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Expression of cluster of differentiation 9 glycoprotein in benign and malignant parotid gland tumours

Published online by Cambridge University Press:  22 May 2009

K Sakamoto*
Affiliation:
Department of Otolaryngology-Head & Neck Surgery, Kurume University School of Medicine, Kurume, Japan
T Ono
Affiliation:
Department of Otolaryngology-Head & Neck Surgery, Kurume University School of Medicine, Kurume, Japan
Y Nakamura
Affiliation:
Department of Pathology, St Mary's Hospital, Kurume, Japan.
H Harada
Affiliation:
Department of Pathology, Kurume University School of Medicine, Kurume, Japan
T Nakashima
Affiliation:
Department of Otolaryngology-Head & Neck Surgery, Kurume University School of Medicine, Kurume, Japan
*
Address for correspondence: Dr Kikuo Sakamoto, Department of Otolaryngology-Head and Neck Surgery, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan. Fax: +81 942 37 1200 E-mail: [email protected]

Abstract

Objectives:

This study aimed to clarify the significance of cluster of differentiation 9 glycoprotein gene expression in human parotid gland tumours.

Methods:

We retrospectively analysed immunohistochemical staining for cluster of differentiation 9 glycoprotein in parotid gland tumours.

Results:

Cluster of differentiation 9 glycoprotein was consistently detected in the normal parotid gland. Regarding benign parotid gland tumours, cluster of differentiation 9 glycoprotein was present in 13 of 18 pleomorphic adenomas, in all Warthin tumours tested (21/21) and in all cases of basal cell adenoma tested (four of four). In contrast, positive staining for cluster of differentiation 9 glycoprotein was less often observed in malignant parotid tumours. Cluster of differentiation 9 glycoprotein was present in 11 of 14 mucoepidermoid carcinomas, in two of five acinic cell carcinomas and in two of five adenoid cystic carcinomas.

Conclusions:

There was a statistically significantly reduced expression of cluster of differentiation 9 glycoprotein in malignant parotid gland tumours, compared with benign parotid gland tumours (p < 0.05). These results suggest that a low level of cluster of differentiation 9 glycoprotein expression in parotid gland tumours may be associated with malignancy.

