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Big-h3내 RGD-motif의 유전자 변이 유도에 의한 유방암 세포의 성장 및 이동성에 미치는 영향
김연향(Yeon-Hyang Kim) 산업기술교육훈련학회 2019 산업기술연구논문지 (JITR) Vol.24 No.4
The extracellular matrix (ECM) plays an important role in cellular migration associated with pathological conditions, such as inflammation and cancer. Big-h3 (also known as transforming growth factor-β-induced protein (TGFBI), beta ig-h3, TGF-b-induced protein h3, keratoepithelin, and RGD-CAP) is an extracellular secretory protein and includes the YH and RGD motifs, which interact with the ECM. In this study, big-h3 and a big-h3 fragment (big-h3-f, 182 amino acids) containing the RGD-motif were cloned. To determine whether the RGD-motif affects cell growth, the aspartic acid residue (D) in the RGD motif of wild-type big-h3 or big-h3-f was mutated to a glutamic acid (E) via site-directed mutagenesis, thereby yielding a RGE-motif containing mutant protein. Big-h3, big-h3-f, mutant big-h3, or mutant big-h3-f were transfected into the human breast cancer cell line MCF-7 and their expression was confirmed using immunoblotting. Our results showed that wild type big-h3 and big-h3-f containing the RGD-motif led to increased cell growth and invasion, compared to the corresponding mutants with the RGE-motif. Therefore, the RGD-motif in big-h3 possibly plays a major role in cell growth and regulation of invasion, in the context of cell-ECM interaction.
Kim Jeong Hee,Choi Jeong In,Che Young Hyun,Sung Su Haeng,Lee Hojae,Lee Sun,Park Jae-Hoon,Lee Yun-Il,Lee Young-Sam,Jeon Won Bae,Kim Yong Jun 한국조직공학과 재생의학회 2023 조직공학과 재생의학 Vol.20 No.7
BACKGROUND Cryopreservation is a crucial method for long-term storage and stable allocation of human pluripotent stem cells (hPSCs), which are increasingly being used in various applications. However, preserving hPSCs in cryogenic conditions is challenging due to reduced recovery rates. METHODS To address this issue, the Arginine-Glycine-Aspartate (RGD) motif was incorporated into a recombinant elastin-like peptide (REP). Human embryonic stem cells (hESCs) were treated with REP containing RGD motif (RGDREP) during suspension and cryopreservation, and the survival rate was analyzed. The underlying mechanisms were also investigated. RESULTS The addition of RGD-REP to the cryopreservation solution improved cell survival and pluripotency marker expression. The improvement was confirmed to be due to the activation of the FAK-AKT cascade by RGD-REP binding to hESC surface interin protein, and consequent inhibition of FoxO3a. The inactivation of FoxO3a reduced the expression of apoptosis-related genes, such as BIM, leading to increased survival of PSCs in a suspension state. CONCLUSION RGD-REP, as a ligand for integrin protein, improves the survival and maintenance of hPSCs during cryopreservation by activating survival signals via the RGD motif. These results have potential implications for improving the efficiency of stem cell usage in both research and therapeutic applications.
Kim, Bum Jin,Choi, Yoo Seong,Choi, Bong-Hyuk,Lim, Seonghye,Song, Young Hoon,Cha, Hyung Joon Wiley Subscription Services, Inc., A Wiley Company 2010 Journal of biomedical materials research. Part A Vol.a94 No.3
<P>Adhesion of cells to a surface is a basic and important requirement in the fields of cell culture and tissue engineering. Previously, we constructed the cell adhesive, fp-151-RGD, by fusion of the hybrid mussel adhesive protein, fp-151, and GRGDSP peptide, one of the major cell adhesion recognition motifs; fp-151-RGD efficiently immobilized cells on coated culture surfaces with no protein and surface modifications, and apparently enhanced cell adhesion, proliferation, and spreading abilities. In the present study, we investigated the potential use of fp-151-RGD as a biomimetic extracellular matrix material at the molecular level by elucidating its substantial effects on integrin-mediated adhesion and signaling. Apoptosis derived from serum deprivation was significantly suppressed on the fp-151-RGD-coated surface, indicating that RGD-induced activation of integrin-mediated signaling triggers the pathway for cell survival. Analysis of the phosphorylation of focal adhesion kinase clearly demonstrated activation of focal adhesion kinase, a well-established indicator of integrin-mediated signaling, on the fp-151-RGD-coated surface, leading to significantly enhanced cell behaviors, including proliferation, spreading and survival, and consequently, more efficient cell culture. © 2010 Wiley Periodicals, Inc. J Biomed Mater Res Part A, 2010</P>
유희영,송영훈,서정현,차형준,황동수 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.2
Endurable coating on biomedical substrates is one of the most important issues in biomedical engineering field. Recently, a robust yet reversible coating has found in the cuticle of mussel byssus and the mimicking of the mussel cuticle coating has been considered as a strategy to build up endurable coating on biomedical materials. To date, the only known protein in the cuticle is mussel foot protein-1 (fp-1). To form endurable and bioactive coating on the biomedical surface, the fusion protein of fp-1 and GRGDSP peptide (fp-1-RGD) was genetically designed and produced in E. coli. The fusion protein of fp-1-RGD was successfully expressed as a form of inclusion body and was simply purified by diluted acetic acid extraction with high purity (~95%). Fp-1-RGD was coated on the tissue culture polystyrene (TCPS) and showed better preosteoblast cell proliferation than that of TCPS. Therefore, the marriage of fp-1 and bioactive peptide can be a good strategy to form bioactive and endurable coating in biomedical field.