In vivo monitoring of angiogenesis in a mouse hindlimb ischemia model using fluorescent peptide-based probes

Subin Park, Jangwook Lee, Mi hee Jo, Jin Hee Na, Sung Gurl Park, Hyeon Ki Jang, Sun Woong Kang, Jong Ho Kim, Byung Soo Kim, Jae Hyung Park, Ick Chan Kwon, Ju Hee Ryu, Kwang Meyung Kim

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Vascular endothelial growth factor receptor (VEGFR) and matrix metalloproteinase (MMP) are up-regulated in ischemic tissue and play pivotal roles in promoting angiogenesis. The purpose of the present study was to evaluate two fluorophore-conjugated peptide probes specific to VEGFR and MMP for dual-targeted in vivo monitoring of angiogenesis in a murine model of hindlimb ischemia. To this end, VEGFR-Probe and MMP-Probe were developed by conjugating distinct near-infrared fluorophores to VEGFR-binding and MMP substrate peptides, respectively. VEGFR-Probe exhibited specific binding to VEGFR on HUVECs, and self-quenched MMP-Probe produced strong fluorescence intensity in the presence of MMPs in vitro. Subsequently, VEGFR-Probe and MMP-Probe were successfully utilized for time course in vivo visualization of VEGFR or MMP, respectively. Simultaneous visualization provided information regarding the spatial distribution of these proteins, including areas of co-localization. This dual-targeted in vivo imaging approach will be useful for understanding the detailed mechanism of angiogenesis and for evaluating therapeutic angiogenesis.

Original languageEnglish
Pages (from-to)1-14
Number of pages14
JournalAmino Acids
DOIs
Publication statusAccepted/In press - 2016 Apr 20

Fingerprint

Vascular Endothelial Growth Factor Receptor
Hindlimb
Matrix Metalloproteinases
Ischemia
Peptides
Monitoring
Fluorophores
Visualization
Spatial distribution
Fluorescence
Tissue
Infrared radiation
Imaging techniques
Substrates

Keywords

  • Angiogenesis
  • Fluorescence imaging
  • Matrix metalloproteinase
  • Molecular imaging
  • Vascular endothelial growth factor receptor

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

Cite this

In vivo monitoring of angiogenesis in a mouse hindlimb ischemia model using fluorescent peptide-based probes. / Park, Subin; Lee, Jangwook; Jo, Mi hee; Na, Jin Hee; Park, Sung Gurl; Jang, Hyeon Ki; Kang, Sun Woong; Kim, Jong Ho; Kim, Byung Soo; Park, Jae Hyung; Kwon, Ick Chan; Ryu, Ju Hee; Kim, Kwang Meyung.

In: Amino Acids, 20.04.2016, p. 1-14.

Research output: Contribution to journalArticle

Park, S, Lee, J, Jo, MH, Na, JH, Park, SG, Jang, HK, Kang, SW, Kim, JH, Kim, BS, Park, JH, Kwon, IC, Ryu, JH & Kim, KM 2016, 'In vivo monitoring of angiogenesis in a mouse hindlimb ischemia model using fluorescent peptide-based probes', Amino Acids, pp. 1-14. https://doi.org/10.1007/s00726-016-2225-0
Park, Subin ; Lee, Jangwook ; Jo, Mi hee ; Na, Jin Hee ; Park, Sung Gurl ; Jang, Hyeon Ki ; Kang, Sun Woong ; Kim, Jong Ho ; Kim, Byung Soo ; Park, Jae Hyung ; Kwon, Ick Chan ; Ryu, Ju Hee ; Kim, Kwang Meyung. / In vivo monitoring of angiogenesis in a mouse hindlimb ischemia model using fluorescent peptide-based probes. In: Amino Acids. 2016 ; pp. 1-14.
@article{ae0e62a8b64142e39bbd68ef8436db45,
title = "In vivo monitoring of angiogenesis in a mouse hindlimb ischemia model using fluorescent peptide-based probes",
abstract = "Vascular endothelial growth factor receptor (VEGFR) and matrix metalloproteinase (MMP) are up-regulated in ischemic tissue and play pivotal roles in promoting angiogenesis. The purpose of the present study was to evaluate two fluorophore-conjugated peptide probes specific to VEGFR and MMP for dual-targeted in vivo monitoring of angiogenesis in a murine model of hindlimb ischemia. To this end, VEGFR-Probe and MMP-Probe were developed by conjugating distinct near-infrared fluorophores to VEGFR-binding and MMP substrate peptides, respectively. VEGFR-Probe exhibited specific binding to VEGFR on HUVECs, and self-quenched MMP-Probe produced strong fluorescence intensity in the presence of MMPs in vitro. Subsequently, VEGFR-Probe and MMP-Probe were successfully utilized for time course in vivo visualization of VEGFR or MMP, respectively. Simultaneous visualization provided information regarding the spatial distribution of these proteins, including areas of co-localization. This dual-targeted in vivo imaging approach will be useful for understanding the detailed mechanism of angiogenesis and for evaluating therapeutic angiogenesis.",
keywords = "Angiogenesis, Fluorescence imaging, Matrix metalloproteinase, Molecular imaging, Vascular endothelial growth factor receptor",
author = "Subin Park and Jangwook Lee and Jo, {Mi hee} and Na, {Jin Hee} and Park, {Sung Gurl} and Jang, {Hyeon Ki} and Kang, {Sun Woong} and Kim, {Jong Ho} and Kim, {Byung Soo} and Park, {Jae Hyung} and Kwon, {Ick Chan} and Ryu, {Ju Hee} and Kim, {Kwang Meyung}",
year = "2016",
month = "4",
day = "20",
doi = "10.1007/s00726-016-2225-0",
language = "English",
pages = "1--14",
journal = "Amino Acids",
issn = "0939-4451",
publisher = "Springer Wien",

