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Hyaluronan And Proteoglycan Link Protein 1 (HAPLN1) promotes Proliferation and Pro-inflammatory phenotype but not mobility of Fibroblast-like Synoviocytes

ABSTRACT: Hyaluronan And Proteoglycan Link Protein 1 (HAPLN1) promotes Proliferation and Pro-inflammatory phenotype but not mobility of Fibroblast-like Synoviocytes

PROVIDER: PRJNA825502 | ENA |

REPOSITORIES: ENA

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Hyaluronan And Proteoglycan Link Protein 1 (HAPLN1) promotes Proliferation and Pro-inflammatory phenotype but not mobility of Fibroblast-like Synoviocytes

Project description:Objectives: HAPLN1 stabilize the macromolecular structure of the extracellular matrix (ECM) and its expression is increased in a few types of musculoskeletal diseases including rheumatoid arthritis (RA). However, its functions are obscure. Methods: Here, how HAPLN1 contributes to the viability, proliferation, mobility and pro-inflammatory phenotype of RA-FLSs was investigated using small interfering RNA (siHAPLN1), over-expression vector (HAPLN1OE) and a recombinant HAPLN1 (rHAPLN1) protein. Results: Interestingly, HAPLN1 promoted proliferation but inhibited migration of RA-FLSs. Earlier we reported the function of metformin, an AMPK activator, in the inhibition of FLSs activation but promotion of HAPLN1 secretion. In this study, we confirmed the findings of up-regulated HAPLN1 in RA patients, and it is positively correlated with AMPK. Both si-HAPLN1 and HAPLN1OE treatment has down-regulated the expression of AMPK-ɑ gene but the levels of phosphorylated AMPK-ɑ were found to be up-regulated in RA-FLSs. Furthermore, si-HAPLN1 had down-regulated the gene and protein expression of proinflammatory factors like TNF-ɑ, MMPs and IL-6, while HAPLN1OE up-regulated their levels. qPCR assay also indicated down regulated TGF-β, ACAN, Fibronectin, collagen Ⅱ, and Ki-67 by si-HAPLN1 treatment, while up-regulated ACAN, Ki-67 and down regulated cyclin-D1 by HAPLN1OE treatment. Proteomics of si-HAPLN1, rHAPLN1 and mRNA-Seq analysis of rHAPLN1 confirmed the functions of HAPLN1 in the activation of inflammation, proliferation, increased cell adhesion, and strengthening of ECM function. Conclusions: Collectively, these findings demonstrate HAPLN1 function in promoting proliferation and pro-inflammatory phenotype of RA-FLSs, which in turn could contribute to RA pathogenesis.

2022-06-22 | GSE200597 | GEO

Hyaluronan And Proteoglycan Link Protein 1 (HAPLN1) promotes Proliferation and Pro-inflammatory phenotype but not mobility of Fibroblast-like Synoviocytes

Project description: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/).

2022-04-08 | PXD033131 | iProX

Cultured cardiomyocytes treated with hyaluronan

Project description:Investigation of the role of hyaluronan in cardiomyocytes . The aims of the study were to determine if cardiomyocytes are capable of detecting hyaluronan and if then intrecellular signaling causes changes in gene expression. The study showed that cardiomyocytes can bind hyaluronan with following change in gene expression.

2011-11-01 | GSE21675 | GEO

Reduced expression of the hyaluronan and proteoglycan link proteins in malignant gliomas.

Project description: Not available

| S-EPMC2785343 | biostudies-literature

TNF treated Synoviocytes

Project description:Time series of human arthritic synoviocytes treated with TNFalpha. Keywords: time-course

2003-07-03 | GSE516 | GEO

Loss of Hyaluronan and Proteoglycan Link Protein-1 Induces Tumorigenesis in Colorectal Cancer.

Project description: Not available

| S-EPMC8710468 | biostudies-literature

RNA expression profiles in fibroblast-like synoviocytes from rheumatoid arthritis patients and trauma patients

Project description:LncRNA and mRNA microarrays were performed to identify differentially expressed lncRNAs and mRNAs in fibroblast-like synoviocytes from rheumatoid arthritis patients compared with fibroblast-like synoviocytes from trauma patients. Fibroblast-like synoviocytes were isolated from synovial tissues. LncRNA and mRNA microarrays were performed using fibroblast-like synoviocytes at passage 3.

2016-06-10 | E-GEOD-83147 | biostudies-arrayexpress

Transcription profiling of human arthritic TNF treated synoviocytes

Project description:Time series of human arthritic synoviocytes treated with TNFalpha.

2008-06-13 | E-GEOD-516 | biostudies-arrayexpress

RNA expression profiles in fibroblast-like synoviocytes from rheumatoid arthritis patients and trauma patients

2016-06-10 | GSE83147 | GEO

High Mobility Group protein mediated transcription requires DNA damage marker Î³-H2AX

Project description:The eukaryotic genome is organized into chromatin, which constitutes the physiological template for DNA-dependent processes including replication, recombination, repair and transcription. Chromatin mediated transcription regulation involves histone modifications, chromatin remodeling and DNA methylation. However, the precise biological function of non-histone chromatin-associated proteins is still unclear. The high mobility group proteins are the most abundant non-histone chromatin-associated proteins. Here we combined proteomic, ChIP-seq and transcriptome data to decipher the mechanism of transcriptional regulation mediated by the high mobility group AT-hook protein 2 (HMGA2). We showed that HMGA2-induced transcription requires H2AX phosphorylation at S139 (H2AXS139ph; Î³-H2AX), mediated by the kinase ataxia telangiectasia mutated (ATM). Furthermore, we demonstrated the relevance of this mechanism within the biological context of TGFB1-signaling. Our results link H2AXS139ph, a marker for DNA damage, to transcription, which is a new function for this histone modification. The interplay between HMGA2, ATM and H2AX is a novel mechanism of transcription initiation. Chip-seq data of HMGA2, H2AXS139ph and ATM obtained from Mouse embryonic Fibroblast cells in wt and Ko of Hmga2

2015-11-04 | E-GEOD-63861 | biostudies-arrayexpress

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