Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Cellular and Molecular Biology Letters

Online
ISSN
1689-1392
See all formats and pricing
More options …
Volume 13, Issue 3

Issues

siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis

Tharinee Susantad
  • Molecular Pathology Laboratory, Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, 25/25 Phuttamonthol Sai 4, Salaya, Nakorn Pathom, Thailand, 73170
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Duncan Smith
  • Molecular Pathology Laboratory, Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, 25/25 Phuttamonthol Sai 4, Salaya, Nakorn Pathom, Thailand, 73170
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-07-07 | DOI: https://doi.org/10.2478/s11658-008-0017-6

Abstract

The laminin-binding protein, variously called the 37/67-kDa high affinity laminin receptor or p40, mediates the attachment of normal cells to the laminin network, and also has a role as a ribosomal protein. Over-expression of this protein has been strongly correlated with the metastatic phenotype. However, few studies have investigated the cellular consequence of the ablation of this gene’s expression. To address this issue, the expression of the 37/67-kDa high affinity laminin receptor was knocked out with several siRNA constructs via RNA interference in transformed liver (Hep3B) cells. In each case where the message was specifically ablated, apoptosis was induced, as determined by annexin V/propidium iodide staining, and by double staining with annexin V and an antibody directed against the 37/67-kDa high affinity laminin receptor. These results suggest that this protein plays a critical role in maintaining cell viability.

Keywords: siRNA; RNA interference; Laminin receptor; p40; Ribosomal; Liver; Silencing; LAMR1

  • [1] Lesot, H., Kuhl, U. and Mark, K.V. Isolation of a laminin-binding protein from muscle cell membranes. EMBO J. 2 (1983) 861–865. Google Scholar

  • [2] Malinoff, H.L. and Wicha, M.S. Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J. Cell Biol. 96 (1983) 1475–1479. http://dx.doi.org/10.1083/jcb.96.5.1475CrossrefGoogle Scholar

  • [3] Rao, N.C., Barsky, S.H., Terranova, V.P. and Liotta, L.A. Isolation of a tumor cell laminin receptor. Biochem. Biophys. Res. Commun. 111 (1983) 804–808. http://dx.doi.org/10.1016/0006-291X(83)91370-0CrossrefGoogle Scholar

  • [4] Rao, C.N., Castronovo, V., Schmitt, M.C., Wewer, U.M., Claysmith, A.P., Liotta, L.A. and Sobel, M.E. Evidence for a precursor of the high-affinity metastasis-associated murine laminin receptor. Biochemistry 28 (1989) 7476–7486. http://dx.doi.org/10.1021/bi00444a047CrossrefGoogle Scholar

  • [5] Yow, H.K., Wong, J.M., Chen, H.S., Lee, C.G., Davis, S., Steele, G.D., Jr. and Chen, L.B. Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein. Proc. Natl. Acad. Sci. USA 85 (1988) 6394–6398. http://dx.doi.org/10.1073/pnas.85.17.6394CrossrefGoogle Scholar

  • [6] Tohgo, A., Takasawa, S., Munakata, H., Yonekura, H., Hayashi, N. and Okamoto, H. Structural determination and characterization of a 40-kDa protein isolated from rat 40 S ribosomal subunit. FEBS Lett. 340 (1994) 133–138. http://dx.doi.org/10.1016/0014-5793(94)80188-6CrossrefGoogle Scholar

  • [7] Auth, D. and Brawerman, G. A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery. Proc. Natl. Acad. Sci. USA 89 (1992) 4368–4372. http://dx.doi.org/10.1073/pnas.89.10.4368CrossrefGoogle Scholar

  • [8] Sato, M., Kinoshita, K., Kaneda, Y., Saeki, Y., Iwamatsu, A. and Tanaka, K. Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40). Biochem. Biophys. Res. Commun. 229 (1996) 896–901. http://dx.doi.org/10.1006/bbrc.1996.1899CrossrefGoogle Scholar

  • [9] Mecham, R.P., Hinek, A., Griffin, G.L., Senior, R.M. and Liotta, L.A. The elastin receptor shows structural and functional similarities to the 67-kDa tumor cell laminin receptor. J. Biol. Chem. 264 (1989) 16652–16657. Google Scholar

