Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 266-281 |
| Seitenumfang | 16 |
| Fachzeitschrift | Biotechnology journal |
| Jahrgang | 9 |
| Ausgabenummer | 2 |
| Publikationsstatus | Veröffentlicht - 4 Feb. 2014 |
| Extern publiziert | Ja |
Abstract
The continuous detection of enzyme activities and their application in medical diagnostics is one of the challenges in the translational sciences. Proteinases represent one of the largest groups of enzymes in the human genome and many diseases are based on malfunctions of proteolytic activity. Fluorescent sensors may shed light on regular and irregular proteinase activity in vitro and in vivo and provide a deeper insight into the function of these enzymes and their role in pathophysiological processes. The focus of this review is on Förster resonance energy transfer (FRET)-based proteinase sensors and reporters because these probes are most likely to provide quantitative data. The medical relevance of proteinases are discussed using lung diseases as a prominent example. Probe design and probe targeting are described and fluorescent probe development for disease-relevant proteinases, including matrix-metalloproteinases, cathepsins, caspases, and other selected proteinases, is reviewed.
ASJC Scopus Sachgebiete
- Immunologie und Mikrobiologie (insg.)
- Angewandte Mikrobiologie und Biotechnologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularmedizin
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in: Biotechnology journal, Jahrgang 9, Nr. 2, 04.02.2014, S. 266-281.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - FRET-based and other fluorescent proteinase probes
AU - Hu, Hai Yu
AU - Gehrig, Stefanie
AU - Reither, Gregor
AU - Subramanian, Devaraj
AU - Mall, Marcus A.
AU - Plettenburg, Oliver
AU - Schultz, Carsten
PY - 2014/2/4
Y1 - 2014/2/4
N2 - The continuous detection of enzyme activities and their application in medical diagnostics is one of the challenges in the translational sciences. Proteinases represent one of the largest groups of enzymes in the human genome and many diseases are based on malfunctions of proteolytic activity. Fluorescent sensors may shed light on regular and irregular proteinase activity in vitro and in vivo and provide a deeper insight into the function of these enzymes and their role in pathophysiological processes. The focus of this review is on Förster resonance energy transfer (FRET)-based proteinase sensors and reporters because these probes are most likely to provide quantitative data. The medical relevance of proteinases are discussed using lung diseases as a prominent example. Probe design and probe targeting are described and fluorescent probe development for disease-relevant proteinases, including matrix-metalloproteinases, cathepsins, caspases, and other selected proteinases, is reviewed.
AB - The continuous detection of enzyme activities and their application in medical diagnostics is one of the challenges in the translational sciences. Proteinases represent one of the largest groups of enzymes in the human genome and many diseases are based on malfunctions of proteolytic activity. Fluorescent sensors may shed light on regular and irregular proteinase activity in vitro and in vivo and provide a deeper insight into the function of these enzymes and their role in pathophysiological processes. The focus of this review is on Förster resonance energy transfer (FRET)-based proteinase sensors and reporters because these probes are most likely to provide quantitative data. The medical relevance of proteinases are discussed using lung diseases as a prominent example. Probe design and probe targeting are described and fluorescent probe development for disease-relevant proteinases, including matrix-metalloproteinases, cathepsins, caspases, and other selected proteinases, is reviewed.
KW - Activity-based probes
KW - Cathepsins
KW - Cell targeting
KW - Chronic inflammatory lung disease
KW - Matrix metalloproteinases
UR - http://www.scopus.com/inward/record.url?scp=84895076669&partnerID=8YFLogxK
U2 - 10.1002/biot.201300201
DO - 10.1002/biot.201300201
M3 - Article
C2 - 24464820
AN - SCOPUS:84895076669
VL - 9
SP - 266
EP - 281
JO - Biotechnology journal
JF - Biotechnology journal
SN - 1860-6768
IS - 2
ER -