Expression of ADAMTS1 in Colorectal Cancer Tissues and Its Correlation with Prognosis_CHINESE JOURNAL OF BASES AND CLINICS IN GENERAL SURGERY

Authors：

 CHENJing , XUXiao-yang , ZHUXin-jiang ,  DAIDong-qiu

Department of Gastrointestinal Surgery, The Fourth Affiliated Hospital, China Medical University, Shenyang 110032, Liaoning Province, China;

Corresponding?author：

DAIDong-qiu, Email: daidq63@163.com

Keywords：

A disintegrin and metalloproteinase with thrombospondin typeⅠmotif; Colorectal cancer; Matrix metalloproteinase; Prognosis

DOI：

10.7507/1007-9424.20140077

Video：

Export PDF Favorites Scan Get Citation

Abstract Full text Figures/Tables Video References Cited by

Objective To investigate the expression of a disintegrin and metalloproteinase with thrombospondin typeⅠmotif (ADAMTS1) in colorectal cancer tissues, and to study the relationship with clinicopathological features and prognosis of it. Methods Expression of ADAMTS1 was evaluated by immunohistochemistry (SP method) in 65 specimens, which obtained by resection from patients with colorectal cancer, including corresponding adjacent benign tissues. Chi-square test was used for analyzing the relationship between expression of ADAMTS1 and clinicopathological features of colorectal cancer tissues. Cox proportional hazard model was used to explore the relationship between expression of ADAMTS1, other clinicopathological parameters, and patients' survival situation. Results The positive expression rate of ADAMTS1 was 40% (26/65) in the colorectal cancer tissues and 85% (55/65) in the adjacent benign tissues, which was significantly higher in adjacent benign tissues (χ²=27.546, P < 0.001). The positive expression rate of ADAMTS1 was significantly lower in the colorectal cancer tissues with lymph node metastasis than that of the colorectal cancer without lymph node metastasis (χ²=5.329, P=0.021). Results of survival analysis showed that median survival time were 27 months in the ADAMTS1-negative group and 70 months in the ADAMTS1-positive group respectively, and the survival situation was better in latter group (χ²=10.151, P=0.001). Results of multivariable prognostic analysis of Cox proportional hazard model showed that colorectal cancer withⅠ-Ⅱstage (RR=3.782, 95% CI:1.509-9.476, P=0.005), without lymph node metastasis (RR=3.107, 95% CI:1.186-8.138, P=0.021), and with positive-expression of ADAMTS1 (RR=2.020, 95% CI:1.071-3.809, P=0.030) had better survival situation. Conclusions Expression of ADAMTS1 is down-regulated in colorectal cancer tissues and it is associated with lymph node metastasis. The prognosis of patients in ADAMTS1-positive group is better than that of ADAMTS1-negative group, suggesting that ADAMTS1 may be an independent prognostic factor in colorectal cancer.

Citation： CHENJing, XUXiao-yang, ZHUXin-jiang, DAIDong-qiu. Expression of ADAMTS1 in Colorectal Cancer Tissues and Its Correlation with Prognosis. CHINESE JOURNAL OF BASES AND CLINICS IN GENERAL SURGERY, 2014, 21(3): 330-334. doi: 10.7507/1007-9424.20140077 Copy