  • [10] McCaffery, P., Neve, R.L. and Drager, U.C. A dorso-ventral asymmetry in the embryonic retina defined by protein conformation. Proc. Natl. Acad. Sci. USA 87 (1990) 8570–8574. http://dx.doi.org/10.1073/pnas.87.21.8570CrossrefGoogle Scholar

  • [11] Rieger, R., Edenhofer, F., Lasmezas, C.I. and Weiss, S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3 (1997) 1383–1388. http://dx.doi.org/10.1038/nm1297-1383CrossrefGoogle Scholar

  • [12] Gauczynski, S., Peyrin, J.M., Haik, S., Leucht, C., Hundt, C., Rieger, R., Krasemann, S., Deslys, J.P., Dormont, D., Lasmezas, C.I. and Weiss, S. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J. 20 (2001) 5863–5875. http://dx.doi.org/10.1093/emboj/20.21.5863CrossrefGoogle Scholar

  • [13] Gauczynski, S., Nikles, D., El-Gogo, S., Papy-Garcia, D., Rey, C., Alban, S., Barritault, D., Lasmezas, C.I. and Weiss, S. The 37-kDa/67-kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes. J. Infect. Dis. 194 (2006) 702–709. http://dx.doi.org/10.1086/505914CrossrefGoogle Scholar

  • [14] Ludewigs, H., Zuber, C., Vana, K., Nikles, D., Zerr, I. and Weiss, S. Therapeutic approaches for prion disorders. Expert Rev. Anti. Infect. Ther. 5 (2007) 613–630. http://dx.doi.org/10.1586/14787210.5.4.613CrossrefGoogle Scholar

  • [15] Vana, K., Zuber, C., Nikles, D. and Weiss, S. Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy. Cell. Mol. Neurobiol. 27 (2007)107–128. http://dx.doi.org/10.1007/s10571-006-9121-1Web of ScienceCrossrefGoogle Scholar

  • [16] Zuber, C., Ludewigs, H. and Weiss, S. Therapeutic approaches targeting the prion receptor LRP/LR. Vet. Microbiol. 123 (2007) 387–393. http://dx.doi.org/10.1016/j.vetmic.2007.04.005Web of ScienceCrossrefGoogle Scholar

  • [17] Wang, K.S., Kuhn, R.J., Strauss, E.G., Ou, S. and Strauss, J.H. High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J. Virol. 66 (1992) 4992–5001. Google Scholar

  • [18] Thepparit, C. and Smith, D.R. Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J. Virol. 78 (2004) 12647–12656. http://dx.doi.org/10.1128/JVI.78.22.12647-12656.2004CrossrefGoogle Scholar

  • [19] Akache, B., Grimm, D., Pandey, K., Yant, S.R., Xu, H. and Kay, M.A. The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9. J. Virol. 80 (2006) 9831–9836. http://dx.doi.org/10.1128/JVI.00878-06CrossrefGoogle Scholar

  • [20] Coggin, J.H. Jr., Barsoum, A.L. and Rohrer, J.W. 37 kiloDalton oncofetal antigen protein and immature laminin receptor protein are identical, universal T-cell inducing immunogens on primary rodent and human cancers. Anticancer Res. 19 (1999) 5535–5542. Google Scholar

  • [21] Zelle-Rieser, C., Barsoum, A.L., Sallusto, F., Ramoner, R., Rohrer, J.W., Holtl, L., Bartsch, G., Coggin, J.J. and Thurnher, M. Expression and immunogenicity of oncofetal antigen-immature laminin receptor in human renal cell carcinoma. J. Urol. 165 (2001) 1705–1709. http://dx.doi.org/10.1016/S0022-5347(05)66398-7CrossrefGoogle Scholar

  • [22] Castronovo, V. Laminin receptors and laminin-binding proteins during tumor invasion and metastasis. Invasion Metastasis 13 (1993) 1–30. Google Scholar

