• 제목/요약/키워드: transferrin receptor

검색결과 49건 처리시간 0.03초

배양 Caco-2 세포 단층막 실험계에서 트란스페린과 옥시다아제효소 포합체의 세포막투과 (Transport of Transferrin-Horseradish Peroxidase Conjugate Through Cultured Caco-2 Cell Monolayer)

  • 김동출;김지혜
    • Journal of Pharmaceutical Investigation
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    • 제29권4호
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    • pp.287-293
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    • 1999
  • Transport study of horseradish peroxidase and transferrin-horseradish peroxidase conjugate was performed using an in vitro Caco-2 cell cultured monolayer grown on a polycarbonate membrane of $Transwell^{\circledR}$, Horseradish peroxidase was not transported across Caco-2 cell monolayer. Transferrin-horseradish peroxidase conjugate was transported through Caco-2 cell monolayer. The apparent membrane permeability coefficient $(P_{app})$ of transferrin horseradish peroxidase conjugate was $6.54{\times}10^{-7}\;cm/sec$. The $P_{app}$ value of transferrin-horseradish peroxidase conjugate across Caco-2 cell monolayer was increased to $11.9{\times}10^{-7}\;cm/sec$ in the presence of $50\;{mu}g/ml$ brefeldin-A. These results suggest the transferrin receptor mediated transcytosis of transferrin-horseradish peroxidase conjugate across Caco-2 cell monolayer.

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마우스에서 뇌관류법과 정맥투여법에 의하여 흰쥐 트란스페린 단일항체의 체내동태 및 혈액-뇌 관문 투과성의 검토 (The Determination of Blood-Brain Barrier Permeability and Pharmacokinetics of a Rat Transferrin Receptor Monoclonal Antibody by Brain Perfusion Method and Intravenous Injection Technique in Mice)

  • 강영숙
    • Biomolecules & Therapeutics
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    • 제10권1호
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    • pp.37-42
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    • 2002
  • Brain drug targeting through the blood-brain barrier (BBB) in vivo is possible with peptidornirnetic monoclonal antibodies that undergo receptor-mediated transcytosis through the BBB. Monoclonal antibody to the rat transferrin receptor, such as the OX26 was studied in rats as a transport vector through BBB on the transferrin receptor. But, OX26 is not an effective brain delivery vector in mouse. In the present studies, rat monoclonal antibody, 8D3 to the mouse transferrin receptor were evaluated for brain drug targeting vector intransgenic mouse model. Pharrnacokinetic parameters in plasma and organ uptakes were determined at varioustimes after i.v. bolus injection of [$^{}125}I$] 8D3 in Balb/c mice. Brain uptake of [$^{}125}I$] 8D3 was also studied with an internal carotid artery perfusioncapillary depletion method. After i.v. injection of [$^{}125}I$] 8D3, plasma concentrations declined biexponentially with elimination half lift of approximately 2.2 hours. Brain uptake of [$^{}125}I$] 8D3 was $0.50{\pm}0.09$ persent of injected dose per g brain after 2 hours i.v. injection. After perfusion 5 min the apparent volume of distibution of [$^{}125}I$] 8D3 in brain was $22.3 {\mu}l/g,$ which was 4.8 fold higher than the intravascular volume. These studies indicate rat monoclonal antibody to the mouse transferrin receptor, 8D3 may be used for brain drug targeting vector in mice.