Type
Main Articles
Copyright
Copyright © JLO (1984) Limited 2009

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References

1Kersey, JH, LeBien, TW, Abramson, CS, Newman, R, Sutherland, R, Greaves, M. A human leukemia-associated and lymphohemopoietic progenitor cell surface structure identified with monoclonal antibody. J Exp Med 1981;153:726–31CrossRefGoogle ScholarPubMed
2Iwamoto, R, Senoh, H, Okada, Y, Uchida, T, Mekada, E. An antibody that inhibits the binding of diphtheria toxin to cells reveals the association of a 27-kDa membrane protein with the diphtheria toxin receptor. J Biol Chem 1991;266:20463–9CrossRefGoogle ScholarPubMed
3Ikeyama, S, Koyama, M, Yamaoka, M, Sasada, R, Miyake, M.Suppression of cell motility and metastasis by transfection with human motility related protein (MRP-1/CD9) DNA. J Exp Med 1993;177:1231–7CrossRefGoogle ScholarPubMed
4Iwamoto, R, Higashiyama, S, Mitamura, T, Taniguchi, N, Klagsbrun, M, Mekada, E. Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity. EMBO J 1994;13:2322–30CrossRefGoogle Scholar
5Higashiyama, S, Iwamoto, R, Goishi, K, Raab, N, Taniguchi, N, Klagsbrun, M, Mekada, E. The membrane protein CD9/DRAP27 potentiates the growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor (HB-EGF). J Cell Biol 1995;128:929–38CrossRefGoogle Scholar
6Nakamura, K, Iwamoto, R, Mekada, E. Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J Cell Biol 1995;129:1691–705CrossRefGoogle Scholar
7Masellis-Smith, A, Shaw, AR. CD9-regulated adhesion. Anti-CD9 monoclonal antibody induces pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin. J Immunol 1994;152:2768–77CrossRefGoogle ScholarPubMed
8Shaw, AR, Domanska, A, Mak, A, Gilchrist, A, Dobler, K, Visser, L, Poppema, S. Ectopic expression of human and feline CD9 in a human B cell line confers β1 integrin-dependent motility on fibronectin and laminin substrates and enhanced tyrosine phosphorylation. J Biol Chem 1995;270:24092–9CrossRefGoogle Scholar
9Higashiyama, M, Taki, T, Ikei, Y, Adachi, M, Huang, C, Koh, T, Kodama, K, Doi, O, Miyake, M.Reduced motility related protein-1 (MRP-1/CD9) gene expression as a factor of poor prognosis in non-small cell lung cancer. Cancer Res 1995;55:6040–4Google ScholarPubMed
10Miyake, M, Nakano, K, Itoi, S, Koh, T, Taki, T. Motility-related protein-1 (MRP-1/CD9) reduction as a factor of poor prognosis in breast cancer. Cancer Res 1996;56:1244–9Google ScholarPubMed
11Mitamura, T, Iwamoto, R, Umata, T, Yomo, T, Urabe, I, Tsuneoka, M, Mekada, E. The 27-kDa diphtheria toxin receptor-associated protein (DRAP27) from Vero cells is the monkey homologue of human CD9 antigen: expression of DRAP27 elevates the number of diphtheria toxin receptors on toxin-sensitive cells. J Cell Biol 1992;118:1389–99CrossRefGoogle ScholarPubMed
12Carter, WG, Wayner, EA, Bouchard, TS, Kaur, P. The role of integrins α2β1 and α3β1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 1990;110:1387–404CrossRefGoogle Scholar
13Si, Z, Hersey, P. Expression of the neuroglandular antigen and analogues in melanoma: CD9 expression appears inversely related to metastatic potential of melanoma. Int J Cancer 1993;54:3743CrossRefGoogle ScholarPubMed
14Horejsi, V, Vlcek, C. Novel structurally distinct family of leukocyte surface glycoproteins including CD9, CD37, CD53 and CD63. FEBS Lett 1991;288:14CrossRefGoogle ScholarPubMed
15Rubinstein, E, Le Naour, F, Lagaudrière, C, Billard, M, Conjeaud, H, Boucheix, C. CD9, CD63, CD81, and CD82 are components of a tetraspan network connected to HLA-DR and VLA integrins. Eur J Immunol 1996;26:2657–65CrossRefGoogle ScholarPubMed
16Dong, JT, Lamb, PW, Rinker-Schaeffer, CW, Vukanovic, J, Ichikawa, T, Isaacs, JT, Barrett, JC. A metastasis suppressor gene for prostate cancer on human chromosome 11p11.2. Science 1995;268:884–6CrossRefGoogle ScholarPubMed
17Hotta, H, Ross, AH, Huebner, K, Isobe, M, Wendeborn, S, Chao, MV, Ricciardi, RP, Tsujimoto, Y, Croce, CM, Koprowski, H.Molecular cloning and characterization of an antigen associated with early stages of melanoma tumor progression. Cancer Res 1988;48:2955–62Google ScholarPubMed
18Nakamura, Y, Yamamoto, M, Sakamoto, K, Ohto, K, Umeda, A, Tsukamoto, T, Nakashima, T. Growth factors, extracellular matrix components and cell adhesion molecules in Warthin's tumor. J Oral Pathol Med 2001;30:290–5CrossRefGoogle ScholarPubMed
19Korsrud, FR, Brandtzaeg, P. Immunohistochemical characterization of cellular immunoglobulins and epithelial marker antigens in Warthin's tumor. Hum Pathol 1984;15:361–7CrossRefGoogle ScholarPubMed
20Kusukawa, J, Ryu, F, Kameyama, T, Mekada, E. Reduced expression of CD9 in oral squamous cell carcinoma: CD9 expression inversely related to high prevalence of lymph node metastasis. J Oral Pathol Med 2001;30:73–9CrossRefGoogle ScholarPubMed