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Erschienen in: Digestive Diseases and Sciences 12/2011

01.12.2011 | Original Article

Clinical Impact of HAb18G/CD147 Expression in Esophageal Squamous Cell Carcinoma

verfasst von: Shaojun Zhu, Yanhong Li, Li Mi, Yang Zhang, Li Zhang, Li Gong, Xiujuan Han, Li Yao, Miao Lan, Zhinan Chen, Wei Zhang

Erschienen in: Digestive Diseases and Sciences | Ausgabe 12/2011

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Abstract

Background

HAb18G/CD147 expression has been associated with many tumor invasion molecules, which play important roles in recurrence and poor differentiation of esophageal squamous cell carcinoma (ESCC). However, the clinical implications of HAb18G/CD147 in ESCC are still unclear.

Aims

In this study, we clarified the clinical significance of HAb18G/CD147 and characterized the association between HAb18G/CD147 and tumor invasion in ESCC cases.

Methods

Tumor tissues were obtained from 86 ESCC patients who underwent surgical resection between 2002 and 2005. All patients that had received previous therapy were excluded. ESCC tissues were analyzed by IHC using anti HAb18G/CD147 antibody. The expression of HAb18G/CD147 mRNA in esophageal cancer cell lines was analyzed by RT–PCR.

Results

HAb18G/CD147 was uniformly expressed in EC109 and EC871214 cell lines, but negatively expressed in EPC2, esophageal normal squamous cell line. HAb18G/CD147 mainly localized to the membrane of tumor cells in 84.9% of ESCC patients (64 out of 86 cases). Furthermore, we also found that higher HAb18G/CD147 expression levels significantly correlated with lymph node metastasis, depth of tumor invasion and differentiation (P < 0.05). But the expression levels of HAb18G/CD147 in lymph node metastatic tissues were almost equal to that in the primary tumor tissues. Furthermore, lymph node metastasis and expression of HAB18G/CD147 were independent prognostic indicators in ESCC.

