Skip to main content
SpringerLink
Log in

Polyozellin blocks tumor necrosis factor α-induced interleukin 8 and matrix metalloproteinase 7 production in the human intestinal epithelial cell line HT-29

  • Drug Actions
  • Published:
Archives of Pharmacal Research Aims and scope Submit manuscript

Abstract

Polyozellin isolated from Polyozellus multiplex (Thelephoraceae) displays potent anti-inflammatory effects in murine macrophages. Here we evaluated whether polyozellin has the potential to ameliorate diseases characterized by mucosal inflammation in intestinal epithelial HT-29 cells. Polyozellin significantly inhibited tumor necrosis factor (TNF)-α-induced interleukin-8 secretion and mRNA expression. Moreover, polyozellin suppressed the expression of matrix metalloproteinase-7 mRNA and extracellular pro-matrix metalloproteinase-7 secretion. A signal transduction study revealed that polyozellin significantly attenuates TNF-α-mediated p38 phosphorylation, inhibitory factor κBα degradation, and nuclear factor-κB-mediated transcriptional activation. Collectively, these results suggest that polyozellin has the potential to attenuate intestinal inflammation and shed light on the novel signal pathway evoked by TNF-α during intestinal inflammation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Subscribe and save

Springer+ Basic
$34.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or eBook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Baeuerle, P. A. and Baltimore, D., NF-kappa B: Ten years after. Cell, 87, 13–20 (1996).

    Article  PubMed  CAS  Google Scholar 

  • Bister, V., Salmela, M. T., Heikkilä, P., Anttila, A., Rintala, R., Isaka, K., Andersson, S., and Saarialho-Kere, U., Matrilysins-1 and -2 (MMP-7 and -26) and metalloelastase (MMP-12), unlike MMP-19, are up-regulated in necrotizing enterocolitis. J. Pediatr. Gastroenterol. Nutr., 40, 60–66 (2005).

    Article  PubMed  CAS  Google Scholar 

  • Bodger, K. and Crabtree, J. E., Helicobacter pylori and gastric inflammation. Br. Med. Bull., 54, 139–150 (1998).

    PubMed  CAS  Google Scholar 

  • Brinckerhoff, C. E. and Matrisian, L. M., Matrix metalloproteinases: a tail of a frog that became a prince. Nat. Rev. Mol. Cell Biol., 3, 207–214 (2002).

    Article  PubMed  CAS  Google Scholar 

  • Castaneda, F. E., Walia, B., Vijay-Kumar, M., Patel, N. R., Roser, S., Kolachala, V. L., Rojas, M., Wang, L., Oprea, G., Garg, P., Gewirtz, A. T., Roman, J., Merlin, D., and Sitaraman, S. V., Targeted deletion of metalloproteinase 9 attenuates experimental colitis in mice: central role of epithelial-derived MMP. Gastroenterology, 129, 1991–2008 (2005).

    Article  PubMed  CAS  Google Scholar 

  • Coëffier, M., Marion, R., Ducrotté, P., and Déchelotte, P., Modulating effect of glutamine on IL-1beta-induced cytokine production by human gut. Clin. Nutr., 22, 407–413 (2003).

    Article  PubMed  Google Scholar 

  • Farrell, R. J. and Peppercorn, M. A., Ulcerative colitis. Lancet, 359, 331–340 (2002).

    Article  PubMed  Google Scholar 

  • Finlay, B. B. and Falkow, S., Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev., 61, 136–169 (1997).

    PubMed  CAS  Google Scholar 

  • Fiocchi, C., Inflammatory bowel disease: etiology and pathogenesis. Gastroenterology, 115, 182–205 (1998).

    Article  PubMed  CAS  Google Scholar 

  • Fiocchi, C., Inflammatory bowel disease. Current concepts of pathogenesis and implications for therapy. Minerva Gastroenterol. Dietol., 48, 215–226 (2002).

    PubMed  CAS  Google Scholar 

  • Gao, Q., Meijer, M. J., Kubben, F. J., Sier, C. F., Kruidenier, L., van Duijn, W., van den Berg, M., van Hogezand, R. A., Lamers, C. B., and Verspaget, H. W., Expression of matrix metalloproteinases-2 and -9 in intestinal tissue of patients with inflammatory bowel diseases. Dig. Liver Dis., 37, 584–592 (2005).

