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Expression of “a disintegrin and metalloproteinase-33” (ADAM-33) protein in laryngeal squamous cell carcinoma

Published online by Cambridge University Press:  02 March 2012

O Topal ,
H Erinanc ,
C Ozer ,
E T Canpolat ,
S B Celik  and
S S Erbek
O Topal*
Affiliation:
Department of Otolaryngology, Faculty of Medicine, Başkent University, Ankara, Turkey
H Erinanc
Affiliation:
Department of Pathology, Faculty of Medicine, Başkent University, Ankara, Turkey
C Ozer
Affiliation:
Department of Otolaryngology, Faculty of Medicine, Başkent University, Ankara, Turkey
E T Canpolat
Affiliation:
Department of Pathology, Faculty of Medicine, Başkent University, Ankara, Turkey
S B Celik
Affiliation:
Department of Otolaryngology, Faculty of Medicine, Başkent University, Ankara, Turkey
S S Erbek
Affiliation:
Department of Otolaryngology, Faculty of Medicine, Başkent University, Ankara, Turkey
*
Address for correspondence: Dr Ozgul Topal, Department of Otolaryngology, Başkent University Konya Research and Teaching Center, Saray Caddesi No 1 Selcuklu, Ankara, 42080Turkey Fax: +90 332 2570637 E-mail: [email protected]
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Abstract

Objective:

A disintegrin and metalloproteinase domain containing protein 33 (also known as ADAM-33) is a member of a matrix metalloproteinase family which mediates extracellular matrix remodelling and changes in cellular adhesion. This study aimed to evaluate expression of this protein in laryngeal squamous cell carcinoma, and to determine its correlation with patients' clinicopathological characteristics.

Subjects and methods:

Forty paraffin blocks of laryngeal carcinoma underwent immunohistochemical staining to detect “a disintegrin and metalloproteinase-33” expression. Case records were reviewed to determine patient characteristics.

Results:

All epithelial, vascular and stromal staining scores were significantly increased in tumour tissue compared with controls (p < 0.001). However, patients' clinical characteristics at the time of diagnosis, and their disease extent, did not correlate significantly with the immunohistochemical staining scores.

Conclusion:

This study suggests that increased expression of “a disintegrin and metalloproteinase-33” may play a role in the pathogenesis of laryngeal carcinoma.

Keywords

Laryngeal NeoplasmsCarcinomaA Disintegrin And Metalloproteinase-33 ProteinHuman
Type
Main Articles
Information
The Journal of Laryngology & Otology , Volume 126 , Issue 5 , May 2012 , pp. 511 - 515
Copyright
Copyright © JLO (1984) Limited 2012

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References

1Almadori, G, Bussu, F, Cadoni, G, Galli, J, Paludetti, G, Maurizi, M. Molecular markers in laryngeal squamous cell carcinoma: towards an integrated clinicobiological approach. Eur J Cancer 2005;41:683–93CrossRefGoogle ScholarPubMed
2Almadori, G, Bussu, F, Paludetti, G. Should there be more molecular staging of head and neck cancer to improve the choice of treatments and thereby improve survival? Curr Opin Otolaryngol Head Neck Surg 2008;16:117–26CrossRefGoogle ScholarPubMed
3Loyo, M, Pai, SI. The molecular genetics of laryngeal cancer. Otolaryngol Clin North Am 2008;41:657–72CrossRefGoogle ScholarPubMed
4Wolfsberg, TG, Primakoff, P, Myles, DG, White, JM. ADAM, a novel family of membrane proteins containing a disintegrin and metalloproteinase domain: multipotential functions in cell-cell and cell-matrix interactions. J Cell Biol 1995;131:275–8CrossRefGoogle Scholar
5Yamamoto, S, Higuchi, Y, Yoshiyama, K, Shimizu, E, Kataoka, M, Hijiya, N et al. ADAM family proteins in the immune system. Immunol Today 1999;20:278–84CrossRefGoogle ScholarPubMed
6Edwards, DR, Handsley, MM, Pennington, CJ. The ADAM metalloproteinases. Mol Aspects Med 2008;29:258–89CrossRefGoogle ScholarPubMed
7Puxeddu, I, Pang, YY, Harvey, A, Haitchi, HM, Nicholas, B, Yoshisue, H et al. The soluble form of a disintegrin and metalloprotease 33 promotes angiogenesis: implications for airway remodeling in asthma. J Allergy Clin Immunol 2008;121:1400–6CrossRefGoogle ScholarPubMed
8American Joint Committee on Cancer. AJCC Cancer Staging Manual. Larynx, 6th edn.New York: Springer; 2002;47–57Google Scholar
9Figueiredo, DL, Mamede, RCM, Spagnoli, GC, Silva, WA Jr, Zago, M, Neder, L et al. High expression of cancer testis antigens MAGE-A, MAGE-C1/CT7, MAGE-C2/CT10, NY-ESO-1, and GAGE in advanced squamous cell carcinoma of the larynx. Head Neck 2011;33:702–7CrossRefGoogle ScholarPubMed
10Erbek, SS, Erinanc, H, Erbek, S, Topal, O, Kiyici, H. Expression of a disintegrin and metalloproteinase 33 protein in nasal polyposis: an immunohistochemical study. Am J Rhinol Allergy 2010;24:79–82CrossRefGoogle ScholarPubMed
11Kim, KE, Song, H, Hahm, C, Yoon, SY, Park, S, Lee, H et al. Expression of ADAM33 is a novel regulatory mechanism in IL-18-secreted process in gastric cancer. J Immunol 2009;182:3548–55CrossRefGoogle ScholarPubMed
12Seniski, GG, Camargo, AA, Ierardi, DF, Ramos, EAS, Grochoski, M, Ribeiro, ESF et al. ADAM33 gene silencing by promotor hypermethylation as a molecular marker in breast invasive lobular carcinoma. BMC Cancer 2009;9:80CrossRefGoogle Scholar
13Dijkstra, A, Postma, DS, Noordhoek, JA, Lodewijk, ME, Kauffman, HF, Hacken, NHT et al. Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung. Virchows Arch 2009;454:441–9CrossRefGoogle Scholar
14Van Eerdewegh, P, Little, RD, Dupuis, J, Del Mastro, RG, Falls, K, Simon, J et al. Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness. Nature 2002;418:426–30CrossRefGoogle ScholarPubMed
15Powell, RN, Wicks, J, Holloway, JW, Holgate, ST, Davies, DE. The splicing and fate of ADAM33 transcripts in primary human airways fibroblasts. Am J Respir Cell Mol Biol 2004;31:13–21CrossRefGoogle ScholarPubMed
16Roy, R, Zhang, B, Moses, MA. Making the cut: protease-mediated regulation of angiogenesis. Exp Cell Res 2006;312:608–22CrossRefGoogle ScholarPubMed