Digitalising Korea - transformations and tensions : the case of audiovisual service trade and intellectual property rights

Since the 1990s, South Korea has enthusiastically developed and applied digital technologies to every sector of economic and social life, and constructed the most intensively connected society in the world. This thesis explores the impact of Digital Korea on the country s cultural industries, focussing particularly on the main audio-visual industries of broadcasting and film. While the push to digitalise Korea has been enthusiastically pursued by successive national governments with the aim of ensuring that Korea maintains its status as a key world economy as the leading edge of capitalism shifts from an industrial to an information base, to fully understand the forms it has taken and its impacts national initiatives have to be placed in the wider context of shifts in the global trading system. With the rise of neo-liberalism across the globe and the perceived ineffectiveness of the World Trade Organisation (WTO) in extending multi-lateral trade, both emerging and developed economies have increasingly embraced Free Trade Agreements (FTAs). In line with this trend, South Korea has signed FTAs with the USA, the European Union (EU) and The Association of Southeast Asian Nations (ASEAN). This thesis explores the interplay between national initiatives and global trade through a detailed case study of the US-led FTA with South Korea (KORUS-FTA) focusing particularly on its implications for the Audiovisual Sector and the accompanying, and pivotal, debates around Intellectual Property Rights (IPRs). The KORUS FTA simultaneously opened the Korean market to American audiovisual content and strengthened existing national IPR laws to match the provisions prevailing within the US. Both these moves were opposed within Korea on the grounds that they operated unequally, to the advantage of the US and the detriment of national production that had, in recent years, enjoyed considerable success in export markets, creating what came to be known as the Korean Wave . In addition utilising the extensive corpus of available public documentation the analysis presented here draws on two original research exercises: in depth interviews with experts in international trade and intellectual property rights, conducted in South Korea, the UK and Switzerland (in Geneva, at the WTO Forum 2008), and a web-based survey of a cross section of professionals working in the Korean broadcasting industry. The results obtained show that while Korean economists followed the government in arguing that signing the FTA with the US was essential if Korea was to remain a major player in the global economy, a majority of those working in the audiovisual sector believed that the terms of the agreement, particularly the imposition of US-style IPR laws, disproportionately favoured US interests and would weaken the strong position the sector had achieved in recent years and impede its future growth

Complete xmlv genome.

<p>(A) Schematic map of the 8176 nt genome of xmlv15. The LTR regions (R, U5, U3) are indicated with boxes. Two open reading frames encoding <i>gag-pro-pol</i> and <i>env</i> polyproteins are predicted. The corresponding start (AUG) and stop codons (UAA) are shown, along with their nucleotide positions. (B) Cloning and sequencing of the xmlvs. The clones obtained by PCR from SAM mouse genomic DNA (black bars) were sequenced. Primers used to amplify individual clones (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0055669#pone-0055669-t001" target="_blank">Table 1</a>) were derived from overlapping xmlv clones (arrows).</p

Detection of the xmlv proviruses.

<p>(A) PCR results screening of the genomic DNA of SAM, C57BL and ICR mouse strains, hamsters and humans. (B) RT-PCR analysis of xmlvs in the brains of various mouse strains, including SAMP8, SAMR1, C57BL and ICR.</p

Multiple sequence alignment of xmlvs.

<p>(A) Sequence comparison of <i>pol</i> gene regions of xmlvs was performed with the corresponding regions of other X-MuLV isolates, DG-75 MuLV and XMRV VP62. (B) Multiple sequence alignment of the deduced amino acid sequences of xmlvs and related MuLVs spanning SU glycoprotein VRA, VRB and VRC, which were characterized by important regions for cellular tropism. This analysis employed the <i>env</i> protein sequences from the following viruses; AKV, Friend MuLV, Moloney MuLV, Rauscher MuLV, prototype polytropic clone MX27, DG-75, MTCR, MuLV MCF247, MuLV MCF 1233, MuLV NFS-Th-1 and MuLV NZB-9-1. The sequences were aligned using ClustalX. The dots indicate residues identical to those from xmlv15, and deleted residues appear as spaces.</p

Phylogenetic analysis of the xmlvs.

<p>Phylogenetic trees were constructed based on (A) the complete genome sequences of the xmlv15 and (B–C) the predicted <i>gag</i>, <i>pro-pol</i> and <i>env</i> polyproteins of xmlvs. The full length nucleotide sequences and the deduced amino acid sequences of the xmlvs as well as the corresponding sequences from identified MuLVs were aligned using ClustalX. The resulting alignments were used to generate neighbor-joining trees. The values at the branch nodes represent the percentage of confidence in a specific branching. The sequences of the xmlvs (xmlv15 and xmlv18) are highlighted in gray. The sequences used in the analysis and in the construction are as follows: non-ecotropic proviruses (mERVs), AKV MuLV, Friend MuLV, Moloney MuLV, Rauscher MuLV, Feline leukemia virus, Gibbon ape leukemia virus, Koala retrovirus, DG-75, MTCR, MuLV MCF 1233, XMRV VP35, MuLV NCI-417, MuLV NZB-9-1, XMRV 22Rv1, MX33 and Rmf2.</p

The cell-cell adhesion mechanisms to form plaques.

