A Trypsin Inhibitor from Rambutan Seeds with Antitumor, Anti-HIV-1 Reverse Transcriptase, and Nitric Oxide-Inducing Properties

Applied Biochemistry and Biotechnology

Volumn 175, Issue 8, 2015, Pages 3828-3839

  Fang, Evandro Fei ^a,b   Ng, Tzi Bun ^a  

^a and Hong Kong Branch of CAS Center for Excellence in Animal Evolution and Genetics   (Hong Kong)

^b NATIONAL INSTITUTE ON AGING   (United States)

Author keywords

Antitumor; Liquid chromatography; Nephelium lappaceum L; Nitric oxide; Protease inhibitor; Rambutan

Indexed keywords

CHEMICAL COMPOUNDS; CHROMATOGRAPHY; COVALENT BONDS; LIQUID CHROMATOGRAPHY; LIQUIDS; MONOTERPENES; NITRIC OXIDE; TUMORS; VOLATILE ORGANIC COMPOUNDS;

ANTI-TUMORS; HIV-1 REVERSE TRANSCRIPTASE; NEPHELIUM LAPPACEUM; NEPHELIUM LAPPACEUM L; PROTEASE INHIBITOR; PROTEOLYTIC ACTIVITIES; RAMBUTAN; TRYPSIN INHIBITORY ACTIVITY;

ENZYME INHIBITION;

ANTINEOPLASTIC AGENT; NITRIC OXIDE; REVERSE TRANSCRIPTASE, HUMAN IMMUNODEFICIENCY VIRUS 1; RNA DIRECTED DNA POLYMERASE; TRYPSIN; TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; CELL PROLIFERATION; CHEMISTRY; DRUG EFFECTS; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; PLANT SEED; SAPINDACEAE;

AMINO ACID SEQUENCE; ANTINEOPLASTIC AGENTS, PHYTOGENIC; CELL PROLIFERATION; HIV REVERSE TRANSCRIPTASE; HUMANS; NITRIC OXIDE; SAPINDACEAE; SEEDS; TRYPSIN; TRYPSIN INHIBITORS;

EID: 84939985436     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-015-1550-1     Document Type: Article

References (39)

