Quantitative proteomic profiling of extracellular matrix and site-specific collagen post-translational modifications in an
3-HyP, 3-hydroxyproline
4-HyP, 4-hydroxyproline
AGC, automatic gain control
ANXA11, annexin A11
BGN, biglycan
COL1A1, collagen-I alpha 1 chain
Collagen
Collagen post-translational modifications
DCN, decorin
ECM, extracellular matrix
Extracellular matrix
FN1, fibronectin 1
G-HyK, galactosylhydroxylysine
GG-HyK, glucosylgalactosylhydroxylysine
HyK, hydroxylysine
HyP, hydroxyproline
ILD, interstitial lung disease
IPF, idiopathic pulmonary fibrosis
LH, lysyl hydroxylase
LOX(L), lysyl oxidase(-like)
LTBP2, latent-transforming growth factor β -binding protein 2
Lysyl glycosylation
Lysyl hydroxylation
P3H, prolyl-3-hydroxylase
P4H, prolyl-4-hydroxylase
PAI1, plasminogen activator inhibitor 1
PCA, principal component analysis
PLOD (LH), procollagen-lysine,2-oxoglutarate 5-dioxygenases (lysyl hydroxylases)
PTM, post-translational modification
Prolyl hydroxylation
Pulmonary fibrosis
SEMA7A, semaphorin 7a
TGF-β, transforming growth factor β
TGM2, transglutaminase 1
Transforming growth factor-β
VCAN, versican
Xaa, Xaa position in the Gly-Xaa-Yaa repeat in triple-helical collagen
Yaa, Yaa position in the Gly-Xaa-Yaa repeat in triple-helical collagen
α-SMA, α-smooth muscle actin
Journal
Matrix biology plus
ISSN: 2590-0285
Titre abrégé: Matrix Biol Plus
Pays: Netherlands
ID NLM: 101775320
Informations de publication
Date de publication:
Feb 2019
Feb 2019
Historique:
received:
24
11
2018
revised:
09
04
2019
accepted:
09
04
2019
entrez:
5
2
2021
pubmed:
13
4
2019
medline:
13
4
2019
Statut:
epublish
Résumé
Lung fibrosis is characterized by excessive deposition of extracellular matrix (ECM), in particular collagens, by fibroblasts in the interstitium. Transforming growth factor-β1 (TGF-β1) alters the expression of many extracellular matrix (ECM) components produced by fibroblasts, but such changes in ECM composition as well as modulation of collagen post-translational modification (PTM) levels have not been comprehensively investigated. Here, we performed mass spectrometry (MS)-based proteomics analyses to assess changes in the ECM deposited by cultured lung fibroblasts from idiopathic pulmonary fibrosis (IPF) patients upon stimulation with transforming growth factor β1 (TGF-β1). In addition to the ECM changes commonly associated with lung fibrosis, MS-based label-free quantification revealed profound effects on enzymes involved in ECM crosslinking and turnover as well as multiple positive and negative feedback mechanisms of TGF-β1 signaling. Notably, the ECM changes observed in this
Identifiants
pubmed: 33543004
doi: 10.1016/j.mbplus.2019.04.002
pii: S2590-0285(19)30004-3
pmc: PMC7852317
doi:
Types de publication
Journal Article
Langues
eng
Pagination
100005Subventions
Organisme : NIDDK NIH HHS
ID : T32 DK007569
Pays : United States
Organisme : NIDDK NIH HHS
ID : R24 DK103067
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK099467
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK065138
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK114809
Pays : United States
Informations de copyright
© 2019 Published by Elsevier B.V.
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