  • [23] Castronovo, V., Claysmith, A.P., Barker, K.T., Cioce, V., Krutzsch, H.C. and Sobel, M.E. (1991). Biosynthesis of the 67 kDa high affinity laminin receptor. Biochem. Biophys. Res. Commun. 177 (1991) 177–183. http://dx.doi.org/10.1016/0006-291X(91)91965-FCrossrefGoogle Scholar

  • [24] Buto, S., Tagliabue, E., Ardini, E., Magnifico, A., Ghirelli, C., van den Brule, F., Castronovo, V., Colnaghi, M.I., Sobel, M.E. and Menard, S. Formation of the 67-kDa laminin receptor by acylation of the precursor. J. Cell. Biochem. 69 (1998) 244–251. http://dx.doi.org/10.1002/(SICI)1097-4644(19980601)69:3<244::AID-JCB2>3.0.CO;2-RCrossrefGoogle Scholar

  • [25] Narumi, K., Inoue, A., Tanaka, M., Isemura, M., Shimo-Oka, T., Abe, T., Nukiwa, T. and Satoh, K. Inhibition of experimental metastasis of human fibrosarcoma cells by anti-recombinant 37-kDa laminin binding protein antibody. Jpn. J. Cancer Res. 90 (1999) 425–431. Google Scholar

  • [26] Kaneda, Y., Kinoshita, K., Sato, M., Saeki, Y., Yamada, R., Wataya-Kaneda, M., and Tanaka, K. The induction of apoptosis in HeLa cells by the loss of LBP-p40. Cell Death Differ. 5 (1998) 20–28. http://dx.doi.org/10.1038/sj.cdd.4400315CrossrefGoogle Scholar

  • [27] Leucht, C., Simoneau, S., Rey, C., Vana, K., Rieger, R., Lasmezas, C.I. and Weiss, S. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep. 4 (2003) 290–295. http://dx.doi.org/10.1038/sj.embor.embor768CrossrefGoogle Scholar

  • [28] Leucht, C., Vana, K., Renner-Muller, I., Dormont, D., Lasmezas, C.I., Wolf, E. and Weiss, S. Knock-down of the 37-kDa/67-kDa laminin receptor in mouse brain by transgenic expression of specific antisense LRP RNA. Transgenic Res. 13 (2004) 81–85. http://dx.doi.org/10.1023/B:TRAG.0000017177.35197.89CrossrefGoogle Scholar

  • [29] Ardini, E., Pesole, G., Tagliabue, E., Magnifico, A., Castronovo, V., Sobel, M.E., Colnaghi, M.I. and Menard, S. The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. Mol. Biol. Evol. 15 (1998) 1017–1025. Google Scholar

  • [30] Knowles B.B., Howe, C.C. and Aden D.P. Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen. Science 209 (1980) 497–499. http://dx.doi.org/10.1126/science.6248960CrossrefGoogle Scholar

  • [31] Elbashir, S.M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411 (2001) 494–498. http://dx.doi.org/10.1038/35078107Web of ScienceCrossrefGoogle Scholar

  • [32] Hannon, G.J. RNA interference. Nature 418 (2002) 244–251. http://dx.doi.org/10.1038/418244aCrossrefGoogle Scholar

  • [33] Hurtado, A., Tseng, J.C. and Meruelo, D. Gene therapy that safely targets and kills tumor cells throughout the body. Rejuvenation Res. 9 (2006) 36–44. http://dx.doi.org/10.1089/rej.2006.9.36CrossrefGoogle Scholar

About the article

Published Online: 2008-07-07

Published in Print: 2008-09-01


Citation Information: Cellular and Molecular Biology Letters, Volume 13, Issue 3, Pages 452–464, ISSN (Online) 1689-1392, DOI: https://doi.org/10.2478/s11658-008-0017-6.

