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PurposeDuring a follow-up program of patients admitted for COVID-19 at our non-ICU Unit, we found that 37% of them had decreased diffusing lung capacity for carbon monoxide (DLCO) 3–6 months after discharge. This prospective observational study aimed to evaluate the evolution of changes in DLCO and respiratory symptoms at the 1-year follow-up visit.MethodsSeventeen (mean age 71 years; 8 males) of 19 eligible patients (DLCO < 80% of predicted at the 3–6 months follow-up visit) completed the 1-year follow-up visit. One patient refused to participate and 1 patient had died 3 months earlier from myocardial infarction. The visit included a self-reported structured questionnaire, physical exam, blood tests, ECG, and spirometry with DLCO.ResultsMean DLCO was significantly improved at the 1-year visit (from 64% of predicted at 3–6 months to 74% of predicted at 1 year; P = 0.003). A clinically significant increase in DLCO (10% or greater) was observed in 11 patients (65%) with complete normalization (> 80% of predicted) in 6 (35%); in the other 6 (35%) it remained unchanged. The prevalence of exertional dyspnea (65–35%, P = 0.17), cough (24–18%, P = 1), and fatigue (76–35%, P = 0.04) decreased at the 1-year visit.ConclusionThese results suggest that DLCO and respiratory symptoms tend to normalize or improve 1 year after hospitalization for COVID-19 in most patients. However, there is also a non-negligible number of patients (about one-third) in whom respiratory changes persist and will need prolonged follow-up.

Fibrosis is the dramatic consequence of a dysregulated reparative process in which activated fibroblasts (myofibroblasts) and Transforming Growth Factor β1 (TGFβ1) play a central role. When exposed to TGFβ1, fibroblast and epithelial cells differentiate in myofibroblasts; in addition, endothelial cells may undergo endothelial-to-mesenchymal transition (EndoMT) and actively participate to the progression of fibrosis. Recently, the role of αv integrins, which recognize the Arg-Gly-Asp (RGD) tripeptide, in the release and signal transduction activation of TGFβ1 became evident. In this study, we present a class of triazole-derived RGD antagonists that interact with αvβ3 integrin. Above different compounds, the RGD-2 specifically interferes with integrin-dependent TGFβ1 EndoMT in Endothelial Colony-Forming Cells (ECPCs) derived from circulating Endothelial Precursor Cells (ECPCs). The RGD-2 decreases the amount of membrane-associated TGFβ1, and reduces both ALK5/TGFβ1 type I receptor expression and Smad2 phosphorylation in ECPCs. We found that RGD-2 antagonist reverts EndoMT, reducing α-smooth muscle actin (α-SMA) and vimentin expression in differentiated ECPCs. Our results outline the critical role of integrin in fibrosis progression and account for the opportunity of using integrins as target for anti-fibrotic therapeutic treatment.

Fibrosis is the dramatic consequence of a dysregulated reparative process in which activated fibroblasts (myofibroblasts) and Transforming Growth Factor beta 1 (TGF beta 1) play a central role. When exposed to TGF beta 1, fibroblast and epithelial cells differentiate in myofibroblasts; in addition, endothelial cells may undergo endothelial-to-mesenchymal transition (EndoMT) and actively participate to the progression of fibrosis. Recently, the role of alpha v integrins, which recognize the Arg-Gly-Asp (RGD) tripeptide, in the release and signal transduction activation of TGF beta 1 became evident. In this study, we present a class of triazole-derived RGD antagonists that interact with alpha v beta 3 integrin. Above different compounds, the RGD-2 specifically interferes with integrin-dependent TGF beta 1 EndoMT in Endothelial Colony-Forming Cells (ECPCs) derived from circulating Endothelial Precursor Cells (ECPCs). The RGD-2 decreases the amount of membrane-associated TGF beta 1, and reduces both ALK5/TGF beta 1 type I receptor expression and Smad2 phosphorylation in ECPCs. We found that RGD-2 antagonist reverts EndoMT, reducing alpha -smooth muscle actin ( alpha -SMA) and vimentin expression in differentiated ECPCs. Our results outline the critical role of integrin in fibrosis progression and account for the opportunity of using integrins as target for anti-fibrotic therapeutic treatment.

Fibrosis is the dramatic consequence of a dysregulated reparative process in which activated fibroblasts (myofibroblasts) and Transforming Growth Factor [beta]1 (TGF[beta]1) play a central role. When exposed to TGF[beta]1, fibroblast and epithelial cells differentiate in myofibroblasts; in addition, endothelial cells may undergo endothelial-to-mesenchymal transition (EndoMT) and actively participate to the progression of fibrosis. Recently, the role of [alpha]v integrins, which recognize the Arg-Gly-Asp (RGD) tripeptide, in the release and signal transduction activation of TGF[beta]1 became evident. In this study, we present a class of triazole-derived RGD antagonists that interact with [alpha]v[beta]3 integrin. Above different compounds, the RGD-2 specifically interferes with integrin-dependent TGF[beta]1 EndoMT in Endothelial Colony-Forming Cells (ECPCs) derived from circulating Endothelial Precursor Cells (ECPCs). The RGD-2 decreases the amount of membrane-associated TGF[beta]1, and reduces both ALK5/TGF[beta]1 type I receptor expression and Smad2 phosphorylation in ECPCs. We found that RGD-2 antagonist reverts EndoMT, reducing [alpha]-smooth muscle actin ([alpha]-SMA) and vimentin expression in differentiated ECPCs. Our results outline the critical role of integrin in fibrosis progression and account for the opportunity of using integrins as target for anti-fibrotic therapeutic treatment.