Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
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Antiproliferative Activity of Lavatera cashmeriana- Protease Inhibitors towards Human Cancer Cells

  • Rakashanda, Syed (Department of Biochemistry, University of Kashmir) ;
  • Qazi, Asif Khurshid (Cancer Pharmacology Division, CSIR Indian Institute of Integrative Medicine) ;
  • Majeed, Rabiya (Cancer Pharmacology Division, CSIR Indian Institute of Integrative Medicine) ;
  • Rafiq, Shaista (Department of Biochemistry, University of Kashmir) ;
  • Dar, Ishaq Mohammad (Department of Biochemistry, University of Kashmir) ;
  • Masood, Akbar (Department of Biochemistry, University of Kashmir) ;
  • Hamid, Abid (Cancer Pharmacology Division, CSIR Indian Institute of Integrative Medicine) ;
  • Amin, Shajrul (Department of Biochemistry, University of Kashmir)
  • Published : 2013.06.30
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Abstract

Background: Proteases play a regulatory role in a variety of pathologies including cancer, pancreatitis, thromboembolic disorders, viral infections and many others. One of the possible strategies to combat these pathologies seems to be the use of protease inhibitors. LC-pi I, II, III and IV (Lavatera cashmerian-protease inhibitors) have been found in vitro to strongly inhibit trypsin, chymotrypsin and elastase, proteases contributing to tumour invasion and metastasis, indicated possible anticancer effects. The purpose of this study was to check in vitro anticancer activity of these four inhibitors on human lung cancer cell lines. Material and Methods: In order to assess whether these inhibitors induced in vitro cytoxicity, SRB assay was conducted with THP-1 (leukemia), NCIH322 (lung) and Colo205, HCT-116 (colon) lines. Results: LC-pi I significantly inhibited the cell proliferation of all cells tested and also LC-pi II was active in all except HCT-116. Inhibition of cell growth by LC-pi III and IV was negligible. $IC_{50}$ values of LC-pi I and II for NCIH322, were less compared to other cell lines suggesting that lung cancer cells are more inhibited. Conclusion: These investigations might point to future preventive as well as curative solutions using plant protease inhibitors for various cancers, especially in the lung, hence warranting their further investigation.

