ArticleStructure (London, England : 1993)2018
Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 47 citations in OpenAlex.
- PCPE1 and PCPE2: When Sequence Similarity Masks Functional Diversity.Arteriosclerosis, thrombosis, and vascular biology · 2026Review
- Transcriptomic analysis of human cartilage identified potential therapeutic targets for hip osteoarthritis.Human molecular genetics · 2025Article
- SOX9 Promotes Collagen VI Secretion by Upregulating PCOLCE in Neurofibroma.Molecular neurobiology · 2024Article
- Predictive value of procollagen c-protease enhancer protein on the prognosis of glioma patients.Heliyon · 2024Article
- Exploring Molecular Alterations in Breast Cancer Among Indian Women Using Label-Free Quantitative Serum Proteomics.Biochemistry research international · 2024Article
- Identification of PCPE-2 as the endogenous specific inhibitor of human BMP-1/tolloid-like proteinases.Nature communications · 2023Article
- High expression of PCOLCE gene indicate poor prognosis in patients and are associated with immune infiltration in glioma.Scientific reports · 2023Article
- Small-Molecule-Mediated Suppression of BMP Signaling by Selective Inhibition of BMP1-Dependent Chordin Cleavage.International journal of molecular sciences · 2023Article
- Degradation of collagen I by activated C1s in periodontal Ehlers-Danlos Syndrome.Frontiers in immunology · 2023Article
- Dynamics of the secreted frizzled related protein Sizzled and potential implications for binding to bone morphogenetic protein-1 (BMP-1).Scientific reports · 2022Article
- Identification of key sex-specific pathways and genes in the subcutaneous adipose tissue from pigs using WGCNA method.BMC genomic data · 2022Article
- Procollagen C-proteinase enhancer 1 promotes physiologic retinal angiogenesisInternational journal of ophthalmology · 2022Article
- Procollagen C-Proteinase Enhancer-1 (PCPE-1) deficiency in mice reduces liver fibrosis but not NASH progression.PloS one · 2022Article
- Pcpe2, a Novel Extracellular Matrix Protein, Regulates Adipocyte SR-BI-Mediated High-Density Lipoprotein Uptake.Arteriosclerosis, thrombosis, and vascular biology · 2021Article
- Procollagen C-proteinase enhancer-1 (PCPE-1), a potential biomarker and therapeutic target for fibrosis.Matrix biology plus · 2021Article
- Suppression of pancreatic ductal adenocarcinoma growth and metastasis by fibrillar collagens produced selectively by tumor cells.Nature communications · 2021Article
- Crystal structure of ADAMTS13 CUB domains reveals their role in global latency.Science advances · 2021Article
- Basic Structure, Physiology, and Biochemistry of Connective Tissues and Extracellular Matrix Collagens.Advances in experimental medicine and biology · 2021Article
- Gemcitabine-Resistant Biomarkers in Bladder Cancer are Associated with Tumor-Immune Microenvironment.Frontiers in cell and developmental biology · 2021Article
- PCOLCE Is Potent Prognostic Biomarker and Associates With Immune Infiltration in Gastric Cancer.Frontiers in molecular biosciences · 2020Article
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11 authors at 3 institutions in 2 countries.
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Abstract
Procollagen C-proteinase enhancer-1 (PCPE-1) is a secreted protein that specifically accelerates proteolytic release of the C-propeptides from fibrillar procollagens, a crucial step in fibril assembly. As such, it is a potential therapeutic target to improve tissue repair and prevent fibrosis, a major cause of mortality worldwide. Here we present the crystal structure of the active CUB1CUB2 fragment of PCPE-1 bound to the C-propeptide trimer of procollagen III (CPIII). This shows that the two CUB domains bind to two different chains of CPIII and that the N-terminal region of one CPIII chain, close to the proteolytic cleavage site, lies in the cleft between CUB1 and CUB2. This suggests that enhancing activity involves unraveling of this chain from the rest of the trimer, thus facilitating the action of the proteinase involved. Support for this hypothesis comes from site-directed mutagenesis, enzyme assays, binding studies, and molecular modeling.
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