파지-펩타이드 문고로부터 트랜스페린 수용체에 결합하는 펩타이드 탐색 (Identification of a Transferrin Receptor-binding Peptide from a Phage-displayed Peptide Library)

  • 김성일;최석정
    • 생명과학회지
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    • 제18권3호
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    • pp.298-303
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    • 2008
  • 펩타이드 문고 기술을 이용하여 흑색종 세포주인 B16FI0에 결합하는 펩타이드 리간드를 검색하였다. 먼저 세포 내부로 들어간 파지들을 선택하는 방법으로 두 번 검색한 후 표면에 결합한 파지들 가운데 트랜스페린 단백질을 이용하여 트랜스페린 수용체에 결합한 파지들만을 선별적으로 용출시키는 방법으로 세 번 검색하였다. 다음으로 이 두 가지 방법을 통해 선별된 파지들에 표현된 펩타이드들을 Pseudomonas exotoxin의 전이 영역과 촉매 영역에 융합시킨 재조합 독소들을 만들었다. B16FI0 세포에 대한 각 재조합 독소의 활성을 측정하여 일곱 개의 클론을 선택한 후 염기서열을 분석하였다. 그 결과 그 가운데 한 클론에서 표현하는 펩타이드의 아미노산 서열이 사람의 트랜스페린과 유사한 서열을 갖는 것으로 확인되었다. 그 펩타이드를 화학적으로 합성한 후 항암제를 포함하는 리포솜에 붙여 실험한 결과 트랜스페린 수용체를 통해 치료물질을 전달할 수 있는 가능성을 지닌 것으로 평가되었다.

계배 근원세포의 융합에 따른 Transferrin 수용체의 변화 (Alteration in the Transferrin Receptor during the Chick Myoblast Fusion in Culture)

  • 이창호;유병제;전영주;정진하;하두봉
    • 한국동물학회지
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    • 제32권2호
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    • pp.163-175
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    • 1989
  • 철 운반 단백질인 Transferrin (Tf)은 계배 근원세포의 분화에 필요한 요소임이 이미 알려져 있다. 따라서 Tf이 작용하는데 필요한 Tf 수용체의 양적 증감은 근원세포의 분화와 깊은 관계가 있을 것으로 생각된다. 본 연구에서는 배양 근원세포의 분화 과정에서 Tf 수용체가 어떠한 변화를 겪는지 알아 보았다. Tf 수용체의 양을 알아보기 위해 세포 표면에 결합되는 125I-Tf의 양을 측정한 결과, Tf 수용체는 근원세포의 분화과정의 하나인 세포융합이 일어나기 약 12시간 전까지 그 양이 증가하다가, 그 이후 근원세포의 분화가 더욱 진행됨에 따라 급격히 감소함을 알 수 있었다. 한편, 근원세포의 융합을 억제하는 여러가지 융합억제제들에 의해서도 그 양이 조절되는 것을 알 수 있었다. 이와 같은 결과들은 통해 근원세포의 분화는 근원세포 표면의 Tf 수용체의 양과 조절되는 것으로 미루어 보아, 생체내에서도 근원세포의 분화에 따라 Tf 수용체의 변화가 있는 것으로 추정되었다.

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뇌종양세포주에서의 성장인자수용체의 발현 : 면역독소 치료의 연구를 위한 예비실험 (Growth Factor Receptor Expression on Brain Tumor Cell Lines : Preliminary Study for in vitro and in vivo Experiments of Immunotoxin Therapy)