Conclusions

The expression of HAb18G/CD147 might be involved in the progression and survival of ESCC. Therefore, HAb18G/CD147 could be a clinical marker for the poor prognosis in ESCC patients and may also be a potentially therapeutic target to improve the progression of ESCC.
Literatur
1.
Zurück zum Zitat Stoner GD, Gupta A. Etiology and chemoprevention of esophageal squamous cell carcinoma. Carcinogenesis. 2001;22:1737–1746.PubMedCrossRef Stoner GD, Gupta A. Etiology and chemoprevention of esophageal squamous cell carcinoma. Carcinogenesis. 2001;22:1737–1746.PubMedCrossRef
2.
Zurück zum Zitat Stoner GD, Rustgi AK. Biology of the esophageal squamous cell carcinoma. Gastrointest Cancers Biol Diagn. 1995;8:141–146. Stoner GD, Rustgi AK. Biology of the esophageal squamous cell carcinoma. Gastrointest Cancers Biol Diagn. 1995;8:141–146.
3.
Zurück zum Zitat WHO. The World Health Report 1997—conquering suffering, enriching humanity. World Health Forum. 1997;18:248–260. WHO. The World Health Report 1997—conquering suffering, enriching humanity. World Health Forum. 1997;18:248–260.
4.
Zurück zum Zitat Reed CE. Surgical management of esophageal carcinoma. Oncologist. 1999;4:95–105.PubMed Reed CE. Surgical management of esophageal carcinoma. Oncologist. 1999;4:95–105.PubMed
5.
Zurück zum Zitat De LL, Curia MC, Aceto GM, et al. Analysis of extended genomic rearrangements in oncological research. Ann Oncol. 2007;18:173–178. De LL, Curia MC, Aceto GM, et al. Analysis of extended genomic rearrangements in oncological research. Ann Oncol. 2007;18:173–178.
6.
Zurück zum Zitat Biswas C, Zhang Y, DeCastro R, et al. The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res. 1995;55:434–439.PubMed Biswas C, Zhang Y, DeCastro R, et al. The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res. 1995;55:434–439.PubMed
7.
Zurück zum Zitat Tang W, Chang SB, Hemler ME. Links between CD147 function, glycosylation, and caveolin-1. Mol Biol Cell. 2004;15:4043–4050.PubMedCrossRef Tang W, Chang SB, Hemler ME. Links between CD147 function, glycosylation, and caveolin-1. Mol Biol Cell. 2004;15:4043–4050.PubMedCrossRef
8.
Zurück zum Zitat Yan L, Zucker S, Toole BP, et al. Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression. Thromb Haemost. 2005;93:199–204.PubMed Yan L, Zucker S, Toole BP, et al. Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression. Thromb Haemost. 2005;93:199–204.PubMed
9.
Zurück zum Zitat Kirk P, Wilson MC, Heddle C, et al. CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. EMBO J. 2000;19:3896–3904.PubMedCrossRef Kirk P, Wilson MC, Heddle C, et al. CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. EMBO J. 2000;19:3896–3904.PubMedCrossRef
10.
Zurück zum Zitat Xu D, Hemler ME. Metabolic activation-related CD147-CD98 complex. Mol Cell Proteomics. 2005;4:1061–1071.PubMedCrossRef Xu D, Hemler ME. Metabolic activation-related CD147-CD98 complex. Mol Cell Proteomics. 2005;4:1061–1071.PubMedCrossRef
11.
Zurück zum Zitat Berditchevski F, Chang S, Bodorova J, et al. Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. J Biol Chem. 1997;272:29174–29180.PubMedCrossRef Berditchevski F, Chang S, Bodorova J, et al. Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. J Biol Chem. 1997;272:29174–29180.PubMedCrossRef
12.
Zurück zum Zitat Curtin KD, Meinertzhagen IA, Wyman RJ. Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture. J Cell Sci. 2005;118:2649–2660.PubMedCrossRef Curtin KD, Meinertzhagen IA, Wyman RJ. Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture. J Cell Sci. 2005;118:2649–2660.PubMedCrossRef
13.
Zurück zum Zitat Gordon JM, Bauer EA, Eisen AZ. Collagenase in human cornea: immunologic localization. Arch Ophthalmol. 1980;98:341–345.PubMedCrossRef Gordon JM, Bauer EA, Eisen AZ. Collagenase in human cornea: immunologic localization. Arch Ophthalmol. 1980;98:341–345.PubMedCrossRef
14.
