix environment and whose activity has been implicated in normal and pathological processes. [1],[2] There are 23 MMPs identified in humans and these are upregulated in response to injury and during tumorgenesis. It has been reported that MMP-3, 8, and 12 null mice show increased tumor growth and / or metastases, while MMP-2, 7, 9, 11, and 19 null mice show decreased tumor growth and / or metastases. [3]

Given their relevance in human cancers it has become increasingly important to gather data about the expression of individual MMPs at different sites and in different cancers, and to determine if they can be utilized as prognostic biomarkers. This has fuelled the development of techniques to analyze their expression and activity in human disease. Studies of MMP expression at a mRNA level have utilized microarray and automated real time polymerase chain reaction (RT-PCR) techniques. [4] Qualitative analysis has utilized in situ hybridization. [5] Other techniques that have been utilized include immunohistochemistry, sandwich-enzyme immunoassay systems, gelatin zymography, immunoblotting, and in situ zymography. [6],[7],[8]

Recent evidence from a host of studies shows members of the MMP family as potential biomarkers for diagnosis, prognosis, early detection of cancer, tumor recurrence, and metastasis, and an assessment of response to therapy in a variety of cancers, including brain tumors. [9],[10],[11],[12],[13],[14],[15],[16],[17],[18]

The present study by Kumar et al.[19] describes a case control study to determine if there is an association between MMP-2 (-1306 C/T) polymorphisms and susceptibility to develop glioblastoma multiforme in an Indian population. This has been done by PCR-restriction fragment length polymorphism in 110 cases and 150 age- and gender-matched controls. Although -1302 MMP2 gene polymorphisms have been demonstrated in malignancies of the lung, breast, cervix, and gastrointestinal tract, the authors have not found this to be the case in their study population of a high-grade brain tumor. MMP 2 and 9 have been demonstrated in gliomas of various grades in other racial populations. The lack of association in this study can be, as pointed out by the authors, due to the study of a small sample size. Larger population studies are required before firm conclusions can be drawn. However, this article serves well as a pilot report on a geographically and ethnically distinct population.

 
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4.Acuff HB, Sinnamon M, Fingleton B, Boone B, Levy SE, Chen X, et al. Analysis of host- and tumor-derived proteinases using a custom dual species microarray reveals a protective role for stromal matrix metalloproteinase-12 in non-small cell lung cancer. Cancer Res 2006;66:7968-75.  Back to cited text no. 4
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8.Hanemaaijer R, Visser H, Konttinen YT, Koolwijk P, Verheijen JH. A novel and simple immunocapture assay for determination of gelatinase-B (MMP-9) activities in biological fluids: Saliva from patients with Sjogren's syndrome contain increased latent and active gelatinase-B levels. Matrix Biol 1998;17:657-65.  Back to cited text no. 8
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9.Choe G, Park JK, Jouben-Steele L, Kremen TJ, Liau LM, Vinters HV, et al. Active matrix metalloproteinase 9 expression is associated with primary glioblastoma subtype. Clin Cancer Res 2002;8:2894-901.  Back to cited text no. 9
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10.Friedberg MH, Glantz MJ, Klempner MS, Cole BF, Perides G. Specific matrix metalloproteinase profiles in the cerebrospinal fluid correlated with the presence of malignant astrocytomas, brain metastases, and carcinomatous meningitis. Cancer 1998;82:923-30.  Back to cited text no. 10
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11.Hilska M, Roberts PJ, Collan YU, Laine VJ, Kossi J, Hirsimaki P, et al. Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer. Int J Cancer 2007;121:714-23.  Back to cited text no. 11
    
12.Jaalinoja J, Herva R, Korpela M, Hoyhtya M, Turpeenniemi-Hujanen T. Matrix metalloproteinase 2 (MMP-2) immunoreactive protein is associated with poor grade and survival in brain neoplasms. J Neurooncol 2000;46:81-90.  Back to cited text no. 12
    
13.Kamat AA, Fletcher M, Gruman LM, Mueller P, Lopez A, Landen CN, Jr., et al. The clinical relevance of stromal matrix metalloproteinase expression in ovarian cancer. Clin Cancer Res 2006;12:1707-14.  Back to cited text no. 13
    
14.Moses MA, Wiederschain D, Loughlin KR, Zurakowski D, Lamb CC, Freeman MR. Increased incidence of matrix metalloproteinases in urine of cancer patients. Cancer Res 1998;58:1395-9.  Back to cited text no. 14
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15.Sauer CG, Kappeler A, Spath M, Kaden JJ, Michel MS, Mayer D, et al. Expression and activity of matrix metalloproteinases-2 and -9 in serum, core needle biopsies and tissue specimens of prostate cancer patients. Virchows Arch 2004;444:518-26.  Back to cited text no. 15
    
16.Tetu B, Brisson J, Wang CS, Lapointe H, Beaudry G, Blanchette C, et al. The influence of MMP-14, TIMP-2 and MMP-2 expression on breast cancer prognosis. Breast Cancer Res 2006;8:R28.  Back to cited text no. 16
    
17.Wu ZS, Wu Q, Yang JH, Wang HQ, Ding XD, Yang F, et al. Prognostic significance of MMP-9 and TIMP-1 serum and tissue expression in breast cancer. Int J Cancer 2008;122:2050-6.  Back to cited text no. 17
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18.Yokoyama M, Ochi K, Ichimura M, Mizushima T, Shinji T, Koide N, et al. Matrix metalloproteinase-2 in pancreatic juice for diagnosis of pancreatic cancer. Pancreas 2002;24:344-347.  Back to cited text no. 18
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19.Kumar R, Malik N, Tungaria A, Kawal P. Matrix metalloproteinase-2 gene polymorphism is not associated with increased glioblastoma multiforme susceptibility: An Indian institutional experience. Neurol India 2011;59:236-40.  Back to cited text no. 19
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