    Article  PubMed  CAS  Google Scholar 

  • Gerard, C. and Rollins, B. J., Chemokines and disease. Nat. Immunol., 2, 108–115 (2001).

    Article  PubMed  CAS  Google Scholar 

  • Gijsbers, K., Van Assche, G., Joossens, S., Struyf, S., Proost, P., Rutgeerts, P., Geboes, K., and Van Damme, J., CXCR1-binding chemokines in inflammatory bowel diseases: down-regulated IL-8/CXCL8 production by leukocytes in Crohn’s disease and selective GCP-2/CXCL6 expression in inflamed intestinal tissue. Eur. J. Immunol., 34, 1992–2000 (2004).

    Article  PubMed  CAS  Google Scholar 

  • Grund, E. M., Kagan, D., Tran, C. A., Zeitvogel, A., Starzinski-Powitz, A., Nataraja, S., and Palmer, S. S., Tumor necrosis factor-alpha regulates inflammatory and mesenchymal responses via mitogen-activated protein kinase kinase, p38, and nuclear factor kappaB in human endometriotic epithelial cells. Mol. Pharmacol., 73, 1394–1404 (2008).

    Article  PubMed  CAS  Google Scholar 

  • Hobbie, S., Chen, L. M., Davis, R. J., and Galán, J. E., Involvement of mitogen-activated protein kinase pathways in the nuclear responses and cytokine production induced by Salmonella typhimurium in cultured intestinal epithelial cells. J. Immunol., 159, 5550–5559 (1997).

    PubMed  CAS  Google Scholar 

  • Hwang, J. S., Song, K. S., Kim, W. G., Lee, T. H., Koshino, H., and Yoo, I. D., Polyozellin, a new inhibitor of prolyl endopeptidase from Polyozellus multiplex. J. Antibiot., 50, 773–777 (1997).

    PubMed  CAS  Google Scholar 

  • Jijon, H. B., Panenka, W. J., Madsen, K. L., and Parsons, H. G., MAP kinases contribute to IL-8 secretion by intestinal epithelial cells via a posttranscriptional mechanism. Am. J. Physiol. Cell Physiol., 283, C31–C41 (2002).

    PubMed  CAS  Google Scholar 

  • Jin, X. Y., Lee, S. H., Kim, J. Y., Zhao, Y. Z., Park, E. J., Lee, B. S., Nan, J. X., Song, K. S., Ko, G., and Sohn, D. H., Polyozellin inhibits nitric oxide production by down-regulating LPS-induced activity of NF-kappaB and SAPK/JNK in RAW 264.7 cells. Planta Med., 72, 857–859 (2006).

    Article  PubMed  CAS  Google Scholar 

  • Jobin, C. and Sartor, R. B., The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection. Am. J. Physiol. Cell Physiol., 278, C451–C462 (2000).

    PubMed  CAS  Google Scholar 

  • Kim, J. H., Lee, J. S., Song, K. S., Kwon, C. S., Kim, Y. K., and Kim, J. S., Polyozellin isolated from Polyozellus multiplex induces phase 2 enzymes in mouse hepatoma cells and differentiation in human myeloid leukaemic cell lines. J. Agric. Food Chem., 52, 451–455 (2004).

    Article  PubMed  CAS  Google Scholar 

  • Lang, A., Lahav, M., Sakhnini, E., Barshack, I., Fidder, H. H., Avidan, B., Bardan, E., Hershkoviz, R., Bar-Meir, S., and Chowers, Y., Allicin inhibits spontaneous and TNFalpha induced secretion of proinflammatory cytokines and chemokines from intestinal epithelial cells. Clin. Nutr., 23, 1199–1208 (2004).

    Article  PubMed  CAS  Google Scholar 

  • Lee, S. H., Seo, G. S., Jin, X. Y., Ko, G., and Sohn, D. H., Butein blocks tumor necrosis factor alpha-induced interleukin 8 and matrix metalloproteinase 7 production by inhibiting p38 kinase and osteopontin mediated signaling events in HT-29 cells. Life Sci., 81, 1535–1543 (2007).

    Article  PubMed  CAS  Google Scholar 

  • Loftus, E. V. Jr., Clinical epidemiology of inflammatory bowel disease: Incidence, prevalence, and environmental influences. Gastroenterology, 126, 1504–1517 (2004).