Zurück zum Zitat Wagoner MD, Kenyon KR. Distribution of collagenase and cell types in sterile ulceration of human corneal grafts. Acta Ophthalmol. 1989;192:65–71. Wagoner MD, Kenyon KR. Distribution of collagenase and cell types in sterile ulceration of human corneal grafts. Acta Ophthalmol. 1989;192:65–71.
15.
Zurück zum Zitat Major TC, Liang L, Lu X, Rosebury W, Bocan TM. Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma. Arterioscler Thromb Vasc Biol. 2002;22:1200–1207.PubMedCrossRef Major TC, Liang L, Lu X, Rosebury W, Bocan TM. Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma. Arterioscler Thromb Vasc Biol. 2002;22:1200–1207.PubMedCrossRef
16.
Zurück zum Zitat Li Z, Ren Y, Wu QC, et al. Macrophage migration inhibitory factor enhances neoplastic cell invasion by inducing the expression of matrixmetalloproteinase 9 and interleukin-8 in nasopharyngeal carcinoma cell lines. J Chin Med. 2004;117:107–114. Li Z, Ren Y, Wu QC, et al. Macrophage migration inhibitory factor enhances neoplastic cell invasion by inducing the expression of matrixmetalloproteinase 9 and interleukin-8 in nasopharyngeal carcinoma cell lines. J Chin Med. 2004;117:107–114.
17.
Zurück zum Zitat Zucker S, Hymowitz M, Rollo EE, et al. Tumorigenic potential of extracellular matrixmetalloproteinase inducer. Am J Pathol. 2001;158:1921–1928.PubMedCrossRef Zucker S, Hymowitz M, Rollo EE, et al. Tumorigenic potential of extracellular matrixmetalloproteinase inducer. Am J Pathol. 2001;158:1921–1928.PubMedCrossRef
18.
Zurück zum Zitat Ramos-Simone N, Hahn-Dantona E, Sipley J, et al. Activation of matrix metalloprotease-9 (MMP-9) via a converting plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem. 1999;274:13066–13076.CrossRef Ramos-Simone N, Hahn-Dantona E, Sipley J, et al. Activation of matrix metalloprotease-9 (MMP-9) via a converting plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem. 1999;274:13066–13076.CrossRef
19.
Zurück zum Zitat Davidson B, Goldberg I, Berner A, et al. EMMPRIN (extracellular matrix metalloproteinase inducer) is a novel marker of poor outcome in serous ovarian carcinoma. Clin Exp Metastasis. 2003;20:161–169.PubMedCrossRef Davidson B, Goldberg I, Berner A, et al. EMMPRIN (extracellular matrix metalloproteinase inducer) is a novel marker of poor outcome in serous ovarian carcinoma. Clin Exp Metastasis. 2003;20:161–169.PubMedCrossRef
20.
Zurück zum Zitat Guo H, Li R, Zucker S, et al. EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. Cancer Res. 2000;60:888–891.PubMed Guo H, Li R, Zucker S, et al. EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. Cancer Res. 2000;60:888–891.PubMed
21.
Zurück zum Zitat Bourguignon L, Gunja-Smith Z, Iida N, et al. CD44v (3, 8–10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J Cell Physiol. 1998;176:206–215.PubMedCrossRef Bourguignon L, Gunja-Smith Z, Iida N, et al. CD44v (3, 8–10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J Cell Physiol. 1998;176:206–215.PubMedCrossRef
22.
Zurück zum Zitat Li Z, Ren Y, Wu QC, et al. Macrophage migration inhibitory factor enhances neoplastic cell invasion by inducing the expression of matrix metalloproteinase 9 and interleukin-8 in nasopharyngeal carcinoma cell lines. Chin Med J. 2004;117:107–114.PubMed Li Z, Ren Y, Wu QC, et al. Macrophage migration inhibitory factor enhances neoplastic cell invasion by inducing the expression of matrix metalloproteinase 9 and interleukin-8 in nasopharyngeal carcinoma cell lines. Chin Med J. 2004;117:107–114.PubMed
23.
Zurück zum Zitat Tang J, Zhou HW, Jiang JL, et al. ßig-h3 is involved in the CD147/CD147-mediated metastasis process in human hepatoma cells. Exp Biol Med. 2007;232:344–352. Tang J, Zhou HW, Jiang JL, et al. ßig-h3 is involved in the CD147/CD147-mediated metastasis process in human hepatoma cells. Exp Biol Med. 2007;232:344–352.
24.
