Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2015 Nov 26:5:16599.
doi: 10.1038/srep16599.

Clinicopathologic significance of legumain overexpression in cancer: a systematic review and meta-analysis

Ye Zhen  1 , Guo Chunlei  1 , Shen Wenzhi  1 , Zhao Shuangtao  1 , Luo Na  1 , Wang Rongrong  1 , Luo Xiaohe  1 , Niu Haiying  1 , Luo Dehong  1 , Jiang Shan  1 , Tan Xiaoyue  1 , Xiang Rong  1
Affiliations
Free PMC article
Review

Clinicopathologic significance of legumain overexpression in cancer: a systematic review and meta-analysis

Ye Zhen et al. Sci Rep. .
Free PMC article

Abstract

Since reports on the clinical significance of legumain in cancer have shown inconsistent results, we systematically evaluated clinical indicators of legumain in cancer. We searched the Cochrane Library, PubMed, Embase, and EBSCO databases and the Wangfang and CNKI databases in China by using "legumain" and ("neoplasms" OR "cancer") as search terms. We included case-controlled studies of legumain and cancer. The quality of the studies was evaluated by using Lichtenstein's guidelines, and valid data was extracted for analysis. In total, 10 articles were included in this study. Meta-analysis showed that legumain was overexpressed in cancer compared with in normal tissue and was higher in stage III-IV disease than in I-II disease. Moreover, legumain overexpression was correlated with poor prognosis and clinical stage. Furthermore, Cancer Genome Atlas data showed that among patients with rectal cancer, those with tumors overexpressing legumain had shorter overall survival than those in the low expression group (P < 0.05). Legumain appears to be involved in tumor development and deterioration; thus, it can potentially be developed into both a marker for monitoring and diagnosing tumors and a therapeutic target.

PubMed Disclaimer

Figures

Figure 1
Figure 1. Forest plot of risk ratios of legumain overexpression in cancer tissue vs normal tissue groups.
Figure 2
Figure 2. Forest plot of risk ratios of legumain overexpression in well-differentiated vs moderate–poorly differentiated tumor groups.
Figure 3
Figure 3. Forest plot of risk ratios of legumain overexpression in N0 vs N+ groups.
Figure 4
Figure 4. Forest plot of risk ratios of legumain overexpression in I–II vs III–IV groups.
Figure 5
Figure 5. Kaplan–Meier survival curve of TCGA data comparing high legumain expression group with low legumain expression group.
Figure 6
Figure 6. Funnel plot of risk ratios of legumain overexpression in cancer tissue vs normal tissue groups.
Figure 7
Figure 7. Funnel plot of risk ratios of legumain overexpression in well-differentiated vs moderate–poorly differentiated tumor groups.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Barrett A. & Rawlings N. Families and clans of cysteine peptidases. Perspectives in Drug Discovery and Design 6, 1–11 (1996).
    1. Chen J. M. et al. Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase. Journal of Biological Chemistry 272, 8090–8098 (1997). - PubMed
    1. Kembhavi A. A., Buttle D. J., Knight C. G. & Barrett A. J. The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays. Archives of biochemistry and biophysics 303, 208–213 (1993). - PubMed
    1. Liu C., Sun C., Huang H., Janda K. & Edgington T. Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy. Cancer research 63, 2957–2964 (2003). - PubMed
    1. Yamane T. et al. Legumain from bovine kidney: its purification, molecular cloning, immunohistochemical localization and degradation of annexin II and vitamin D-binding protein. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1596, 108–120 (2002). - PubMed

Substances

LinkOut - more resources