1. Peter, G., Tornai-Lehoczki, J., Dlauchy, D., & Vitanyi, G. (2000). Pichia sporocuriosa sp. nov., a new yeast isolated from rambutan. Antonie Van Leeuwenhoek, 77, 37–42.
2. Ragasa, C. Y., de Luna, R. D., Cruz, W. C., Jr., & Rideout, J. A. (2005). Monoterpene lactones from the seeds of Nephelium lappaceum. Journal of Natural Products, 68, 1394–1396.
3. Nawawi, A., Nakamura, N., Hattori, M., Kurokawa, M., & Shiraki, K. (1999). Inhibitory effects of Indonesian medicinal plants on the infection of herpes simplex virus type 1. Phytotherapy Research, 13, 37–41.
4. Roongpisuthipong, C., Banphotkasem, S., Komindr, S., & Tanphaichitr, V. (1991). Postprandial glucose and insulin responses to various tropical fruits of equivalent carbohydrate content in non-insulin-dependent diabetes mellitus. Diabetes Research and Clinical Practice, 14, 123–131.
5. Kelso, J. M., Jones, R. T., & Yunginger, J. W. (1998). Anaphylaxis after initial ingestion of rambutan, a tropical fruit. Journal of Allergy and Clinical Immunology, 102, 145–146.
6. Nishizawa, M., Adachi, K., Sastrapradja, S., & Hayashi, Y. (1983). Isolation of individual type II cyanolipids from Nephelium lappaceum [Extraction of powdered seeds]. Phytochemistry, 22, 2853–2855.
7. Bullangpoti, V., Visetson, S., Milne, J., & Pornbanlualap, S. (2004). Effects of mangosteen’s peels and rambutan’s seeds on toxicity, esterase and glutathione-S-transferase in rice weevil (Sitophilus oryzae L.). Natural Science, 38, 84–89.
8. Khonkarn, R., Okonogi, S., Ampasavate, C., & Anuchapreeda, S. (2010). Investigation of fruit peel extracts as sources for compounds with antioxidant and antiproliferative activities against human cell lines. Food and Chemical Toxicology, 48, 2122–2129.
9. Lasekan, O., & Abbas, K. A. (2012). Distinctive exotic flavor and aroma compounds of some exotic tropical fruits and berries: a review. Critical Reviews in Food Science and Nutrition, 52, 726–735.
10. Ong, P. K., Acree, T. E., & Lavin, E. H. (1998). Characterization of volatiles in rambutan fruit (Nephelium lappaceum L.). Journal of Agricultural and Food Chemistry, 46, 611–615.
11. Sonwai, S., & Ponprachanuvut, P. (2012). Characterization of physicochemical and thermal properties and crystallization behavior of krabok (Irvingia Malayana) and rambutan seed fats. Journal of Oleo Science, 61, 671–679.
12. Sun, L., Zhang, H., & Zhuang, Y. (2012). Preparation of free, soluble conjugate, and insoluble-bound phenolic compounds from peels of rambutan (Nephelium lappaceum) and evaluation of antioxidant activities in vitro. Journal of Food Science, 77, C198–204.
13. Thitilertdecha, N., Teerawutgulrag, A., Kilburn, J. D., & Rakariyatham, N. (2010). Identification of major phenolic compounds from Nephelium lappaceum L. and their antioxidant activities. Molecules, 15, 1453–1465.
14. Jirapongsananuruk, O., Jirarattanasopa, N., Pongpruksa, S., Vichyanond, P., & Piboonpocanun, S. (2011). Glyceraldehyde-3-phosphate dehydrogenase as a major allergen in rambutan-induced anaphylaxis. Annals of Allergy, Asthma, and Immunology, 106, 545–547.
15. Sun, J., Su, W., Peng, H., Zhu, J., Xu, L., & Bruna, N. M. (2010). Two endogenous substrates for polyphenoloxidase in pericarp tissues of postharvest rambutan fruit. Journal of Food Science, 75, C473–477.
16. Southan, C. (2001). A genomic perspective on human proteases. FEBS Letters, 498, 214–218.
17. Laskowski, M., & Qasim, M. A. (2000). What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes? Biochimica et Biophysica Acta, 1477, 324–337.
18. Losso, J. N. (2008). The biochemical and functional food properties of the Bowman-Birk inhibitor. Critical Reviews in Food Science and Nutrition, 48, 94–118.
19. Fang, E. F., Hassanien, A. A., Wong, J. H., Bah, C. S., Soliman, S. S., & Ng, T. B. (2010). Purification and modes of antifungal action by Vicia faba cv. Egypt trypsin inhibitor. Journal of Agricultural and Food Chemistry, 58, 10729–10735.
20. Fang, E. F., Wong, J. H., Bah, C. S., Lin, P., Tsao, S. W., & Ng, T. B. (2010). Bauhinia variegata var. variegata trypsin inhibitor: from isolation to potential medicinal applications. Biochemical and Biophysical Research Communications, 396, 806–811.