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References

  1. Akizuki M, Fukutomi T, Takasugi M, et al (2007). Prognostic significance of immunoreactive neutrophil elastase in human breast cancer: long-term follow-up results in 313 patients. Neoplasia, 9, 260-264. https://doi.org/10.1593/neo.06808
  2. Barrett AJ (1981). Leukocyte elastase. Methods Enzymol, 80, 581-88. https://doi.org/10.1016/S0076-6879(81)80046-8
  3. Clemente A, Marin-Manzano CM, Jimenez E, et al (2012). The anti-proliferative effect of TI1B, a major Bowman-Birk isoinhibitor from pea (Pisum sativum L.), on HT29 colon cancer cells is mediated through protease inhibition. Br J Nutr, 108, 135-44. https://doi.org/10.1017/S000711451200075X
  4. Clemente A, Moreno FJ, Marin-Manzano CM, et al (2010). The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases. Mol Nutr Food Res, 54, 396-405. https://doi.org/10.1002/mnfr.200900122
  5. de Mejia EG and Dia VP (2010). The role of neutraceutical proteins and peptides in apoptosis, angiogenesis and metastasis of cancer cells. Cancer Metastasis Rev, 29, 511-28. https://doi.org/10.1007/s10555-010-9241-4
  6. Foekens JA, Ries C, Look MP, et al (2003). The prognostic value of polymorphonuclear leukocyte elastase in patients with primary breast cancer. Cancer Res, 63, 337-41.
  7. Hossain, MS, Azad AK, Sayem SM, et al (2007). Production and partial characterization of feather-degrading keratinolytic serine protease from Bacillus licheniformis MZK-3. J Boil Sci, 7, 599-606. https://doi.org/10.3923/jbs.2007.599.606
  8. Houghton P, Fang R, Techatanawat I, et al (2007). The sulphorhodamine (SRB) assay and other approaches to testing plant extracts and derived compounds for activities related to reputed anticancer activity. Methods, 42, 377-87 https://doi.org/10.1016/j.ymeth.2007.01.003
  9. Hunt KK, Wingate H, Yokota T, et al (2013). Elafin, an inhibitor of elastase, is a prognostic indicator in breast cancer. Breast Cancer Research, 15.
  10. Jedina KA, and Maliar T (2005). Inhibitors of proteases as anticancer drugs. Neoplasma, 52, 185-192.
  11. Kaul MK (1997). Medicinal plants of Kashmir and Ladakh: Temperate and cold Arid Himalya" Indus Publishing, India 24.
  12. Khan H, Subhan M, Mehmood S, et al (2008). Purification and characterization of serine protease from seeds of Holarrhena antidysenterica . Biotechnology, 7, 94-99. https://doi.org/10.3923/biotech.2008.94.99
  13. Mageea PJ, Owusu-Apentena R, McCannb MJ, et al (2012). Chickpea (Cicer arietinum) and Other Plant-Derived Protease Inhibitor Concentrates Inhibit Breast and Prostate Cancer Cell Proliferation In vitro. Nutrition and Cancer, 64, 741-48 https://doi.org/10.1080/01635581.2012.688914
  14. Matej R, Mandakova P, Netikova I, et al (2007). Proteinase-Activated Receptor-2 Expression in Breast Cancer and the Role of Trypsin on Growth and Metabolism of Breast Cancer Cell Line MDA MB-231. Physiol Res, 56, 475-84.
  15. Mittendorf EA (2012). Cellular Uptake of Neutrohpil Elastase Links Inflammation to Adaptive Immunity. UT GSBS Dissertations and Theses (Open Access), 303.
  16. Nyberg P, Moilanen M, Paju A, et al (2002). MMP-9 Activation by Tumor Trypsin-2 Enhances in vivo Invasion of Human Tongue Carcinoma Cells. J Dent Res, 81, 831-35. https://doi.org/10.1177/154405910208101207
  17. Nyberg P, Ylipalosaari M, Sorsa T, Sal T (2006). Trypsin and their role in carcinoma growth. Exp Cell Res, 312, 1219-28. https://doi.org/10.1016/j.yexcr.2005.12.024
  18. Queen MM, Ryan RE, Holzer RG, et al (2005). Breast cancer cells stimulate neutrophils to produce oncostatin M: potential implications for tumor progression. Cancer Res, 65, 8896-904 https://doi.org/10.1158/0008-5472.CAN-05-1734
  19. Quemener C, Gabison EE, Naimi B et al (2007) Extracellular matrix metalloproteinase inducer up-regulates the urokinasetype plasminogen activator system promoting tumor cell invasion. Cancer Res, 67, 9-15. https://doi.org/10.1158/0008-5472.CAN-06-2448
  20. Rakashanda S, Ishaq M, Masood A, Amin S (2012). Antibacterial activity of a Trypsin-chymotrypsin-elastase inhibitor isolated from Lavatera cashmeriana camb. seeds. J Animal & Plant Sci, 22, 983-6.
  21. Rakashanda S, Mubashir S, Qureshi Y, et al (2013). Trypsin inhibitors from Lavatera cashmeriana camb. seeds: isolation, characterization and in-vitro cytoxic activity. Int J Pharmaceutical Science Invention, 2, 55-65.
  22. Ramachandran R, Noorbakhsh F, Defea K, Hollenberg MD (2012). Targeting proteinase-activated receptors: therapeutic potential and challenges. Nat Rev Drug Discov, 11, 69-86. https://doi.org/10.1038/nrd3615
  23. Rawlings ND, Morton FR and Barrett AJ (2006). MEROPS: the peptidase database. Nucleic Acids Res, 34, 270-2. https://doi.org/10.1093/nar/gkj089
  24. Soreide K, Janssen EA, Korner H, Baak JPA (2006). Trypsin in colorectal cancer: molecular biological mechanisms of proliferation, invasion and metastasis. J Pathol, 209, 145-56.
  25. Tochi BN, Wang Z, Xu SY and Zhang W (2008). Therapeutic application of pineapple protease (bromelain): A review. Pak J Nutr, 7, 513-20. https://doi.org/10.3923/pjn.2008.513.520
  26. Uchima Y, Sawada T, Nishihara T, et al (2003). Identification of a trypsinogen activity stimulating factor produced by pancreatic cancer cells: its role in tumor invasion and metastasis. Int J Mol Med, 12, 871-78.
  27. Yamamoto H, Ikv S, Adachi Y, et al (2003). Association of trypsin expression with tumor progression and matrilysin expression in human colorectal cancer. J Pathol, 199, 176-84. https://doi.org/10.1002/path.1277
  28. Ye XJ, Ng TB (2011). Antitumor and HIV-1 Reverse Transcriptase Inhibitory Activities of a Hemagglutinin and a Protease Inhibitor from Mini-Black Soybean. Evidence-Based Complementary and Alternative Medicine, 1-12.

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