Update publication information. Label-free proteomics study was applied to FLSs transfected by si-HAPLN1, or treated by rHAPLN1 (50 ng/ml) and their controls for 48 h by PTMBiolabs, Inc. (Hangzhou, China). Each concentration was tested with 3 biological replicates. LC−MS/MS proteomics analysis was performed on an EASY-nLC 1000 ultra-performance liquid chromatography (UPLC) system, followed by MS/MS using Q Exactive Plus (ThermoFisher Scientific, USA) coupled online to the UPLC system. The MS/MS data were retrieved by the Maxquant search engine (v1.6.6.0). A human database was searched (Swiss-Prot). The decoy database anti-library was used to reduce the false positive rate (FDR). The FDR was adjusted to < 1%, and the minimum score for modified peptides was set > 40. Proteins with a fold-change ≥1.50 or ≤0.67 between si-HAPLN1, rHAPLN1 and their controls were considered as expression significant. Based on the protein sequence alignment method, the protein domain functions were defined by InterProScan (http://www.ebi.ac.uk/interpro/).