  • 김기욱
    • Journal of Korean Neurosurgical Society
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    • 제29권6호
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    • pp.731-737
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    • 2000
  • 목 적 : 종양세포의 세포면에서는 성장인자 수용체들이 과발현되고 이들이 성장인자들과 결합함으로서 세포의 성장을 촉진하게 된다. 원발성 악성 뇌종양에 대한 새로운 치료법 중 하나가 면역독소를 사용하는 방법이다. 독소는 대상 세포의 세포면에 있는 수용체를 통해 세포질로 이행되며, 면역독소가 선택적인 항종양작용을 나타내기 위해서는 수용체가 과발현되어야 한다. 강력한 세포독성의 효과가 있음에도 불구하고 면역독소를 환자에 투여하였을 때 종양을 완치시키지는 못하였는데, 면역독소의 효과에 영향을 미치는 여러 인자들에 대한 더 많은 연구가 요구된다. 이러한 연구에 사용되어질 뇌종양세포주들에서 성장인자수용체들의 발현 여부를 알아보기 위해 본 연구를 시행하였다. 대상 및 방법 : 한 개의 수모세포종 세포주(Daoy)와 두 개의 교모세포종 세포주(U373 MG, T98 G)에서, transferrin 수용체, insulin-like growth factor-1 수용체, 그리고 interleukin-4 수용체들의 발현을 flow cytometric analysis를 이용하여 조사하였다. 결 과 : Transferrin 수용체와 interleukin-4 수용체는 Daoy, U373 MG, 그리고 T98 G 모두에서 발현되었다. Insulin-like growth factor-1 수용체는 Daoy와 U373 MG에서는 발현되었지만 T98 G에서는 발현되지 않았다. 결 론 : Transferrin 수용체와 interleukin-4 수용체는 면역독소 치료에 적합한 것으로 보인다. 본 실험의 결과는 상기의 세포주를 사용하여 면역독소와 관련된 실험을 하는데 참고가 되어야하며, 면역독소 치료에 있어서 적절한 면역독소를 선택하는 문제 등 치료 모델을 확립하는데 고려되어야 할 것이다.

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Cloning and Characterization of the Putative Transferrin Receptor cDNA from the Olive Flounder (Paralichthys olivaceus)

  • Won Kyoung-Mi;Park Soo-Il
    • Fisheries and Aquatic Sciences
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    • 제6권2호
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    • pp.101-104
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    • 2003
  • A cDNA clone for the olive flounder (Paralichthys olivaceus) transferrin receptor (fTfR) was isolated from a leukocytes cDNA library. The fTfR gene consisted of 2,319 bp encoding 773 amino acid residues. The amino acid sequence alignment of the fTfR showed that their size and hydrophobic profile are similar. In addition, the Tyr-Thr-Arg-Phe (YTRF) motif that is the recognition signal for high-efficiency endocytosis, is conserved very well. This motif is important for functional properties of TfR. The deduced amino acid sequence had $42.4-42.9\%$ identities with the previously reported TfRs of vertebrates. The fTfR was expressed in the blood, kidney, spleen, and liver of healthy olive flounder by the Northern blot hybridization.

계배 신경아세포의 분화에 따른 Transferrin 수용체의 변화 (Changes in the Level of Transferrin Receptor during the Differentiation of Chick Brain Neuroblasts)

  • 이창호;전영주
    • 한국동물학회지
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    • 제35권2호
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    • pp.144-148
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    • 1992
  • Insulin and transfenin (Tf) were found to be essential for suwival and differentiation of brain neuroblasts obtained from chick embryo. This requirement, however, is Changed from insulin to Tf upon neuronal development of the embryo, and this phenomenon is due to the changes in the levels of corresponding receptors. Using cultured neuroblasts, the level of Tf receptor is also found to increase Lvhile that of insulin receptor falls dramatically during the course of the cell differentiation. These results suggest that the development-specific changes in the levels of insulin and Tf receptors in embryo can be reproduced in the culture system during the differentiation period. Because the culture system used was a defined medium and contained no other macromolecules than insulin and Tf, it appears possible that insulin and Tf may act as signalling molecules in the control of neuronal development.

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The usefulness of soluble transferrin receptor in the diagnosis and treatment of iron deficiency anemia in children