Zurück zum Zitat Cheng MF, Tzao C, Tsai WC, et al. Expression of EMMPRIN and matriptase in esophageal squamous cell carcinoma: correlation with clinicopathological parameters. Dis Esophagus. 2006;19:482–486.PubMedCrossRef Cheng MF, Tzao C, Tsai WC, et al. Expression of EMMPRIN and matriptase in esophageal squamous cell carcinoma: correlation with clinicopathological parameters. Dis Esophagus. 2006;19:482–486.PubMedCrossRef
25.
Zurück zum Zitat Tang J, Wu YM, Zhao P, Yang XM, Jiang JL, Chen ZN. Overexpression of HAb18G/CD147 promotes invasion and metastasis via alpha3beta1 integrin mediated FAK-paxillin and FAK-PI3K-Ca2+ pathways. Cell Mol Life Sci. 2008;65:2933–2942.PubMedCrossRef Tang J, Wu YM, Zhao P, Yang XM, Jiang JL, Chen ZN. Overexpression of HAb18G/CD147 promotes invasion and metastasis via alpha3beta1 integrin mediated FAK-paxillin and FAK-PI3K-Ca2+ pathways. Cell Mol Life Sci. 2008;65:2933–2942.PubMedCrossRef
26.
Zurück zum Zitat Iwasa S, Okada K, Chen WT, et al. Increased expression of seprase, a membrane-type serine protease, is associated with lymph node metastasis in human colorectal cancer. Cancer Lett. 2003;199:91–98.PubMedCrossRef Iwasa S, Okada K, Chen WT, et al. Increased expression of seprase, a membrane-type serine protease, is associated with lymph node metastasis in human colorectal cancer. Cancer Lett. 2003;199:91–98.PubMedCrossRef
27.
Zurück zum Zitat Ariga N, Sato E, Ohuchi N, Nagura H, Ohtani H. Stromal expression of fibroblast activation protein/seprase, a cell membrane serine proteinase and gelatinase, is associated with longer survival in patients with invasive ductal carcinoma of breast. Int J Cancer. 2001;95:67–72.PubMedCrossRef Ariga N, Sato E, Ohuchi N, Nagura H, Ohtani H. Stromal expression of fibroblast activation protein/seprase, a cell membrane serine proteinase and gelatinase, is associated with longer survival in patients with invasive ductal carcinoma of breast. Int J Cancer. 2001;95:67–72.PubMedCrossRef
28.
Zurück zum Zitat Caudroy S, Polette M, Tournier JM, et al. Expression of the extracellular matrix metalloproteinase inducer (EMMPRIN) and the matrix metalloproteinase-2 in bronchopulmonary and breast lesions. J Histochem Cytochem. 1999;47:1575–1580.PubMedCrossRef Caudroy S, Polette M, Tournier JM, et al. Expression of the extracellular matrix metalloproteinase inducer (EMMPRIN) and the matrix metalloproteinase-2 in bronchopulmonary and breast lesions. J Histochem Cytochem. 1999;47:1575–1580.PubMedCrossRef
29.
Zurück zum Zitat Polette M, Gilles C, Marchand V, et al. Tumor collagenase stimulatory factor (TCSF) expression and localization in human lung and breast cancers. J Histochem Cytochem. 1997;45:703–709.PubMedCrossRef Polette M, Gilles C, Marchand V, et al. Tumor collagenase stimulatory factor (TCSF) expression and localization in human lung and breast cancers. J Histochem Cytochem. 1997;45:703–709.PubMedCrossRef
30.
Zurück zum Zitat Bordador LC, Li X, Toole B, et al. Expression of EMMPRIN by oral squamous cell carcinoma. Int J Cancer. 2000;85:347–352.PubMedCrossRef Bordador LC, Li X, Toole B, et al. Expression of EMMPRIN by oral squamous cell carcinoma. Int J Cancer. 2000;85:347–352.PubMedCrossRef
31.
Zurück zum Zitat Thorns C, Feller AC, Merz H. EMMPRIN (CD 174) is expressed in Hodgkin’s lymphoma and anaplastic large cell lymphoma. An immunohistochemical study of 60 cases. Anticancer Res. 2002;22:1983–1986.PubMed Thorns C, Feller AC, Merz H. EMMPRIN (CD 174) is expressed in Hodgkin’s lymphoma and anaplastic large cell lymphoma. An immunohistochemical study of 60 cases. Anticancer Res. 2002;22:1983–1986.PubMed
32.
Zurück zum Zitat Gabison EE, Huet E, Baudouin C, Menashi S. Direct epithelial-stromal interaction in corneal wound healing: Role of EMMPRIN/CD147 in MMPs induction and beyond. Prog Retin Eye Res. 2009;28:19–33.PubMedCrossRef Gabison EE, Huet E, Baudouin C, Menashi S. Direct epithelial-stromal interaction in corneal wound healing: Role of EMMPRIN/CD147 in MMPs induction and beyond. Prog Retin Eye Res. 2009;28:19–33.PubMedCrossRef