<p>(A) Scheme of PrP-MuLV-Gal interaction in cell membrane. (B) Based on our data between the cells PrP-Gal3 has binding activity and Gal3-CAgag-Gal6 shows binding activity. To produce the plaques, Gal3 is suggested to combine between PrP and MuLV. Gal6 is suggested to combine two different viruses to form plaques.</p

Different susceptibility to MuLV infection of MoPrP^<i>KO</i>, MoPrP^<i>wild</i> and MoPrP^<i>mut</i> neuronal cells.

<p>Neuronal cells expressing PrP^C, regardless of their type, were shown to have higher susceptibility to MuLV infection in illumination microscopy. Neuronal cells expressing MoPrP^<i>wild</i>, ZW, or PrP^C with the 3F4 epitope, or MoPrP^<i>mut</i> with the octarepeat deletion, PrPΔ, showed intense staining of both PrP and CAgag at a similar level. The location of PrP in these cells was primarily in cytosol and membrane before MuLV infection. After MuLV infection, PrP staining was observed in the nucleus, cytosol, and also membranes. MuLV infection was observed mainly in cytosol by detection of CAgag. Neuronal cells expressing P101L mutant type of PrP^C, MoPrP^<i>mut</i>, were also susceptible to MuLV infection. The PrP^C of P101L was mainly located in the nuclear portion of the cells, thus the overlapping between PrP^C and CAgag was not observed clearly through illumination microscopy. MuLV infections in astroglial cells were not affected by PrP^C. Different from neuronal cells, astroglial cells were largely resistant to infection by MuLV. Green, PrP; Red, CAgag; Blue, DAPI; Yellow, Merge. Scale bar = 20 μm.</p

Expression and binding activity of PrP^C with galectin-1,-3, and -6 mRNAs and proteins.

<p>(A) Expression of mRNA levels of galectin-1, -3, and -6 was observed by quantitative RT-PCR method. Binding activity of PrP^C with galectin-1, -3, and -6 mRNAs was investigated by immunoprecipitation of mRNA-protein complex method using anti-PrP antibody (anti-3F10). Galectin-1 mRNA is constitutively expressed regardless of no infection or MuLV infection. Galectin-3 mRNA expression is closely related with PrP^C expression, thus it is detected in PrP^C-expressing neuronal cells but not in PrP^-/- neuronal cells. Galectin-6 mRNA expression is related to MuLV infection in PrP^C-expressing cells but not in PrP^-/- cells, P101L cells and PrP^+/+ astroglial cells. Binding activity of PrP^C to galectin mRNAs was closely related to MuLV infection in PrP^+/+ cells. For P101L cells, the binding activity to galectin-1 and -6 was unusual in that binding occurred in non-infected cells. This may have contributed to the large plaque size seen in P101L cells. (B) Anti-PrP (3F10) antibody was used to proceed immunoprecipitation then anti-PrP (3F10) (27–33 kDa), -galectin-1 (Gal1)(14 kDa), -galectin-3 (Gal3)(31 kDa), -galectin-6 (Gal6)(32 kDa), and –CAgag (30 kDa) antiboties were used to detect expression level of each protein. PrP was detected in all PrP expressing cell lines: ZW, 3F4, PrPΔ, P101L, and ICR cell lines regardless of infected or non-infected. CAgag and Gal3 was detected in MuLV-infected neuronal cell lines: ZW, 3F4, PrPΔ, and P101L cell lines. Gal1 and Gal6 was not detected in any of cell lines regardless of infected or non-infected. (C) Anti-CAgag antibody was used to proceed immunoprecipitation then anti-PrP (3F10) (27–33 kDa), -galectin-1 (Gal1)(14 kDa), -galectin-3 (Gal3)(31 kDa), -galectin-6 (Gal6)(32 kDa), and –CAgag (30 kDa) antiboties were used to detect expression level of each protein. CAgag was detected in all MuLV infected cells and Gal1 was not detected. PrP, Gal3, and Gal6 was detected at MuLV-infected PrP^+/+ cells.</p

Expression levels of the PrP^C genes and proteins in neuronal and astroglial cell lines.

<p>(A) Analysis of expression levels of <i>Prnp</i> in <i>Prnp</i>^-/-, Zpl, Vec, and Za, and <i>Prnp</i>^+/+, ZW, 3F4, PrPΔ, P101L, and ICR cell lines. ZW, 3F4, P101L, and ICR-A cell lines contained full-length of <i>Prnp</i> (789 bp). Cell lines expressing wild-type PrP^C are called the ZW cell line (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0167293#pone.0167293.t001" target="_blank">Table 1</a>). PrPΔ cell line contained shorter length <i>Prnp</i> (663 bp). Zpl, Vec, and Za cell lines were negative for <i>Prnp</i> detection. (B) Protein levels of PrP in cell lines were consistent with the results of RT-PCR analysis. PrPΔ cell line showed shorter length PrP. (C) Densitometry analysis of PrP protein expression showed no significant difference between wild-type cells and PrP-transfected cells. Relative values are represented as the mean±SEM. Cell lines were assessed by three separate experiments. ZW 13–2, 100±7.82; 3F4-A3, 87.8±9.53; PrPΔP1-3, 93.8±9.11; P101L-C4, 83.94±9.41; ICR-A3, 88.75±10.23.</p

Primer sequences and conditions for RT-PCR.

<p>Primer sequences and conditions for RT-PCR.</p