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Ji-Hyun Yeom,Eunkyoung Shin,Hanyong Jin,Haifeng Liu,Yongyang Luo,Youngwoo Nam,Minkyung Ryu,Wooseok Song,Heeyoun Chi,Jeongkyu Kim,Kangseok Lee,Jeehyeon Bae 한국공업화학회 2023 Journal of Industrial and Engineering Chemistry Vol.126 No.-
Antibodies are being increasingly used for therapeutic purposes due to their remarkable target specificityand affinity. However, currently available antibody therapies are restricted to target proteins in the outercell membrane or in the extracellular fluids because of the lack of technologies for effective intracellulardelivery of antibodies. Here, we report an efficient and versatile intracellular antibody delivery system. This system is based on gold nanoparticles (AuNPs) conjugated with DNA aptamers (Apt) against theFc region of IgG (AuNP-AptIgG), allowing to load any antibodies onto the AuNP-AptIgG by simple mixing. This AuNP-AptIgG-Ab platform was effective for cytosolic delivery of antibodies to clinically importantmutant proteins via scavenger receptors and caveolae-mediated endocytosis. Specifically, cancer cellsexpressing BRAFV600E, a variant of BRAF identified in numerous types of cancers, exhibited reduced cellviability by 70% when BRAFV600E antibodies were intracellularly delivered using the AuNP-AptIgG(AuNP-AptIgG-aBRAFV600E). In addition, subcutaneous injection of AuNP-AptIgG-aBRAFV600E into in vivoxenografted melanoma tumors expressing BRAFV600E resulted in both inhibition of proliferation andinduction of apoptosis, leading to tumor regression in mice. Thus, our findings indicate that the AuNPAptIgG-Ab system can serve as a promising platform for effective intracellular delivery of antibodies fortherapeutic purposes.
An Mi-Jin,Lee Hyun Min,Kim Chul-Hong,Shin Geun-Seup,Jo Ah-Ra,Kim Ji-Young,Kim Mi Jin,Kim Jin Ho,Park Jinhong,Hwangbo Yujeong,Kim Jeongkyu,Kim Jung-Woong 한국유전학회 2023 Genes & Genomics Vol.45 No.4
Background The transcription factor orthodenticle homeobox 2 (OTX2) has critical functions in brain and eye development, and its mutations in humans are related to retinal diseases, such as ocular coloboma and microphthalmia. However, the regulatory mechanisms of OTX2 are poorly identified. Objective The identification of JNK1 as an OTX2 regulatory protein through the protein interaction and phosphorylation. Methods To identify the binding partner of OTX2, we performed co-immunoprecipitation and detected with a pooled antibody that targeted effective kinases. The protein interaction between JNK1 and OTX2 was identified with the co-immunoprecipitation and immunocytochemistry. In vivo and in vitro kinase assay of JNK1 was performed to detect the phosphorylation of OTX2 by JNK1. Results JNK1 directly interacted with OTX2 through the transactivation domain at the c-terminal region. The protein–protein interaction and co-localization between JNK1 and OTX2 were further validated in the developing P0 mouse retina. In addition, we confirmed that the inactivation of JNK1 K55N mutant significantly reduced the JNK1-mediated phosphorylation of OTX2 by performing an immune complex protein kinase assay. Conclusion c-Jun N-terminal kinase 1 (JNK1) phosphorylates OTX2 transcription factor through the protein–protein interaction.
( Wonjun Choi ),( Jinsook Seok ),( Inyoung Choi ),( Jikwon Park ),( Jeongkyu Shin ),( Soonae Lee ),( Wonyoung Paik ),( Jonghak Lee ) 대한산부인과학회 2015 Obstetrics & Gynecology Science Vol.58 No.5
Revascularization is critical for successful ovarian tissue transplantation. Vascular endothelial growth factor (VEGF) and angiopoietin-2 (angpt-2) are the principal mediators of neovascularization. This study was designed to assess VEGF and angpt-2 levels in cryopreserved ovarian tissue after heterotopic autotransplantation.Ovarian tissues harvested from ICR mice at 5 to 6 weeks of age were stratified as follows: no cryopreservation (controls, group I); vitrification in VFS-40 (vitrification, group II); and gradual freezing in dimethyl sulfoxide (slow-freezing, group III). Frozen specimens were thawed at room temperature, assaying VEGF and angpt-2 levels 1 week after cryopreservation and 2 weeks after autotransplantation.VEGF and angpt-2 protein levels were significantly lower in cryopreserved ovaries of groups II and III than in controls (group I, P<0.05), whereas groups II and III did not differ significantly in this regard. After autotransplantation of cryopreserved ovarian tissue, VEGF and angpt-2 protein levels did not differ significantly by technique but tended to be lower than corresponding levels in controls.Expression of angiogenic factors in ovarian tissue is thought to vary by method of cryopreservation. Our findings indicate that levels of angiogenic factors expressed in cryopreserved ovarian tissue after autotransplantation do not differ appreciably from control levels, regardless of cryopreservation technique.