• Polymer(Korea)
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• v.38 no.2
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• pp.156-163
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• 2014

Hydroxyapatite has osteoconductivity, biocompatibility and noninflammatory, and it has been used clinically as artificial bone. In this study, we prepared hydroxyapatite/poly(lactic-co-glycolic acid) (PLGA) scaffolds using 0, 10, 20, 40 and 60 wt% of hydroxyapatite. We analyzed compressive strength, SEM analysis and FTIR for mechanical property of 3D hydroxyapatite/PLGA scaffolds. For biocompatibility tests, cell proliferation and viability were measured via MTT assay and SEM. We analyzed RT-PCR, FACS, histology (H&E, ED-1) for anti-inflammatory effect. This study showed that hydroxyapatite hybrid scaffolds have low inflammatory reaction compared with the PLGA. This result has a potential for the application of artificial bone graft material.

• Journal of Life Science
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• v.33 no.7
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• pp.531-537
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• 2023

Intracellular and axonal transport is mediated by microtubule-dependent motor proteins, such as kinesins and cytoplasmic dynein. Kinesin moves along the microtubule to the positive end of the microtubule, while dynein moves to the negative end of the microtubule. Kinesin-1 was first identified as a kinesin superfamily protein (KIF) that functions in the intracellular transport of various cargoes, including organelles, neurotransmitter receptors, and mRNA-protein complexes, through interactions between the carboxyl (C)-terminal domain and the cargo. It interacts with other cargoes, but the adapter/scaffold proteins that mediate between kinesin-1 and the cargo have yet to be fully identified. In this study, a yeast two-hybrid screen was used to identify adapter proteins that interact with the C-terminal region of KIF5A. We found an association between the C-terminal region of KIF5A and the cyclin-dependent kinase 2-associated protein 1 (CDK2AP1), originally identified in malignant hamster oral keratinocytes. CDK2AP1 bound to the C-terminal region of KIF5A and did not interact with KIF3A (the motor of kinesin-2), KIF5B, KIF5C, and kinesin light chain 1 (KLC1). The C-terminal region of CDK2AP1 is essential for its interaction with KIF5A. When co-expressed in HEK-293T cells, CDK2AP1 and kinesin-1 co-immunoprecipitated and co-localized in the cells. These results suggest that the KIF5A-CDK2AP1 interaction serves as an adapter protein connecting kinesin-1 and the cargo when kinesin-1 transports cargo in cells.