Expression of MMP2 and MMP9 (Gelatinases A and B) in Human Colon Cancer Cells

被引：33
|
作者：
Damodharan, Umadevi [1 ]
Ganesan, Ravikumar [2 ]
Radhakrishnan, Uma C. [2 ]
机构：
[1] Karpagam Arts & Sci Coll, Dept Biochem, Coimbatore 641029, Tamil Nadu, India
[2] Karpagam Univ, Dept Biochem, Coimbatore 641029, Tamil Nadu, India
来源：
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2011年 / 165卷 / 5-6期
关键词：
Matrix metalloproteinase; Colon cancer; Emodin; Sodium nitroprusside; Nitric oxide; ANTHRAQUINONES; EMODIN;
D O I：
10.1007/s12010-011-9342-8
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Matrix metalloproteinases (MMPs) are a family of zinc-dependent neutral endopeptidases, collectively capable of degrading essentially all matrix components. Elevated levels of distinct MMPs are detected in tumor tissue or serum of patients with advanced cancer, and they are the major prognostic indicators in cancer. Inhibition of MMPs has been explored as a therapeutic goal for almost two decades. Nitric oxide (NO), a free radical plays an important role in signaling pathways in regulation of MMP expression. In the present study, we demonstrated the role of exogenous NO levels in the regulation of MMP2 and MMP9 (gelatinases A and B) in colon cancer cell line WiDr and its inhibition with emodin (a naturally occurring anthraquinone).
引用
收藏
页码：1245 / 1252
页数：8
相关论文
共 50 条
  • [21] Nectin-3 is a new biomarker that mediates the upregulation of MMP2 and MMP9 in ovarian cancer cells
    Xu, Feixue
    Si, Xiaoqiang
    Wang, Jing
    Yang, Aihong
    Qin, Tiansheng
    Yang, Yongxiu
    BIOMEDICINE & PHARMACOTHERAPY, 2019, 110 : 139 - 144
  • [22] EXPRESSION OF GELATINASES (MMP-2, MMP-9) IN HUMAN ARTICULAR CARTILAGE
    Lipari, L.
    Gerbino, A.
    INTERNATIONAL JOURNAL OF IMMUNOPATHOLOGY AND PHARMACOLOGY, 2013, 26 (03) : 817 - 823
  • [23] Rab40b regulates trafficking of MMP2 and MMP9 during invadopodia formation and invasion of breast cancer cells
    Jacob, Abitha
    Jing, Jian
    Lee, James
    Schedin, Pepper
    Gilbert, Simon M.
    Peden, Andrew A.
    Junutula, Jagath R.
    Prekeris, Rytis
    JOURNAL OF CELL SCIENCE, 2013, 126 (20) : 4647 - 4658
  • [24] Regulation of MMP2 and MMP9 metalloproteinases by FSH and growth factors in bovine granulosa cells
    Portela, Valerio M.
    Veiga, Angela
    Price, Christopher A.
    GENETICS AND MOLECULAR BIOLOGY, 2009, 32 (03) : 516 - 520
  • [25] Immunolocalization of MMP9 and MMP2 in osteolytic metastasis originating from MDA-MB-231 human breast cancer cells
    Liu, Bo
    Cui, Jian
    Sun, Jing
    Li, Juan
    Han, Xiuchun
    Guo, Jie
    Yi, Min
    Amizuka, Norio
    Xu, Xin
    Li, Minqi
    MOLECULAR MEDICINE REPORTS, 2016, 14 (02) : 1099 - 1106
  • [26] THE EXPRESSION LEVELS OF MMP2, MMP9 IN EXPRESSED PROSTATIC SECRETIONS AS A DISCRIMINATORY MARKER BETWEEN PROSTATE CANCER AND INFLAMMATION
    Hidas, Guy
    Benjamin, Nisman
    Gofrit, Ofer N.
    Yutkin, Vladimir
    Duvdevani, Mordechai
    Pode, Dov
    JOURNAL OF UROLOGY, 2009, 181 (04): : 658 - 658
  • [27] Clinical characteristics of TIMP2, MMP2, and MMP9 gene polymorphisms in colorectal cancer
    Park, Kyung Sook
    Kim, Seon Jeong
    Kim, Kyung Ho
    Kim, Jin Cheon
    JOURNAL OF GASTROENTEROLOGY AND HEPATOLOGY, 2011, 26 (02) : 391 - 397
  • [28] Differential regulation of MMP2 and MMP9 activity by stretch in the arterial wall
    Lehoux, S
    Mallat, Z
    Esposito, B
    Merval, R
    Tedgui, A
    HYPERTENSION, 1998, 32 (04) : 789 - 789
  • [29] Fetal MMP2/MMP9 polymorphisms and intrauterine growth restriction risk
    Gremlich, Sandrine
    Nguyen, Daniel
    Reymondin, Danielle
    Hohlfeld, Patrick
    Vial, Yvan
    Witkin, Steven S.
    Gerber, Stefan
    JOURNAL OF REPRODUCTIVE IMMUNOLOGY, 2007, 74 (1-2) : 143 - 151
  • [30] Evidence that reduced glutathione (GSH) is a potent inhibitor of gelatinases MMP2 and MMP9 at its normal concentrations in extracellular fluid (ECF).
    Upadhya, GA
    Strasberg, SM
    HEPATOLOGY, 1999, 30 (04) : 311A - 311A
12345