• Title/Summary/Keyword: Complex Pore Pattern

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Experimental Research of ZrO2/BCP/PCL Scaffold with Complex Pore Pattern for Bone Tissue Regeneration (골 조직 재생을 위한 복합 공극 패턴을 가진 ZrO2/BCP/PCL 인공지지체의 실험적 평가)

  • Sa, Min-Woo;Shim, Hae-Ri;Kim, Jong Young
    • Transactions of the Korean Society of Mechanical Engineers A
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    • v.39 no.11
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    • pp.1153-1159
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    • 2015
  • Recently, synthetic biopolymers and bioceramics such as poly (${\varepsilon}$-caprolactone)(PCL), hydroxyapatite, tricalcium phosphate, biphasic calcium phosphate(BCP), and zirconia have been used as substrates to generate various tissues or organs in tissue engineering. Thus, the purpose of this study was the characterization of $ZrO_2$/BCP/PCL(ZBP) scaffold for bone tissue regeneration. Based on the result of single-line test, blended 3D ZBP scaffolds with fully interconnected pores and new complex pore pattern of $45^{\circ}+135^{\circ}$-type and staggered-type were successfully fabricated using a polymer deposition system. Furthermore, the effect of ZBP scaffold on mechanical property was analyzed. In addition, in vitro cell interaction of ZBP scaffold on MG63 cells was evaluated using a cell counting kit-8(CCK-8) assay.

The development of encoded porous silicon nanoparticles and application to forensic purpose (코드화 다공성 실리콘 나노입자의 개발 및 법과학적 응용)

  • Shin, Yeo-Ool;Kang, Sanghyuk;Lee, Joonbae;Paeng, Ki-Jung
    • Analytical Science and Technology
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    • v.22 no.3
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    • pp.247-253
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    • 2009
  • Porous silicon films are electrochemically etched from crystalline silicon wafers in an aqueous solution of hydrofluoric acid(HF). Careful control of etching conditions (current density, etch time, HF concentration) provides films with precise, reproducible physical parameters (morphology, porosity and thickness). The etched pattern could be varied due to (1) current density controls pore size (2) etching time determines depth and (3) complex layered structures can be made using different current profiles (square wave, triangle, sinusoidal etc.). The optical interference spectrum from Fabry-Perot layer has been used for forensic applications, where changes in the optical reflectivity spectrum confirm the identity. We will explore a method of identifying the specific pattern code and can be used for identities of individual code with porous silicon based encoded nanosized smart particles.

The Distribution of ATPase and Porin in the Bovine Heart Mitochondrial Cristae (소(牛) 심근 미토콘드리아의 ATPase와 porin의 분포)

  • Kim, Tae-Keun;Min, Byoung-Hoon;Kim, Soo-Jin
    • Applied Microscopy
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    • v.40 no.4
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    • pp.261-266
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    • 2010
  • ATP is the energy source synthesized at the electron transferase that consist of complex I, II, III, IV and V in mitochondrial cristae. The complex V functions as ATPase which composed of sub-complex $F_0$ and $F_1$. Porin or VDAC (voltagedependent anion-selective channel), is a family of small pore-forming proteins of the mitochondrial outer membrane, and play important roles in the regulated flux of anion, proton and metabolites between the cytosolic and mitochondrial compartments. The channel allows the diffusion of negatively charged solutes such as succinate, malate, and ATP in the fully open state, but of positively charged ions in subconducting state. In this study, in order to investigate the relationship of the function and localization between porin and ATPase we observed the distribution of porin and ATPase in the mitochondria of the bovine heart. Monoclonal antibodies against porin and ATPase ${\beta}$-subunit were used to detect porin and ATPase using light microscope with immunohistochemistry and immunofluorescence, and using electron microscope with immunogold-labeling. ATPase were stained in longitudinal section region in cardiac muscle, porin were stained in longitudinal section region in cardiac muscle. We viewed more specific pattern of localization and distribution of these proteins using immunofluorescence method. There were some region which were labeled with porin or ATPase respectively, and others which were labeled both proteins in cardiac muscle. The electron microscope results showed that immunogold labeled porin were labeled locally at mitochondrial outer membrane and ATPase were labeled evenly at mitochondrial cristae. But ATPase was not labeled at mitochondria cristae. These results confirmed the subcellular localizations of porin and ATPase in mitochondrial outer membrane and cristae. Also, we assumed that ATP synthesis always does not activation in all mitochondria exist in the bovine cardiac muscle.