Fluorescent Probes of Tissue Transglutaminase Reveal Its Association with Arterial Stiffening
| Autor: | Pierre Moreau, Amina Mulani, Simon Moreau, Jeffrey W. Keillor, Nicolas Chabot |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Tissue transglutaminase
Guinea Pigs Kinetics Clinical Biochemistry 030204 cardiovascular system & hematology Stain Biochemistry 03 medical and health sciences 0302 clinical medicine GTP-Binding Proteins Fibrosis medicine.artery Drug Discovery medicine Animals Protein Glutamine gamma Glutamyltransferase 2 Amino Acid Sequence Enzyme Inhibitors Peptide sequence Molecular Biology Aorta Fluorescent Dyes 030304 developmental biology Pharmacology 0303 health sciences Transglutaminases biology Rhodamines Chemistry General Medicine medicine.disease Fluorescence Rats Disease Models Animal Hypertension Biophysics Arterial stiffness biology.protein Molecular Medicine Peptides |
| Zdroj: | Chemistry & Biology. 17(10):1143-1150 |
| ISSN: | 1074-5521 |
| DOI: | 10.1016/j.chembiol.2010.06.019 |
| Popis: | SummaryTissue transglutaminase (TG2) catalyzes the crosslinking of proteins. TG2 has been implicated in fibrosis and vascular calcification, both of which lead to a common feature of aging known as arterial stiffness. In order to probe the role of TG2 in arterial rigidification, we have prepared a fluorescent irreversible inhibitor as a probe for TG2 activity (RhodB-PGG-K(Acr)-LPF-OH). This probe was synthesized on solid support, characterized kinetically (kinact = 0.68 min-1, KI = 79 μM), and then used to stain the aorta from rats used as a model of isolated systolic hypertension (ISH). Interestingly, TG2 activity was thus shown to increase over 4 weeks of the hypertension model, corresponding with the previously observed increase in arterial stiffness. These results clearly suggest an association between TG2 and the phenomenon of arterial rigidification. |
| Databáze: | OpenAIRE |
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