1.	?Gerhardt S, Hassall G, Hawtin P, et al. Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains[J]. J Mol Biol, 2007, 373(4):891-902.
2.	Kuno K, Kanada N, Nakashima E, et al. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene[J]. J Biol Chem, 1997, 272(1):556-562.
3.	Rocks N, Paulissen G, El Hour M, et al. Emerging roles of ADAM and ADAMTS metalloproteinases in cancer[J]. Biochimie, 2008, 90(2):369-379.
4.	Yang P, Baker KA, Hagg T. The ADAMs family:coordinators of nervous system development, plasticity and repair[J]. Prog Neurobiol, 2006, 79(2):73-94.
5.	Mochizuki S, Okada Y. ADAMs in cancer cell proliferation and progression[J]. Cancer Sci, 2007, 98(5):621-628.
6.	Llamazares M, Obaya AJ, Moncada-Pazos A, et al. The ADAM-TS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway[J]. J Cell Sci, 2007, 120(Pt 20):3544-3552.
7.	Handsley MM, Edwards DR. Metalloproteinases and their inhibi-tors in tumor angiogenesis[J]. Int J Cancer, 2005, 115(6):849-860.
8.	Kuno K, Bannai K, Hakozaki M, et al. The carboxyl-terminal half region of ADAMTS-1 suppresses both tumorigenicity and experimental tumor metastatic potential[J]. Biochem Biophys Res Commun, 2004, 319(4):1327-1333.
9.	Kuno K, Okada Y, Kawashima H, et al. ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan[J]. FEBS Lett, 2000, 478(3):241-245.
10.	Rocks N, Paulissen G, Quesada-Calvo F, et al. ADAMTS-1 metalloproteinase promotes tumor development through the induction of a stromal reaction in vivo[J]. Cancer Res, 2008, 68(22):9541-9550.
11.	Luque A, Carpizo DR, Iruela-Arispe ML. ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165[J]. J Biol Chem, 2003, 278(26):23656-23665.
12.	Vázquez F, Hastings G, Ortega MA, et al. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity[J]. J Biol Chem, 1999, 274(33):23349-23357.
13.	Choi JE, Kim DS, Kim EJ, et al. Aberrant methylation of ADAM-TS1 in non-small cell lung cancer[J]. Cancer Genet Cytogenet, 2008, 187(2):80-84.
14.	Masui T, Hosotani R, Tsuji S, et al. Expression of METH-1 and METH-2 in pancreatic cancer[J]. Clin Cancer Res, 2001, 7(11):3437-3443.
15.	Gustavsson H, Wang W, Jennbacken K, et al. ADAMTS1, a putative anti-angiogenic factor, is decreased in human prostate cancer[J]. BJU Int, 2009, 104(11):1786-1790.
16.	Lind GE, Kleivi K, Meling GI, et al. ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis[J]. Cell Oncol, 2006, 28(5-6):259-272.
17.	Freitas VM, do Amaral JB, Silva TA, et al. Decreased expression of ADAMTS-1 in human breast tumors stimulates migration and invasion[J]. Mol Cancer, 2013, 12:2.
18.	Liu YJ, Xu Y, Yu Q. Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro-and antimetastatic activity, respectively[J]. Oncogene, 2006, 25(17):2452-2467.
19.	Keightley MC, Sales KJ, Jabbour HN. PGF2α-F-prostanoid rece-ptor signalling via ADAMTS1 modulates epithelial cell invasion and endothelial cell function in endometrial cancer[J]. BMC Cancer, 2010, 10:488.
20.	Lu X, Wang Q, Hu G, et al. ADAMTS1 and MMP1 proteolytically engage EGF-like ligands in an osteolytic signaling cascade for bone metastasis[J]. Genes Dev, 2009, 23(16):1882-1894.
21.	陳靜, 戴冬秋, 支宇, 等.胃癌和轉移淋巴結組織ADAMTS1表達及其生物學意義的探討[J].中華腫瘤防治雜志, 2012, 19(1):53-56.
22.	Chu D, Zhao Z, Zhou Y, et al. Matrix metalloproteinase-9 is associated with relapse and prognosis of patients with colorectal cancer[J]. Ann Surg Oncol, 2012, 19(1):318-325.
23.	楊小玲, 何凌霄, 徐禹, 等. 169例結腸癌患者術后3年生存期影響因素分析[J].中國普外基礎與臨床雜志, 2012, 19(7):771-773.
24.	Kirat HT, Ozturd E, Lavery IC, et al. The predictive value of preoperative carcinoembryonic antigen level in the prognosis of colon cancer[J]. Am J Surg, 2012, 204(4):447-452.
25.	Porter S, Span PN, Sweep FC, et al. ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma[J]. Int J Cancer, 2006, 118(5):1241-1247.