}

TY - JOUR

T1 - In vivo monitoring of angiogenesis in a mouse hindlimb ischemia model using fluorescent peptide-based probes

AU - Park, Subin

AU - Lee, Jangwook

AU - Jo, Mi hee

AU - Na, Jin Hee

AU - Park, Sung Gurl

AU - Jang, Hyeon Ki

AU - Kang, Sun Woong

AU - Kim, Jong Ho

AU - Kim, Byung Soo

AU - Park, Jae Hyung

AU - Kwon, Ick Chan

AU - Ryu, Ju Hee

AU - Kim, Kwang Meyung

PY - 2016/4/20

Y1 - 2016/4/20

N2 - Vascular endothelial growth factor receptor (VEGFR) and matrix metalloproteinase (MMP) are up-regulated in ischemic tissue and play pivotal roles in promoting angiogenesis. The purpose of the present study was to evaluate two fluorophore-conjugated peptide probes specific to VEGFR and MMP for dual-targeted in vivo monitoring of angiogenesis in a murine model of hindlimb ischemia. To this end, VEGFR-Probe and MMP-Probe were developed by conjugating distinct near-infrared fluorophores to VEGFR-binding and MMP substrate peptides, respectively. VEGFR-Probe exhibited specific binding to VEGFR on HUVECs, and self-quenched MMP-Probe produced strong fluorescence intensity in the presence of MMPs in vitro. Subsequently, VEGFR-Probe and MMP-Probe were successfully utilized for time course in vivo visualization of VEGFR or MMP, respectively. Simultaneous visualization provided information regarding the spatial distribution of these proteins, including areas of co-localization. This dual-targeted in vivo imaging approach will be useful for understanding the detailed mechanism of angiogenesis and for evaluating therapeutic angiogenesis.

AB - Vascular endothelial growth factor receptor (VEGFR) and matrix metalloproteinase (MMP) are up-regulated in ischemic tissue and play pivotal roles in promoting angiogenesis. The purpose of the present study was to evaluate two fluorophore-conjugated peptide probes specific to VEGFR and MMP for dual-targeted in vivo monitoring of angiogenesis in a murine model of hindlimb ischemia. To this end, VEGFR-Probe and MMP-Probe were developed by conjugating distinct near-infrared fluorophores to VEGFR-binding and MMP substrate peptides, respectively. VEGFR-Probe exhibited specific binding to VEGFR on HUVECs, and self-quenched MMP-Probe produced strong fluorescence intensity in the presence of MMPs in vitro. Subsequently, VEGFR-Probe and MMP-Probe were successfully utilized for time course in vivo visualization of VEGFR or MMP, respectively. Simultaneous visualization provided information regarding the spatial distribution of these proteins, including areas of co-localization. This dual-targeted in vivo imaging approach will be useful for understanding the detailed mechanism of angiogenesis and for evaluating therapeutic angiogenesis.

KW - Angiogenesis

KW - Fluorescence imaging

KW - Matrix metalloproteinase

KW - Molecular imaging

KW - Vascular endothelial growth factor receptor

UR - http://www.scopus.com/inward/record.url?scp=84964374593&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84964374593&partnerID=8YFLogxK

U2 - 10.1007/s00726-016-2225-0

DO - 10.1007/s00726-016-2225-0

M3 - Article

SP - 1

EP - 14

JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

ER -