  • Yoon, Se Hoon;Kim, Dong Sup;Yu, Seung Taek;Shin, Sae Ron;Choi, Du Young
    • Clinical and Experimental Pediatrics
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    • 제58권1호
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    • pp.15-19
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    • 2015
  • Purpose: Soluble transferrin receptor (sTfR) is a truncated extracellular form of the membrane transferrin receptor produced by proteolysis. Concentrations of serum sTfR are related to iron status and erythropoiesis in the body. We investigated whether serum sTfR levels can aid in diagnosis and treatment of iron deficiency anemia (IDA) in children. Methods: Ninety-eight patients with IDA were enrolled and were classified according to age at diagnosis. Group 1 comprised 78 children, aged 6-59 months, and group 2 comprised 20 adolescents, aged 12-16 years. Results: In group 1, patients' serum sTfR levels correlated negatively with mean corpuscular volume; hemoglobin (Hb), ferritin, and serum iron levels; and transferrin saturation and positively with total iron binding capacity (TIBC) and red cell distribution width. In group 2, patients' serum sTfR levels did not correlate with ferritin levels and TIBC, but had a significant relationship with other iron indices. Hb and serum sTfR levels had a significant inverse relationship in both groups; however, in group 1, there was no correlation between Hb and serum ferritin levels. In 30 patients of group 1, serum sTfR levels were significantly decreased with an increase in Hb levels after iron supplementation for 1 month. Conclusion: Serum sTfR levels significantly correlated with other diagnostic iron parameters of IDA and inversely correlated with an increase in Hb levels following iron supplementation. Therefore, serum sTfR levels can be a useful marker for the diagnosis and treatment of IDA in children.

Novel Trimeric Complex for Efficient Uptake of Plasmid Vector into HepG2 Cells

  • Joo, Jong-Hyuck;Park, Jong-Gu
    • 대한의생명과학회지
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    • 제9권2호
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    • pp.67-74
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    • 2003
  • Viral and non-viral vectors have been used in the delivery of genetic materials into animal cells and tissues, with each approach having pros and cons. Non-viral vectors have many useful merits such as easy preparation, low immunity and size tolerance of a transgene when compared to those of viral vectors. Delivery specificity may be achieved by complex formation between receptor ligands and a non-viral vector. In the present study, non-viral vector systems are investigated in an effort to find a practical delivery means for gene therapy, Receptor-ligand interaction between transferrin-receptor and transferrin was utilized for efficient gene transfer into cancer cells. A plasmid vector, pcDNA3 (LacZ) was ligated with a small duplexed oligo fragment in which a Biotin- VN$^{TM}$ phosphoramidite was placed in the middle of the oligo. The plasmid vector labeled by biotin was then conjugated with biotin-labeled transferrin via streptavidin. This trimeric conjugates were delivered to a hepatoma cell line, HepG2. The delivery efficiency of the trimeric conjugate was 2-fold higher than that of cationic liposomes used for transfection of a plasmid vector. These results demonstrate that a plasmid vector can be efficiently transferred into cells by forming a trimeric complex of plasmid vector-linker-ligand.

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사람 혈청 트란스페린수용체의 단클론 항체를 이용한 방사면역측정과 철영양상태의 진단 (Immunoradiometric Assay using Monoclonal Antibody Against Human Serum Transferrin Receptor for Diagnosis of Iron Deficiency)

  • 김승렬
    • Journal of Nutrition and Health
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    • 제29권9호
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    • pp.971-980
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    • 1996
  • The soluble transferrin receptor(TfR) in human serum has been shown recently to be a truncated form of intact membrane bound receptor containing most of the extracellular domain. We purfied the transferin-free TfR from human serum by immounoaffinity chromatography which produced the single protein identity in high resolution gel chormatography. The monoclonal antibodies(MAb) against purifed serum TfR were produced by fusion of spleen cells o fimmunized Balb/c mice and SP2 cells. Ten hybrids producing MAb specific for serum TfR were identifed and determine their iostypes. A immunoraddiometric assay (IRMA) for serum TfR was established using two monoclonal IgG1 antibodies as the coating and indicator antibodies on the bosis of their suitability in sandwich IRMA of serum TfR. The mean serum TfR levels in the 15 normal male, 15 normal female, and 19 iron-deficient subjects were 5.4$\pm$0.98, 4.6$\pm$0/76, and 18.0$\pm$12.8mg/1, respectively, and the difference in mean values between normal and iron deficient subjects was significant(p=0.0005). There existed the inverse logarithmic relationship(r=-0.9336, p<0.0001) between the serum TfR and ferritin levels.

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