33.
Zurück zum Zitat Yu W, Liu J, Xiong X, Ai Y, Wang H. Expression of MMP9 and CD147 in invasive squamous cell carcinoma of the uterine cervix and their implication. Pathol Res Pract. 2009;205:709–715.PubMedCrossRef Yu W, Liu J, Xiong X, Ai Y, Wang H. Expression of MMP9 and CD147 in invasive squamous cell carcinoma of the uterine cervix and their implication. Pathol Res Pract. 2009;205:709–715.PubMedCrossRef
34.
Zurück zum Zitat Riethdorf S, Reimers N, Assmann V, et al. High incidence of EMMPRIN expression in human tumors. Int J Cancer. 2006;119:1800–1810.PubMedCrossRef Riethdorf S, Reimers N, Assmann V, et al. High incidence of EMMPRIN expression in human tumors. Int J Cancer. 2006;119:1800–1810.PubMedCrossRef
35.
Zurück zum Zitat Nabeshima K, Iwasaki H, Koga K, Hojo H, Suzumiya J, Kikuchi M. Emmprin (basigin/CD147): matrix metalloproteinase modulator and multifunctional cell recognition molecule that plays a critical role in cancer progression. Pathol Int. 2006;56:359–367.PubMedCrossRef Nabeshima K, Iwasaki H, Koga K, Hojo H, Suzumiya J, Kikuchi M. Emmprin (basigin/CD147): matrix metalloproteinase modulator and multifunctional cell recognition molecule that plays a critical role in cancer progression. Pathol Int. 2006;56:359–367.PubMedCrossRef
36.
Zurück zum Zitat Tang Y, Kesavan P, Nakada MT, Yan L. Tumor-stroma interaction: positive feedback regulation of extracellular matrix metalloproteinase inducer (EMMPRIN) expression and matrix metalloproteinase-dependent generation of soluble EMMPRIN. Mol Cancer Res. 2004;2:73–80.PubMed Tang Y, Kesavan P, Nakada MT, Yan L. Tumor-stroma interaction: positive feedback regulation of extracellular matrix metalloproteinase inducer (EMMPRIN) expression and matrix metalloproteinase-dependent generation of soluble EMMPRIN. Mol Cancer Res. 2004;2:73–80.PubMed
37.
Zurück zum Zitat Moll UM, Lane B, Zucker S, Suzuki K, Nagase H. Localization of collagenase at the basal plasma membrane of a human pancreatic carcinoma cell line. Cancer Res. 1990;50:6995–7002.PubMed Moll UM, Lane B, Zucker S, Suzuki K, Nagase H. Localization of collagenase at the basal plasma membrane of a human pancreatic carcinoma cell line. Cancer Res. 1990;50:6995–7002.PubMed
38.
Zurück zum Zitat Caudroy S, Polette M, Nawrocki-Raby B, et al. EMMPRIN-mediated MMP regulation in tumor and endothelial cells. Clin Exp Metastasis. 2002;19:697–702.PubMedCrossRef Caudroy S, Polette M, Nawrocki-Raby B, et al. EMMPRIN-mediated MMP regulation in tumor and endothelial cells. Clin Exp Metastasis. 2002;19:697–702.PubMedCrossRef
39.
Zurück zum Zitat Menashi S, Serova M, Ma L, Vignot S, Mourah S, Calvo F. Regulation of extracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells. Cancer Res. 2003;63:7575–7580.PubMed Menashi S, Serova M, Ma L, Vignot S, Mourah S, Calvo F. Regulation of extracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells. Cancer Res. 2003;63:7575–7580.PubMed
40.
Zurück zum Zitat Qian AR, Zhang W, Cao JP, et al. Downregulation of CD147 expression alters cytoskeleton architecture and inhibits gelatinase production and SAPK pathway in human hepatocellular carcinoma cells. J Exp Clin Cancer Res. 2008;27:50.PubMedCrossRef Qian AR, Zhang W, Cao JP, et al. Downregulation of CD147 expression alters cytoskeleton architecture and inhibits gelatinase production and SAPK pathway in human hepatocellular carcinoma cells. J Exp Clin Cancer Res. 2008;27:50.PubMedCrossRef
Metadaten
Titel
Clinical Impact of HAb18G/CD147 Expression in Esophageal Squamous Cell Carcinoma
verfasst von
Shaojun Zhu
Yanhong Li
Li Mi
Yang Zhang
Li Zhang
Li Gong
Xiujuan Han
Li Yao
Miao Lan
Zhinan Chen
Wei Zhang
Publikationsdatum
01.12.2011
Verlag
Springer US
Erschienen in
Digestive Diseases and Sciences / Ausgabe 12/2011
Print ISSN: 0163-2116
Elektronische ISSN: 1573-2568
DOI
https://doi.org/10.1007/s10620-011-1812-x

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