Export Citation

© 2008 University of Wrocław, Poland. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Leila Vania, Thalia M. Rebelo, Eloise Ferreira, and Stefan F. T. Weiss
BMC Cancer, 2018, Volume 18, Number 1
[2]
Carryn J. Chetty, Eloise Ferreira, Katarina Jovanovic, and Stefan F.T. Weiss
Experimental Cell Research, 2017
[4]
Taoufik Khalfaoui, Jean-François Groulx, Georges Sabra, Amel GuezGuez, Nuria Basora, Patrick Vermette, Jean-François Beaulieu, and Michelina Plateroti
PLoS ONE, 2013, Volume 8, Number 8, Page e74337
[5]
Lisa Venticinque, Kelly V. Jamieson, Daniel Meruelo, and Maddy Parsons
PLoS ONE, 2011, Volume 6, Number 1, Page e15895
[6]
Thandokuhle Khumalo, Eloise Ferreira, Katarina Jovanovic, Rob B. Veale, Stefan F. T. Weiss, and Corinne Ida Lasmezas
PLOS ONE, 2015, Volume 10, Number 10, Page e0139584
[8]
Aadilah Omar, Katarina Jovanovic, Bianca Da Costa Dias, Danielle Gonsalves, Kiashanee Moodley, Robert Caveney, Vusi Mbazima, and Stefan FT Weiss
Expert Opinion on Therapeutic Patents, 2011, Volume 21, Number 1, Page 35
[10]
Filipe Vilas-Boas, Ana Bagulho, Rita Tenente, Vitor H. Teixeira, Gabriel Martins, Gonçalo da Costa, Ana Jerónimo, Carlos Cordeiro, Miguel Machuqueiro, and Carla Real
Free Radical Biology and Medicine, 2016, Volume 90, Page 145
[11]
Katarina Jovanovic, Carryn J Chetty, Thandokuhle Khumalo, Bianca Da Costa Dias, Eloise Ferreira, Sibusiso T Malindisa, Robert Caveney, Boitelo T Letsolo, and Stefan FT Weiss
Expert Opinion on Therapeutic Patents, 2015, Volume 25, Number 5, Page 567
[12]
Vincent DiGiacomo and Daniel Meruelo
Biological Reviews, 2016, Volume 91, Number 2, Page 288
[13]
Bianca Da Costa Dias, Katarina Jovanovic, Danielle Gonsalves, and Stefan F.T. Weiss
Prion, 2011, Volume 5, Number 3, Page 126
[14]
Dae-Geun Song, Yoon Suk Kim, Byung Chul Jung, Ki-Jong Rhee, and Cheol-Ho Pan
Applied Biochemistry and Biotechnology, 2013, Volume 171, Number 7, Page 1630
[15]
Lisa Venticinque and Daniel Meruelo
Journal of Proteome Research, 2012, Volume 11, Number 10, Page 4863
[16]
Pietro Formisano, Pia Ragno, Ada Pesapane, Daniela Alfano, Anna Teresa Alberobello, Vincenza Elena Anna Rea, Raffaella Giusto, Francesca W. Rossi, Francesco Beguinot, Guido Rossi, and Nunzia Montuori
Journal of Cellular and Molecular Medicine, 2012, Volume 16, Number 7, Page 1435
[17]
Heike Pflanz, Karen Vana, Gerda Mitteregger, Ingrid Renner-Müller, Claudia Pace, Helmut Küchenhoff, Hans A. Kretzschmar, Eckhard Wolf, and Stefan Weiss
Journal of Molecular Biology, 2009, Volume 388, Number 4, Page 721
[18]
Aadilah Omar, Uwe Reusch, Stefan Knackmuss, Melvyn Little, and Stefan F.T. Weiss
Journal of Molecular Biology, 2012, Volume 419, Number 1-2, Page 102
[19]
J Scheiman, K V Jamieson, J Ziello, J-C Tseng, and D Meruelo
Cell Death and Disease, 2010, Volume 1, Number 5, Page e42
[20]
Jonathan Scheiman, Jen-Chieh Tseng, Yun Zheng, and Daniel Meruelo
Molecular Therapy, 2010, Volume 18, Number 1, Page 63
[21]
H. Pflanz, K. Vana, G. Mitteregger, C. Pace, D. Messow, C. Sedlaczek, D. Nikles, H. A. Kretzschmar, and S. F. T. Weiss
Journal of General Virology, 2009, Volume 90, Number 1, Page 269

Comments (0)

Please log in or register to comment.
Log in