Increased Expression of Hyaluronic Acid Binding Protein 1 Is Correlated With Poor Prognosis in Patients With Breast Cancer

被引:55
作者
Chen, Yan-Bo [1 ]
Jiang, Chuan-Tao [2 ]
Zhang, Guo-Qiang [1 ]
Wang, Jin-Song [1 ]
Pang, Da [1 ]
机构
[1] Harbin Med Coll, Dept Breast Surg, Affiliated Tumor Hosp, Harbin 150081, Heilongjiang Pr, Peoples R China
[2] Univ Texas Hlth Sci Ctr, Brown Fdn Inst Mol Med, Houston, TX USA
关键词
breast cancer; HABP1; prognosis; metastasis; SPLICING FACTOR SF2; TUMOR-CELLS; GLOBULAR HEADS; P-32; PROTEIN; HABP1/P32/GC1QR; LOCALIZATION; DROSOPHILA; APOPTOSIS; POLARITY; SURFACE;
D O I
10.1002/jso.21329
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Background and Objectives: Hyaluronic acid binding protein I (HABP1), a family of proteins interacting with hyaluronan (HA), had been associated with cell adhesion and tumor invasion. The aim of this Study was to investigate the correlation between clinicopathologic factors and patient survival time with the expression of HABP1 in breast cancer patients. Methods: Expression of HABP1 mRNA and protein were detected with real-time quantitative PCR and immunohistochemical staining in 63 breast cancer and non-cancerous matched tissues. Results: The mRNA expression level of HABP1 was unrelated to the patient's age, tumor size, histological grade, TNM stage. However, it proved to be positively related to axillary nodes metastasis (P=0.008). Furthermore, it was shown that the survival rate of patients with low HABP1 expression was significantly higher than that of patients with high HABP1 expression (P=0.025). Multivariate analysis revealed that HABP1 mRNA expression level was a significant factor for predicting prognosis (P=0.022). The immunohistochemistry results showed that the expression level of HABP1 in breast cancer cells was higher than that in normal breast cells. Conclusion: HABP1 might be an independent predictive factor for breast cancer prognosis and up-regulation of HABP1 might play an important role in the metastasis of breast cancer. J. Surg. Oncol. 2009;100:382-386 (C) 2009 Wiley-Liss, Inc.
引用
收藏
页码:382 / 386
页数:5
相关论文
共 34 条
[1]   Hyaluronan in peritumoral stroma and malignant cells associates with breast cancer spreading and predicts survival [J].
Auvinen, P ;
Tammi, R ;
Parkkinen, J ;
Tammi, M ;
Ågren, U ;
Johansson, R ;
Hirvikoski, P ;
Eskelinen, M ;
Kosma, VM .
AMERICAN JOURNAL OF PATHOLOGY, 2000, 156 (02) :529-536
[2]   p32 is a novel mammalian Lgl binding protein that enhances the activity of protein kinase Cζ and regulates cell polarity [J].
Bialucha, Carl U. ;
Ferber, Emma C. ;
Pichaud, Franck ;
Peak-Chew, Sew Y. ;
Fujita, Yasuyuki .
JOURNAL OF CELL BIOLOGY, 2007, 178 (04) :575-581
[3]   Epithelial polarity and proliferation control:: links from the Drosophila neoplastic tumor suppressors [J].
Bilder, D .
GENES & DEVELOPMENT, 2004, 18 (16) :1909-1925
[4]   Mitochondrial protein p32 can accumulate in the nucleus [J].
Brokstad, KA ;
Kalland, KH ;
Russell, WC ;
Matthews, DA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 281 (05) :1161-1169
[5]   Excessive reactive oxygen species induces apoptosis in fibroblasts: Role of mitochondrially accumulated hyaluronic acid binding protein 1 (HABP1/p32/gC1qR) [J].
Chowdhury, Anindya Roy ;
Ghosh, Ora ;
Datta, Kasturi .
EXPERIMENTAL CELL RESEARCH, 2008, 314 (03) :651-667
[6]   Multifunctional activities of human fibroblast 34-kDa hyaluronic acid-binding protein [J].
Das, S ;
Deb, TB ;
Kumar, R ;
Datta, K .
GENE, 1997, 190 (01) :223-225
[7]   Molecular cloning of human fibroblast hyaluronic acid-binding protein confirms its identity with P-32, a protein co-purified with splicing factor SF2 - Kyaluronic acid-binding protein as P-32 protein, co-purified with splicing factor SF2 [J].
Deb, TB ;
Datta, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (04) :2206-2212
[8]   Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma [J].
Fogal, Valentina ;
Zhang, Lianglin ;
Krajewski, Stan ;
Ruoslahti, Erkki .
CANCER RESEARCH, 2008, 68 (17) :7210-7218
[9]   Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway [J].
Ghatak, S ;
Misra, S ;
Toole, BP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (41) :38013-38020
[10]   Structure and function of gC1q-R: a multiligand binding cellular protein [J].
Ghebrehiwet, B ;
Peerschke, EIB .
IMMUNOBIOLOGY, 1998, 199 (02) :225-238