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Journal of Cancer Research and Clinical Oncology

Erschienen in:

01.03.2011 | Original Paper

Comparative study of stromal metalloproteases expression in patients with benign hyperplasia and prostate cancer

verfasst von: Safwan Escaff, Jesús M. Fernández, Luis O. González, Aurelio Suárez, Salomé González-Reyes, José M. González, Francisco J. Vizoso

Erschienen in: Journal of Cancer Research and Clinical Oncology | Ausgabe 3/2011

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Abstract

Purpose

The aim of the present work was to perform a comparative study of stromal cell expressions of MMPs and TIMPs between benign and malignant prostate tissues.

Methods

An immunohistochemical study was performed using specific antibodies against metalloproteases (MMPs) −1, −2, −7, 9, 11, 13, 14 and their tissue inhibitors (TIMPs) −1, 2 and 3, on prostate specimens from 133 patients with clinical localized prostate carcinoma and from 50 patients with BPH.

Results

Our results showed higher percentages of expressions of MMPs and TIMPs by fibroblasts or by mononuclear inflammatory cells (MICs) in prostate carcinomas compared to these cells in BPH. The detection of MMP-2 expression by stromal fibroblasts and/or MMP-2, 9 and TIMP-3 expression by stromal MICs was associated with a 100% of specificity for diagnoses of prostate cancer. We found that the combination of MMP-2 expression by fibroblasts and/or MMP-9 by MICs and/or TIMP-2 by MICs yielded a sensitivity of 47.4%.

Conclusions

Despite of a limited sensitivity (50%), the combination of MMP-TIMPs expression in stromal cells (MMP-2 by fibroblasts and TIMPs by MICs) in our study provided a specificity of 100% for prostate cancer diagnosis.

Bhowmick NA, Moses HL (2005) Tumor-stroma interactions. Curr Opin Genet Dev 15:97–101CrossRefPubMed

Cheng L, Jones TD, Pan CX, Barbarin A, Eble JN, Koch MO (2005) Anatomic distribution and pathologic characterization of small-volume prostate cancer (< 0.5 ml) in whole-mount prostatectomy specimens. Mod Pathol 18:1022–1026CrossRefPubMed

Cornelius LA, Nehring LC, Harding E et al (1998) Matrix metalloproteinases generate angiostatin: effects on neovascularization. J Immunol 161:6845–6852PubMed

Egeblad M, Werb Z (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2:161–174CrossRefPubMed

Epstein JI, Walsh PC, Carmichael M, Brendler CB (1994) Pathologic and clinical findings to predict tumor extent of nonpalpable (stage T1c) prostate cancer. Jama 271:368–374CrossRefPubMed

Fingleton B, Vargo-Gogola T, Crawford HC, Matrisian LM (2001) Matrilysin [MMP-7] expression selects for cells with reduced sensitivity to apoptosis. Neoplasia 3:459–468CrossRefPubMed

Goodson WH III, Ljung BM, Moore DH II et al (1993) Tumor labeling indices of primary breast cancers and their regional lymph node metastases. Cancer 71:3914–3919CrossRefPubMed

Hughes C, Murphy A, Martin C, Sheils O, O’Leary J (2005) Molecular pathology of prostate cancer. J Clin Pathol 58:673–684CrossRefPubMed

Jiang Y, Goldberg ID, Shi YE (2002) Complex roles of tissue inhibitors of metalloproteinases in cancer. Oncogene 21:2245–2252CrossRefPubMed

Jones JL, Walker RA (1997) Control of matrix metalloproteinase activity in cancer. J Pathol 183:377–379CrossRefPubMed

Kim JB, Stein R, O’Hare MJ (2005) Tumour-stromal interactions in breast cancer: the role of stroma in tumourigenesis. Tumour Biol 26:173–185CrossRefPubMed

Liu N, Lapcevich RK, Underhill CB et al (2001) Metastatin: a hyaluronan-binding complex from cartilage that inhibits tumor growth. Cancer Res 61:1022–1028PubMed

Manes S, Llorente M, Lacalle RA et al (1999) The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells. J Biol Chem 274:6935–6945CrossRefPubMed

Marberger M, Carroll PR, Zelefsky MJ et al (2008) New treatments for localized prostate cancer. Urology 72:S36–S43CrossRefPubMed

Nelson AR, Fingleton B, Rothenberg ML, Matrisian LM (2000) Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol 18:1135–1149PubMed

Noel A, Boulay A, Kebers F et al (2000) Demonstration in vivo that stromelysin-3 functions through its proteolytic activity. Oncogene 19:1605–1612CrossRefPubMed

Parker RL, Huntsman DG, Lesack DW et al (2002) Assessment of interlaboratory variation in the immunohistochemical determination of estrogen receptor status using a breast cancer tissue microarray. Am J Clin Pathol 117:723–728CrossRefPubMed

Stamey TA, Yang N, Hay AR, McNeal JE, Freiha FS, Redwine E (1987) Prostate-specific antigen as a serum marker for adenocarcinoma of the prostate. N Engl J Med 317:909–916CrossRefPubMed

Stetler-Stevenson WG (1999) Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention. J Clin Invest 103:1237–1241CrossRefPubMed

Tlsty TD, Coussens LM (2006) Tumor stroma and regulation of cancer development. Annu Rev Pathol 1:119–150CrossRefPubMed

Turk V, Kos J, Turk B (2004) Cysteine cathepsins (proteases)–on the main stage of cancer? Cancer Cell 5:409–410CrossRefPubMed

Wurtz SO, Schrohl AS, Sorensen NM et al (2005) Tissue inhibitor of metalloproteinases-1 in breast cancer. Endocr Relat Cancer 12:215–227CrossRefPubMed

Titel: Comparative study of stromal metalloproteases expression in patients with benign hyperplasia and prostate cancer
verfasst von: Safwan Escaff
Jesús M. Fernández
Luis O. González
Aurelio Suárez
Salomé González-Reyes
José M. González
Francisco J. Vizoso
Publikationsdatum: 01.03.2011
Verlag: Springer-Verlag
Erschienen in: Journal of Cancer Research and Clinical Oncology / Ausgabe 3/2011
Print ISSN: 0171-5216
Elektronische ISSN: 1432-1335
DOI: https://doi.org/10.1007/s00432-010-0906-8

Springer Medizin

Comparative study of stromal metalloproteases expression in patients with benign hyperplasia and prostate cancer