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Suppression of Spontaneous Dermatitis in NC/Nga Murine Model by PG102 Isolated from Actinidia arguta
Park, Eun-Jin,Park, Kyoung Chul,Eo, Haekwan,Seo, Jangkyun,Son, Miwon,Kim, Kyu Han,Chang, Yoon-Seok,Cho, Sang-Heon,Min, Kyung-Up,Jin, Mirim,Kim, Sunyoung The Society for Investigative Dermatology, Inc 2007 The Journal of investigative dermatology Vol.127 No.5
Atopic dermatitis (AD) is a chronic inflammatory skin disease, which requires safe and effective pharmacological therapy. We previously found that two preparations from Actinidia arguta, PG102T, and PG102E, could modulate Th1/Th2 pathways and suppress IgE biosynthesis. This study was performed to assess the therapeutic effects of PG102T and PG102E on the development of dermatitis in NC/Nga mice, characterized by the spontaneous onset of AD along with an elevated level of IgE under conventional conditions. PG102T or PG102E administration significantly reduced dermatitis severity as well as scratching tendency in conventional mice. The suppression of dermatitis by PG102 was accompanied by a decrease in the plasma level of IgE, IgG1, and IL-4 and also by an increase in that of IgG2a and IL-12. The splenic level of IL-4, IL-5, and IL-10 was downregulated, whereas that of IFN-γ and IL-12 was increased. The number of eosinophils and the expression of eotaxin and thymus and activation-regulated chemokine were decreased by PG102T or PG102E. Histological findings also indicated that the thickening of epidermis/dermis and the dermal infiltration of inflammatory cells including mast cells were greatly inhibited. These data suggest that PG102 may be effective therapeutic agents for the treatment of AD.Journal of Investigative Dermatology (2007) 127, 1154–1160. doi:10.1038/sj.jid.5700658; published online 28 December 2006
Expression of an Angiogenin Binding Peptide and Its Anti-Angiogenic Activity
Choi, Suk-Jung,Yoon, Kyoung-Bum,Ahn, Miwon,Park, Jong-Won The Korea Science and Technology Center 1998 BMB Reports Vol.31 No.5
In the previous report (Choi et al., 1997), the angiogenin binding peptides identified from a phage-peptide library were analyzed by using the fusion proteins composed of the Escherichia coli maltose binding protein and its corresponding peptides. However, it was difficult to obtain a sufficient amount of the fusion proteins required for further analysis because of the low expression level. We now report a high level expression of the fusion protein and analysis of its anti-angiogenin activity. The use of strong T7 promoter and removal of signal sequence allowed about a 20-fold increase in the expression efficiency of the fusion protein. We were able to obtain about 10 mg of purified fusion protein from one liter of culture. The purified fusion protein showed angiogenin-specific affinity and inhibited the binding of biotinylated actin to human angiogenin at IC60 of 0.6 mM. Its anti-angioenin activity was also revealed by the chorio-allantoic membrane assay.