1. ?Gerhardt S, Hassall G, Hawtin P, et al. Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains[J]. J Mol Biol, 2007, 373(4):891-902.
2. Kuno K, Kanada N, Nakashima E, et al. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene[J]. J Biol Chem, 1997, 272(1):556-562.
3. Rocks N, Paulissen G, El Hour M, et al. Emerging roles of ADAM and ADAMTS metalloproteinases in cancer[J]. Biochimie, 2008, 90(2):369-379.
4. Yang P, Baker KA, Hagg T. The ADAMs family:coordinators of nervous system development, plasticity and repair[J]. Prog Neurobiol, 2006, 79(2):73-94.
5. Mochizuki S, Okada Y. ADAMs in cancer cell proliferation and progression[J]. Cancer Sci, 2007, 98(5):621-628.
6. Llamazares M, Obaya AJ, Moncada-Pazos A, et al. The ADAM-TS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway[J]. J Cell Sci, 2007, 120(Pt 20):3544-3552.
7. Handsley MM, Edwards DR. Metalloproteinases and their inhibi-tors in tumor angiogenesis[J]. Int J Cancer, 2005, 115(6):849-860.
8. Kuno K, Bannai K, Hakozaki M, et al. The carboxyl-terminal half region of ADAMTS-1 suppresses both tumorigenicity and experimental tumor metastatic potential[J]. Biochem Biophys Res Commun, 2004, 319(4):1327-1333.
9. Kuno K, Okada Y, Kawashima H, et al. ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan[J]. FEBS Lett, 2000, 478(3):241-245.
10. Rocks N, Paulissen G, Quesada-Calvo F, et al. ADAMTS-1 metalloproteinase promotes tumor development through the induction of a stromal reaction in vivo[J]. Cancer Res, 2008, 68(22):9541-9550.
11. Luque A, Carpizo DR, Iruela-Arispe ML. ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165[J]. J Biol Chem, 2003, 278(26):23656-23665.
12. Vázquez F, Hastings G, Ortega MA, et al. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity[J]. J Biol Chem, 1999, 274(33):23349-23357.
13. Choi JE, Kim DS, Kim EJ, et al. Aberrant methylation of ADAM-TS1 in non-small cell lung cancer[J]. Cancer Genet Cytogenet, 2008, 187(2):80-84.
14. Masui T, Hosotani R, Tsuji S, et al. Expression of METH-1 and METH-2 in pancreatic cancer[J]. Clin Cancer Res, 2001, 7(11):3437-3443.
15. Gustavsson H, Wang W, Jennbacken K, et al. ADAMTS1, a putative anti-angiogenic factor, is decreased in human prostate cancer[J]. BJU Int, 2009, 104(11):1786-1790.
16. Lind GE, Kleivi K, Meling GI, et al. ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis[J]. Cell Oncol, 2006, 28(5-6):259-272.
17. Freitas VM, do Amaral JB, Silva TA, et al. Decreased expression of ADAMTS-1 in human breast tumors stimulates migration and invasion[J]. Mol Cancer, 2013, 12:2.
18. Liu YJ, Xu Y, Yu Q. Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro-and antimetastatic activity, respectively[J]. Oncogene, 2006, 25(17):2452-2467.
19. Keightley MC, Sales KJ, Jabbour HN. PGF2α-F-prostanoid rece-ptor signalling via ADAMTS1 modulates epithelial cell invasion and endothelial cell function in endometrial cancer[J]. BMC Cancer, 2010, 10:488.
20. Lu X, Wang Q, Hu G, et al. ADAMTS1 and MMP1 proteolytically engage EGF-like ligands in an osteolytic signaling cascade for bone metastasis[J]. Genes Dev, 2009, 23(16):1882-1894.
21. 陳靜, 戴冬秋, 支宇, 等.胃癌和轉移淋巴結組織ADAMTS1表達及其生物學意義的探討[J].中華腫瘤防治雜志, 2012, 19(1):53-56.
22. Chu D, Zhao Z, Zhou Y, et al. Matrix metalloproteinase-9 is associated with relapse and prognosis of patients with colorectal cancer[J]. Ann Surg Oncol, 2012, 19(1):318-325.
23. 楊小玲, 何凌霄, 徐禹, 等. 169例結腸癌患者術后3年生存期影響因素分析[J].中國普外基礎與臨床雜志, 2012, 19(7):771-773.
24. Kirat HT, Ozturd E, Lavery IC, et al. The predictive value of preoperative carcinoembryonic antigen level in the prognosis of colon cancer[J]. Am J Surg, 2012, 204(4):447-452.
25. Porter S, Span PN, Sweep FC, et al. ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma[J]. Int J Cancer, 2006, 118(5):1241-1247.

CHINESE JOURNAL OF BASES AND CLINICS IN GENERAL SURGERY

Expression of ADAMTS1 in Colorectal Cancer Tissues and Its Correlation with Prognosis

Abstract Full text Figures/Tables Video References Cited by

Previous Article

Next Article

Format

Content