    Article  PubMed  Google Scholar 

  • MacGillivray, M. K., Cruz, T. F., and McCulloch, C. A., The recruitment of the interleukin-1 (IL-1) receptor-associated kinase (IRAK) into focal adhesion complexes is required for IL-1beta-induced ERK activation. J. Biol. Chem., 275, 23509–23515 (2000).

    Article  PubMed  CAS  Google Scholar 

  • Medina, C. and Radomski, M. W., Role of matrix metalloproteinases in intestinal inflammation. J. Pharmacol. Exp. Ther., 318, 933–938 (2006).

    Article  PubMed  CAS  Google Scholar 

  • Mott, J. D. and Werb, Z., Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol., 16, 558–564 (2004).

    Article  PubMed  CAS  Google Scholar 

  • Neurath, M. F., Finotto, S., and Glimcher, L. H., The role of Th1/Th2 polarization in mucosal immunity. Nat. Med., 8, 567–573 (2002).

    Article  PubMed  CAS  Google Scholar 

  • Salmela, M. T., MacDonald, T. T., Black, D., Irvine, B., Zhuma, T., Saarialho-Kere, U., and Pender, S. L., Upregulation of matrix metalloproteinases in a model of T cell mediated tissue injury in the gut: analysis by gene array and in situ hybridisation. Gut, 51, 540–547 (2002).

    Article  PubMed  CAS  Google Scholar 

  • Salmela, M. T., Pender, S. L., Karjalainen-Lindsberg, M. L., Puolakkainen, P., Macdonald, T. T., and Saarialho-Kere, U., Collagenase-1 (MMP-1), matrilysin-1 (MMP-7), and stromelysin-2 (MMP-10) are expressed by migrating enterocytes during intestinal wound healing. Scand. J. Gastroenterol., 39, 1095–1104 (2004).

    Article  PubMed  CAS  Google Scholar 

  • Schuppan, D. and Hahn, E. G., MMPs in the gut: inflammation hits the matrix. Gut, 47, 12–14 (2000).

    Article  PubMed  CAS  Google Scholar 

  • Seifert, W. F., Wobbes, T., and Hendriks, T., Divergent patterns of matrix metalloproteinase activity during wound healing in ileum and colon of rats. Gut, 39, 114–119 (1996).

    Article  PubMed  CAS  Google Scholar 

  • Sternlicht, M. D. and Werb, Z., How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol., 17, 463–516 (2001).

    Article  PubMed  CAS  Google Scholar 

  • Strober, W., Fuss, I. J., and Blumberg, R. S., The immunology of mucosal models of inflammation. Annu. Rev. Immunol., 20, 495–549 (2002).

    Article  PubMed  CAS  Google Scholar 

  • Von Lampe, B., Barthel, B., Coupland, S. E., Riecken, E. O., and Rosewicz, S., Differential expression of matrix metalloproteinases and their tissue inhibitors in colon mucosa of patients with inflammatory bowel disease. Gut, 47, 63–73 (2000).

    Article  Google Scholar 

  • Yu, Y. and Chadee, K., Prostaglandin E2 stimulates IL-8 gene expression in human colonic epithelial cells by a posttranscriptional mechanism. J. Immunol., 161, 3746–3752 (1998).

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Pharmaceutical Research and Development, College of Pharmacy, Wonkwang University, Iksan, Chonbuk, 570-749, Korea

    Sung Hee Lee & Dong Hwan Sohn

  2. School of Applied Biosciences, College of Agriculture and Life Sciences, Kyungpook National University, Daegu, 702-701, Korea

    Kyung-Sik Song

  3. Digestive Disease Research Institute, Wonkwang University School of Medicine, Iksan, 570-749, Korea

    Geom Seog Seo

Authors
  1. Sung Hee Lee
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Kyung-Sik Song
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Dong Hwan Sohn
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Geom Seog Seo
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Geom Seog Seo.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lee, S.H., Song, KS., Sohn, D.H. et al. Polyozellin blocks tumor necrosis factor α-induced interleukin 8 and matrix metalloproteinase 7 production in the human intestinal epithelial cell line HT-29. Arch. Pharm. Res. 34, 91–97 (2011). https://doi.org/10.1007/s12272-011-0111-6

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12272-011-0111-6

Key words

Search

Navigation