• 제목/요약/키워드: bovine lactoferricin

검색결과 8건 처리시간 0.021초

Determination of the minimal sequence of bovine lactoferricin responsible for apoptosis induction

  • Yoo, Yung-Choon;Lee, Kyung-Bok;Lee, Hoi-Young
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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    • pp.134.2-135
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    • 2003
  • We examined the minimal amino acid sequence of bovine lactoferricin (Lfcin-B), a cationic peptide corresponding to residues 17-41 near the N-terminus of bovine lactoferrin, to induce apoptosis in THP-l human monocytic leukemic cells using synthetic peptides. A synthetic peptide (Lfc-17/29, amino acid sequence; FKCRRWQWRMKKL) which is consist of 13 amino acids near the N-terminus of Lfcin-B induced cell death in THP-1 cells in a dose-dependent manner, showing apparent apoptotic changes such as hypodiploid forms of genomic DNA and apoptotic DNA fragmentation. (omitted)

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미생물을 이용한 우유 유래 항균펩타이드(락토페리신)의 생산 (Production of Milk-Originated Antimicrobial Peptide, Lactoferricin, in E. coli)

  • 강대경
    • Journal of Dairy Science and Biotechnology
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    • 제25권2호
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    • pp.17-20
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    • 2007
  • Bovine lactoferricin(LFcin B) is a peptide of 25 amino acids that originated from the N terminus of bovine lactoferrin, and is characterized as having potent antimicrobial activity against bacteria, fungi, protozoa and viruses. But, direct expression of Lfcin B is lethal to Escherichia coli. For the efficient production of Lfcin B in microorganism, we developed an expression system in which the gene for cationic Lfcin B was fused to an anionic peptide gene, and successfully expressed the concatemeric fusion gene in E. coli. The purified recombinant Lfcin B was found to have antimicrobial activity, as chemically synthesized Lfcin B peptide does.

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미생물을 이용한 우유 유래 항균펩타이드(락토페리신)의 생산 (Production of milk-originated antimicrobial peptide, lactoferricin, in E. coli)

  • 강대경
    • 한국유가공학회:학술대회논문집
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    • 한국유가공기술과힉회 2007년도 추계학술발표대회
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    • pp.13-20
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    • 2007
  • Bovine lactoferricin(LFcin B) is a peptide of 25 amino acids that originated from the N terminus of bovine lactoferrin, and is characterized as having potent antimicrobial activity against bacteria, fungi, protozoa and viruses. But, direct expression of Lfcin B is lethal to Escherichia coli. For the efficient production of Lfcin B in E. coli, we developed an expression system in which the gene for cationic Lfcin B was fused to an anionic peptide gene, and successfully expressed the concatemeric fusion gene in E. coli. The purified recombinant Lfcin B was found to have antimicrobial activity, as the native Lfcin B peptide does.

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Involvement of G1 arrest and caspase-3 activation in apoptosis induced by bovine lactoferricin

  • Yoo, Yung-Choon;Lee, Kyung-Bok
    • 대한약학회:학술대회논문집
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    • 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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    • pp.325.2-325.2
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    • 2002
  • We investigated the effect of bovine lactoferricin (Lfcin-B) on cell cycle regulation and caspase activation in tumor cells. Treatment with Lfcin-B resulted in the production of intracellular reactive oxygen species (ROS) during apoptosis of THP-1 cells. Biochemical analysis revealed that Lfcin-B-induced apoptosis. the cell cycle arrest and caspase activation were completely abrogated by addition of an antioxidant such as N-acetylcysteine(NAC). (omitted)

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HC11 세포에서 인체 락토페리신의 발현 (Expression of Human Lactoferricin in HC11 Cells)

  • 남명수
    • 농업과학연구
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    • 제28권2호
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    • pp.92-98
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    • 2001
  • 락토페리신은 다양한 생리활성을 나타내는 락토페린(약 80kD)에서 유래된 항균성펩타이드 분획물(5kD)이다. 마우스HC11유선상피세포에서 인체 락토페리신의 발현은 bovine beta-casein을 promotor로 하고 인체 락토페리신 cDNA를 삽입하여 제작한 pBL1-cin발현벡타를 이용하였다. 이 발현벡타를 이용하여 인체 락토페리신 발현여부를 RT-PCR, northern blot, dot blot분석을 통하여 확인하였다. pBL1-cin 발현백타를 HC11세포에 transfection 하여 얻은 RNA를 이용하여 RT-PCR를 한 결과 150bp의 크기로 확인되었고 Northern blot 분석결과는 약 2.3 kb의 크기로 확인되었다. 인체 락토페린 polyclonal항체를 이용하여 dot blot한 결과 인체 락토페리신이 분비됨을 확인하였다.

