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ProteomicsConsequences of fibroblast ablation in adult murine hearts
Fibroblasts produce the majority of collagen in the heart and are thought to regulate extracellular matrix (ECM) turnover. However, the in vivo role of fibroblasts in structuring the basal ECM network is poorly understood. To examine the effects of fibroblast loss on the microenvironment in the adul...
ORGANISM(S): Mus musculus (Mouse) 
2023-03-10 | PXD021741 | Pride
Shotgun Murine Fibroblast ablated Labelfree analysis 
ProteomicsIdentification of potential protein biomarkers associated with congenital diaphragmatic hernia in human amniotic fluid
Congenital diaphragmatic hernia (CDH) results from incomplete diaphragm development and can be associated with pulmonary hypoplasia, pulmonary hypertension, and heart failure. Currently, few biomarkers are available. Since amniotic fluid comprises proteins of both fetal and maternal origin, its anal...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD041165 | Pride
Surfactant protein b Osteopontin Galectin-3 Amniotic fluid Kallikrein-5 Proteomics 
UnknownSolid state engineering of Bi2S3/rGO nanostrips: an excellent electrode material for energy storage applications.
Not available
S-EPMC11019906 | biostudies-literature
ProteomicsSubstrate identification of ADAMTS16
Secreted and cell-surface proteases are major mediators of extracellular matrix remodelling, but their mechanisms and regulatory impact are poorly understood. We developed a mass spectrometry approach using cell free ECM produced by mouse Balb/c 3T3 cells in vitro to identify fibronectin as a novel ...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2018-04-23 | PXD007284 | Pride
Adamts16 Fibronectin Lc-ms/ms 
ProteomicsProteolytic information flows from human knee osteoarthritic cartilage to synovial fluid and defines the roles of key drug targets -1
Objectives: Proteolytic cartilage loss is a major mechanism of osteoarthritis (OA) pathogenesis but few joint breakdown biomarkers are currently available. We sought to determine the overlap of proteolytic peptides in OA cartilage and synovial fluid on a proteome-wide scale with the goals of increa...
ORGANISM(S): Homo sapiens (Human) 
2025-02-04 | PXD048053 | Pride
Proteolysis Synovial fluid Cartilage Protease Proteomics Osteoarthritis 
UnknownThe <i>Shigella flexneri</i> effector IpaH1.4 facilitates RNF213 degradation and protects cytosolic bacteria against interferon-induced ubiquitylation.
Not available
S-EPMC12662631 | biostudies-literature
ProteomicsADAMTS7, a target in atherosclerosis, cooperates with homolog ADAMTS12 to protect against myxomatous valve degeneration
The metalloprotease ADAMTS7, a drug target in atherosclerosis and vascular restenosis, is thought to have no relevant physiological role in the cardiovascular system. However, potential cooperation with its close homolog, ADAMTS12, that may mask such a role remains unexplored. The objective of the p...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2025-05-07 | PXD055550 | Pride
Metalloproteinase Hypertrophy Chondroitin sulfate Heart valve Fibrosis Adamts Regurgitation Extracellular matrix Myxomatous valve 
ProteomicsPost-translational regulation and proteolytic activity of human adamts-8: a comparison with adamts-1, -4, and -5
A Disintegrin-like And Metalloprotease with Thrombospondin type 1 motifs (ADAMTS)-8 is a secreted protease which has been recently implicated in the pathogenesis of pulmonary arterial hypertension (PAH). However, the substrate repertoire of ADAMTS-8 and regulation of its activity are incompletely u...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027724 | Pride
Ecm Opn Protease Pah Adamts 
ProteomicsCombined genetic-pharmacologic inactivation of tightly linked ADAMTS proteases uncovers a requirement for versican and glypican-6 proteolysis in cardiac development-1
Background: Extracellular matrix remodeling mechanisms are understudied in cardiac development and congenital heart defects. Two similar matrix-degrading metalloproteases, ADAMTS1 and ADAMTS5, are extensively co-expressed during mouse cardiac development. The mouse mutants of each have mild cardiac ...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2025-05-06 | PXD045868 | Pride
Proteomics Cardiac jelly Proteases Tetralogy of fallot Proteoglycan Trabeculation 
ProteomicsO-Fucosylation of ADAMTSL2 Thrombospondin Type 1 Repeats is Required for Secretion and is Impacted by Geleophysic Dysplasia-Causing Mutations
A disintegrin-like and metalloprotease domain with thrombospondin type 1 repeats-like 2 (ADAMTSL2) is a matricellular protein that interacts with latent TGF-b binding protein 1 and fibrillin-1. ADAMTSL2 mutations cause an autosomal recessive connective tissue disorder named geleophysic dysplasia 1 (...
ORGANISM(S): Mus musculus (Mouse) 
2020-10-01 | PXD018902 | Pride
Geleophysic dysplasia Thrombospondin type 1 repeats Tsr glycosylation Adamtsl2 o-fucosylation 
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