21. Fang, E. F., Wong, J. H., & Ng, T. B. (2010). Thermostable Kunitz trypsin inhibitor with cytokine inducing, antitumor and HIV-1 reverse transcriptase inhibitory activities from Korean large black soybeans. Journal of Bioscience and Bioengineering, 109, 211–217.
22. Nielsen, T. B., & Reynolds, J. A. (1978). Measurements of molecular weights by gel electrophoresis. Methods in Enzymology, 48, 3–10.
23. Fang, E. F., Pan, W. L., Wong, J. H., Chan, Y. S., Ye, X. J., & Ng, T. B. (2011). A new Phaseolus vulgaris lectin induces selective toxicity on human liver carcinoma Hep G2 cells. Archives of Toxicology, 85, 1551–1563.
24. Wong, J. H., Wong, C. C., & Ng, T. B. (2006). Purification and characterization of a galactose-specific lectin with mitogenic activity from pinto beans. Biochimica et Biophysica Acta, 1760, 808–813.
25. Bah, C. S., Fang, E. F., Ng, T. B., Mros, S., McConnell, M., & Bekhit, A.-D. (2011). Purification and characterization of a rhamnose-binding chinook salmon roe lectin with antiproliferative activity toward tumor cells and nitric oxide-inducing activity toward murine macrophages. Journal of Agricultural and Food Chemistry, 59, 5720–5728.
26. Fang, E. F., Lin, P., Wong, J. H., Tsao, S. W., & Ng, T. B. (2010). A lectin with anti-HIV-1 reverse transcriptase, antitumor, and nitric oxide inducing activities from seeds of Phaseolus vulgaris cv. extralong autumn purple bean. Journal of Agricultural and Food Chemistry, 58, 2221–2229.
27. Odei-Addo, F., Frost, C., Smith, N., Ogawa, T., Muramoto, K., Oliva, M. L., Graf, L., & Naude, R. (2014). Biochemical characterization of Acacia schweinfurthii serine proteinase inhibitor. Journal of Enzyme Inhibition and Medicinal Chemistry, 29, 633–638.
28. Richardson, M. (Ed.). (1991). Seed storage proteins: the enzyme inhibitors. New York: Academic.
29. Bao, R., Zhou, C. Z., Jiang, C., Lin, S. X., Chi, C. W., & Chen, Y. (2009). The ternary structure of the double-headed arrowhead protease inhibitor API-A complexed with two trypsins reveals a novel reactive site conformation. Journal of Biological Chemistry, 284, 26676–26684.
30. Fang, E. F., Bah, C. S., Wong, J. H., Pan, W. L., Chan, Y. S., Ye, X. J., & Ng, T. B. (2012). A potential human hepatocellular carcinoma inhibitor from Bauhinia purpurea L. seeds: from purification to mechanism exploration. Archives of Toxicology, 86, 293–304.
31. Wang, K. J., Takahata, Y., Kono, Y., & Kaizuma, N. (2008). Allelic differentiation of Kunitz trypsin inhibitor in wild soybean (Glycine soja). Theoretical and Applied Genetics, 117, 565–573.
32. Bangsberg, D. R., Hecht, F. M., Charlebois, E. D., Zolopa, A. R., Holodniy, M., Sheiner, L., Bamberger, J. D., Chesney, M. A., & Moss, A. (2000). Adherence to protease inhibitors, HIV-1 viral load, and development of drug resistance in an indigent population. AIDS, 14, 357–366.
33. Law, C. K., & Mang, O. (2007). Cancer incidence in Hong Kong. Medical Bulletin, 12, 18–21.
34. Dia, V. P., Berhow, M. A., & Gonzalez De Mejia, E. (2008). Bowman-Birk inhibitor and genistein among soy compounds that synergistically inhibit nitric oxide and prostaglandin E2 pathways in lipopolysaccharide-induced macrophages. Journal of Agricultural and Food Chemistry, 56, 11707–11717.
35. Huang, G. J., Sheu, M. J., Chen, H. J., Chang, Y. S., & Lin, Y. H. (2007). Inhibition of reactive nitrogen species in vitro and ex vivo by trypsin inhibitor from sweet potato ‘Tainong 57’ storage roots. Journal of Agricultural and Food Chemistry, 55, 6000–6006.
36. Inoue, K., Takano, H., Yanagisawa, R., Sakurai, M., Shimada, A., Sato, H., Kato, Y., & Yoshikawa, T. (2005). Antioxidative role of urinary trypsin inhibitor in acute lung injury induced by lipopolysaccharide. International Journal of Molecular Medicine, 16, 1029–1033.
37. Nakatsuka, M., Asagiri, K., Noguchi, S., Habara, T., & Kudo, T. (2000). Nafamostat mesilate, a serine protease inhibitor, suppresses lipopolysaccharide-induced nitric oxide synthesis and apoptosis in cultured human trophoblasts. Life Sciences, 67, 1243–1250.
38. Venturini, G., Colasanti, M., & Ascenzi, P. (1998). Aprotinin, the first competitive protein inhibitor of NOS activity. Biochemical and Biophysical Research Communications, 249, 263–265.
39. Chuang, M. T., Lin, Y. S., & Hou, W. C. (2007). Ancordin, the major rhizome protein of madeira-vine, with trypsin inhibitory and stimulatory activities in nitric oxide productions. Peptides, 28, 1311–1316.