In vivo imaging of matrix metalloprotease 12 and matrix metalloprotease 13 activities in the mouse model of collagen-induced arthritis
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
In vivo imaging of matrix metalloprotease 12 and matrix metalloprotease 13 activities in the mouse model of collagen-induced arthritis. / Lim, Ngee Han; Meinjohanns, Ernst; Bou-Gharios, George; Gompels, Luke L.; Nuti, Elisa; Rossello, Armando; Devel, Laurent; Dive, Vincent; Meldal, Morten Peter; Nagase, Hideaki.
I: Arthritis & Rheumatism, Bind 66, Nr. 3, 2014, s. 589-598.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - In vivo imaging of matrix metalloprotease 12 and matrix metalloprotease 13 activities in the mouse model of collagen-induced arthritis
AU - Lim, Ngee Han
AU - Meinjohanns, Ernst
AU - Bou-Gharios, George
AU - Gompels, Luke L.
AU - Nuti, Elisa
AU - Rossello, Armando
AU - Devel, Laurent
AU - Dive, Vincent
AU - Meldal, Morten Peter
AU - Nagase, Hideaki
N1 - Copyright © 2013 American College of Rheumatology.
PY - 2014
Y1 - 2014
N2 - Objective. To develop enzyme activatable Förster resonance energy transfer (FRET) substrate probes to detect MMP-12 and MMP-13 activities in vivo in mouse models of inflammatory arthritis Methods. Peptidic FRET probes activated by MMP-12 and MMP-13 were reverse designed from inhibitors selected from a peptide phosphinic inhibitor library. Selectivity of the probes was demonstrated in vitro using MMP-1, MMP-2, MMP-3, MMP-12, and MMP-13. In vivo activation of the probe was tested in the zymosan-induced mouse model of inflammation and probe specificity was evaluated by the metalloprotease inhibitor GM6001 and specific synthetic inhibitors of MMP-12 and MMP-13. The probes were used to follow these enzyme activities in the collagen-induced arthritis (CIA) model in vivo. Results. The MMP-12- and MMP-13-activity probes (MMP12ap and MMP13ap, respectively) discriminated between the two enzymatic activities. The in vivo activation of these probes was inhibited by GM6001 and by their respective specific inhibitors. In the CIA model, MMP12ap activation peaked 5 days after disease onset and showed strong correlation with disease severity during this time (r = 0.85; p
AB - Objective. To develop enzyme activatable Förster resonance energy transfer (FRET) substrate probes to detect MMP-12 and MMP-13 activities in vivo in mouse models of inflammatory arthritis Methods. Peptidic FRET probes activated by MMP-12 and MMP-13 were reverse designed from inhibitors selected from a peptide phosphinic inhibitor library. Selectivity of the probes was demonstrated in vitro using MMP-1, MMP-2, MMP-3, MMP-12, and MMP-13. In vivo activation of the probe was tested in the zymosan-induced mouse model of inflammation and probe specificity was evaluated by the metalloprotease inhibitor GM6001 and specific synthetic inhibitors of MMP-12 and MMP-13. The probes were used to follow these enzyme activities in the collagen-induced arthritis (CIA) model in vivo. Results. The MMP-12- and MMP-13-activity probes (MMP12ap and MMP13ap, respectively) discriminated between the two enzymatic activities. The in vivo activation of these probes was inhibited by GM6001 and by their respective specific inhibitors. In the CIA model, MMP12ap activation peaked 5 days after disease onset and showed strong correlation with disease severity during this time (r = 0.85; p
U2 - 10.1002/art.38295
DO - 10.1002/art.38295
M3 - Journal article
C2 - 24285340
VL - 66
SP - 589
EP - 598
JO - Arthritis & Rheumatology
JF - Arthritis & Rheumatology
SN - 2326-5205
IS - 3
ER -
ID: 99351347