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Bovine Lactoferricin Induces Intestinal Epithelial Cell Activation through Phosphorylation of FAK and Paxillin and Prevents Rotavirus Infection

  • Jeong, Ye Young;Lee, Ga Young;Yoo, Yung Choon
    • Journal of Microbiology and Biotechnology
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    • 제31권8호
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    • pp.1175-1182
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    • 2021
  • We investigated the effect of bovine lactoferricin (Lfcin-B), a peptide derived from bovine lactoferrin, on activation of intestinal epithelial cells in IEC-6 intestinal cell, and protection against in vivo rotavirus (RV) infection. Treatment with Lfcin-B significantly enhanced the growth of IEC-6 cells and increased their capacity for attachment and spreading in culture plates. Also, Lfcin-B synergistically augmented the binding of IEC-6 cells to laminin, a component of the extracellular matrix (ECM). In the analysis of the intracellular mechanism related to Lfcin-B-induced activation of IEC-6 cells, this peptide upregulated tyrosine-dependent phosphorylation of focal adhesion kinase (FAK) and paxillin, which are intracellular proteins associated with cell adhesion, spreading, and signal transduction during cell activation. An experiment using synthetic peptides with various sequences of amino acids revealed that a sequence of 9 amino acids (FKCRRWQWR) corresponding to 17-25 of the N-terminus of Lfcin-B is responsible for the epithelial cell activation. In an in vivo experiment, treatment with Lfcin-B one day before RV infection effectively prevented RV-induced diarrhea and significantly reduced RV titers in the bowels of infected mice. These results suggest that Lfcin-B plays meaningful roles in the maintenance and repair of intestinal mucosal tissues, as well as in protecting against intestinal infection by RV. Collectively, Lfcin-B is a promising candidate with potential applications in drugs or functional foods beneficial for intestinal health and mucosal immunity.

외부유전자가 도입된 체세포를 이용한 소 형질전환 복제란 생산 (Production of Bovine Transgenic Embryos Derived from Non-transfected and Transfected Adult Cells)

  • J. K. Cho;M.M.U. Bhuiyan;G. Jang;Park, E. S.;J. M. Lim;S. K. Kang;Lee, B. C.;W. S. Hwang
    • 한국수정란이식학회지
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    • 제17권2호
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    • pp.109-115
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    • 2002
  • The present study was conducted for the production of transgenic cloned cows those secrete human lactoferricin into milk by somatic cell nuclear transfer (NT). To estimate detrimental effects of gene transfection on transgenic cloned embryo production, development rates of NT embryos were compared between transfected and non-transfected cumulus and ear fibroblast cells. An expression plasmid for human lactofericin (pbeta-LFC) was constructed by inserting a bovine beta-casein promoter, a green fluorescent protein (GFP) marker gene, and human lactoferricin target gene into a pcDNA3 plasmid. Two bovine somatic cell lines (cumulus cell and ear fibroblast) were established and transfected with the expression plasmid using a liposomal transfection reagent, Fugene6 as a carrier. Cumulus cell and ear fibroblast were transfected at the passage of 2 to 4, trypsinized and GFP-expressing cells were randomly selected and used for somatic cell NT. Developmental competences (rates of fusion, cleavage, and blastocyst formation) in bovine transgenic somatic cell NT embryos reconstructed with non-transfectecd cells were significantly higher than those from transfected cells in cumulus cell and ear fibroblast (P<0.05). This study indicated that transfection of done. cell has detrimental effect on embryo development in bovine transgenic NT.

Sensitivity of Pseudomonas syringae to Bovine Lactoferrin Hydrolysates and Identification of a Novel Inhibitory Peptide

  • Kim, Woan-Sub;Kim, Pyeung-Hyeun;Shimazaki, Kei-ichi
    • 한국축산식품학회지
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    • 제36권4호
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    • pp.487-493
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    • 2016
  • The antimicrobial activity of bovine lactoferrin hydrolysates (bLFH) was measured against Pseudomonas strains (P. syringae and P. fluorescens) in vitro. To compare susceptibility to bLFH, minimal inhibitory concentration (MIC) values were determined using chemiluminescence assays and paper disc plate assays. Antimicrobial effect against P. fluorescens was not observed by either assay, suggesting that bLFH did not exhibit antimicrobial activity against P. fluorescens. However, a significant inhibition of P. syringae growth was observed in the presence of bLFH. The addition of bLFH in liquid or solid medium inhibited growth of P. syringae in a dose-dependent manner. Furthermore, a bLFH peptide with antimicrobial activity toward P. syringae was isolated and identified. The N-terminal amino acid sequences of thus obtained antimicrobial bLFH peptides were analyzed by a protein sequencer and were found to be Leu-Arg-Ile-Pro-Ser-Lys-Val-Asp-Ser-Ala and Phe-Lys-Cys-Arg-Arg-Trp-Gln-Trp-Arg-Met. The latter peptide sequence is known to be characteristic of lactoferricin. Therefore, in the present study, we identified a new antimicrobial peptide against P. syringae, present within the N-terminus and possessing the amino acid sequence of Leu-Arg-Ile-Pro-Ser-Lys-Val-Asp-Ser-Ala.