Structure and proteolytic susceptibility of the inhibitory C-terminal tail of cardiac troponin I.
Calpain
Intrinsically disordered protein
Ischemia-reperfusion injury
Mass spectrometry
Matrix metalloproteinase-2
Myocardial infarction
Myocardial stunning
Nuclear magnetic resonance (NMR) spectroscopy
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
14
09
2018
revised:
22
11
2018
accepted:
14
01
2019
pubmed:
20
1
2019
medline:
4
12
2019
entrez:
20
1
2019
Statut:
ppublish
Résumé
Cardiac troponin I (cTnI) has two flexible tails that control the cardiac cycle. The C-terminal tail, cTnI Soluble fragments of cTnI containing its N- and C-terminal tails, cTnI cTnI Both N-terminal and C-terminal tails of cTnI are susceptible to cleavage by MMP-2 and calpain-2. Binding to cTnC or actin confers some protection to proteolysis, which can be understood in terms of their interactions as probed by NMR studies. cTnI is an important marker of intracellular proteolysis in cardiomyocytes, given its many protease-specific cut sites, high natural abundance, indispensable functional role, and clinical use as gold standard biomarker of myocardial injury.
Sections du résumé
BACKGROUND
Cardiac troponin I (cTnI) has two flexible tails that control the cardiac cycle. The C-terminal tail, cTnI
METHODS
Soluble fragments of cTnI containing its N- and C-terminal tails, cTnI
RESULTS
cTnI
CONCLUSIONS
Both N-terminal and C-terminal tails of cTnI are susceptible to cleavage by MMP-2 and calpain-2. Binding to cTnC or actin confers some protection to proteolysis, which can be understood in terms of their interactions as probed by NMR studies.
GENERAL SIGNIFICANCE
cTnI is an important marker of intracellular proteolysis in cardiomyocytes, given its many protease-specific cut sites, high natural abundance, indispensable functional role, and clinical use as gold standard biomarker of myocardial injury.
Identifiants
pubmed: 30659884
pii: S0304-4165(19)30014-5
doi: 10.1016/j.bbagen.2019.01.008
pii:
doi:
Substances chimiques
Actins
0
Recombinant Proteins
0
Troponin I
0
Calpain
EC 3.4.22.-
CAPN2 protein, human
EC 3.4.22.53
Matrix Metalloproteinase 2
EC 3.4.24.24
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
661-671Subventions
Organisme : CIHR
Pays : Canada
Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.