Time-lapse monitoring of TLR2 ligand internalization with newly developed fluorescent probes

Yohei Arai; Kouhei Yokoyama; Yuki Kawahara; Qi Feng; Ippei Ohta; Atsushi Shimoyama; Shinsuke Inuki; Koichi Fukase; Kazuya Kabayama; Yukari Fujimoto

doi:10.1039/c7ob03205f

Time-lapse monitoring of TLR2 ligand internalization with newly developed fluorescent probes

Yohei Arai, Kouhei Yokoyama, Yuki Kawahara, Qi Feng, Ippei Ohta, Atsushi Shimoyama, Shinsuke Inuki, Koichi Fukase, Kazuya Kabayama, Yukari Fujimoto

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

As a mammalian toll-like receptor family member protein, TLR2 recognizes lipoproteins from bacteria and modulates the immune response by inducing the expression of various cytokines. We have developed fluorescence-labeled TLR2 ligands with either hydrophilic or hydrophobic fluorescence groups. The labeled ligands maintained the inflammatory IL-6 induction activity and enabled us to observe the internalization and colocalization of the TLR2 ligands using live-cell imaging. The time-lapse monitoring in the live-cell imaging of the fluorescence-labeled TLR2 ligand showed that TLR2/CD14 expression in the host cells enhanced the internalization of TLR2 ligand molecules.

Original language	English
Pages (from-to)	3824-3830
Number of pages	7
Journal	Organic and Biomolecular Chemistry
Volume	16
Issue number	20
DOIs	https://doi.org/10.1039/c7ob03205f
Publication status	Published - 2018

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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title = "Time-lapse monitoring of TLR2 ligand internalization with newly developed fluorescent probes",

abstract = "As a mammalian toll-like receptor family member protein, TLR2 recognizes lipoproteins from bacteria and modulates the immune response by inducing the expression of various cytokines. We have developed fluorescence-labeled TLR2 ligands with either hydrophilic or hydrophobic fluorescence groups. The labeled ligands maintained the inflammatory IL-6 induction activity and enabled us to observe the internalization and colocalization of the TLR2 ligands using live-cell imaging. The time-lapse monitoring in the live-cell imaging of the fluorescence-labeled TLR2 ligand showed that TLR2/CD14 expression in the host cells enhanced the internalization of TLR2 ligand molecules.",

author = "Yohei Arai and Kouhei Yokoyama and Yuki Kawahara and Qi Feng and Ippei Ohta and Atsushi Shimoyama and Shinsuke Inuki and Koichi Fukase and Kazuya Kabayama and Yukari Fujimoto",

note = "Funding Information: This work was supported by Grants-in-Aid for Scientific Research, KAKENHI (Y. F.; JP26102732, JP26282211, JP17H02207, JP17H05800 and JP16H01162; K. F.; JP26882036, JP23241074, JP15H05836, and JP16H01885) by MEXT-Supported Program (JSPS) for the Strategic Research Foundation at Private Universities (K. K.; S1411010), by NEXT-program from JSPS (Y. F.; LR025), Mizutani Foundation for Glycoscience (Y. F.), Mishima Kaiun Memorial Foundation (Y. F.) and Takeda Science Foundation (Y. F.). Publisher Copyright: {\textcopyright} 2018 The Royal Society of Chemistry.",

year = "2018",

doi = "10.1039/c7ob03205f",

language = "English",

volume = "16",

pages = "3824--3830",

journal = "Organic and Biomolecular Chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

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TY - JOUR

T1 - Time-lapse monitoring of TLR2 ligand internalization with newly developed fluorescent probes

AU - Arai, Yohei

AU - Yokoyama, Kouhei

AU - Kawahara, Yuki

AU - Feng, Qi

AU - Ohta, Ippei

AU - Shimoyama, Atsushi

AU - Inuki, Shinsuke

AU - Fukase, Koichi

AU - Kabayama, Kazuya

AU - Fujimoto, Yukari

N1 - Funding Information: This work was supported by Grants-in-Aid for Scientific Research, KAKENHI (Y. F.; JP26102732, JP26282211, JP17H02207, JP17H05800 and JP16H01162; K. F.; JP26882036, JP23241074, JP15H05836, and JP16H01885) by MEXT-Supported Program (JSPS) for the Strategic Research Foundation at Private Universities (K. K.; S1411010), by NEXT-program from JSPS (Y. F.; LR025), Mizutani Foundation for Glycoscience (Y. F.), Mishima Kaiun Memorial Foundation (Y. F.) and Takeda Science Foundation (Y. F.). Publisher Copyright: © 2018 The Royal Society of Chemistry.

PY - 2018

Y1 - 2018

N2 - As a mammalian toll-like receptor family member protein, TLR2 recognizes lipoproteins from bacteria and modulates the immune response by inducing the expression of various cytokines. We have developed fluorescence-labeled TLR2 ligands with either hydrophilic or hydrophobic fluorescence groups. The labeled ligands maintained the inflammatory IL-6 induction activity and enabled us to observe the internalization and colocalization of the TLR2 ligands using live-cell imaging. The time-lapse monitoring in the live-cell imaging of the fluorescence-labeled TLR2 ligand showed that TLR2/CD14 expression in the host cells enhanced the internalization of TLR2 ligand molecules.

AB - As a mammalian toll-like receptor family member protein, TLR2 recognizes lipoproteins from bacteria and modulates the immune response by inducing the expression of various cytokines. We have developed fluorescence-labeled TLR2 ligands with either hydrophilic or hydrophobic fluorescence groups. The labeled ligands maintained the inflammatory IL-6 induction activity and enabled us to observe the internalization and colocalization of the TLR2 ligands using live-cell imaging. The time-lapse monitoring in the live-cell imaging of the fluorescence-labeled TLR2 ligand showed that TLR2/CD14 expression in the host cells enhanced the internalization of TLR2 ligand molecules.

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DO - 10.1039/c7ob03205f

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AN - SCOPUS:85047553363

VL - 16

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EP - 3830

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

SN - 1477-0520

IS - 20

ER -

Time-lapse monitoring of TLR2 ligand internalization with newly developed fluorescent probes

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