Procollagen C-Endopeptidase Enhancer (PCOLCE) ELISA Kits

Human Procollagen C-Endopeptidase Enhancer (PCOLCE) interaction partners

1. Serum PCPE-1 might be used as a noninvasive marker of liver fibrosis in chronic hepatitis B.

2. Results suggest that PCPE-1 binding to syndecans and/or fibronectin may control collagen fibril assembly on the cell surface.

3. The analysis of the PCPE-1 interaction network based on Gene Ontology terms suggests that, besides its role in collagen deposition, PCPE-1 might be involved in tumour growth, neurodegenerative diseases and angiogenesis.

4. The results of this study suggested that nuclear entrapment of PCOLCE and its extracellular depletion represents a novel molecular mechanism in late-onset muscle fibrosis.

5. Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.

6. data generated by our system, support our hypothesis that combined data on PCPE concentration and isoforms may be useful for the diagnosis and follow-up of bone diseases

7. Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide region only.

8. procollagen C-proteinase enhancer-1 (PCPE-1) binds to heparin/heparan sulfate and has a role in interaction with cells

9. Role of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity.

10. Data show that only those containing both PCPE1 CUB1 and CUB2 were capable of enhancing BMP-1 activity and binding to a mini-procollagen substrate with nanomolar affinity.

11. PCPE binds to sites on either side of the procollagen cleavage site, thereby facilitating the action of procollagen C-proteinases.

12. PCPE1 and PCPE2 were found to be collagen-binding proteins, capable of binding at multiple sites on the triple helical portions of fibrillar collagens and also capable of competing for such binding with procollagen C-proteinases

13. procollagen C-proteinase enhancer is an elongated multidomain glycoprotein as shown by small angle x-ray scattering

14. the three-dimensional structure of the NTR domain of human PCOLCE1 is the first example of a structural domain with the canonical features of an NTR module

15. chordinase activity of BMP1 is not enhanced by PCPE-1

16. tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains

17. PCPE-stimulating activity requires a calcium binding motif in the CUB1 domain that is highly conserved among CUB-containing proteins

18. in bone fracture patients, 12 proteins were related to bone/cartilage metabolism, including: TGF-beta induced protein IG-H(3), cartilage acidic protein 1, procollagen C proteinase enhancer protein and TGF-beta receptor III.

19. PCPE-1 interacts with beta2-microglobulin (beta2-m) and may help initiate beta2-m amyloid fibril formation in connective tissues

20. Procollagen I mRNA expression was decreased by synovial fluid from patients with prosthesis loosening.

Mouse (Murine) Procollagen C-Endopeptidase Enhancer (PCOLCE) interaction partners

1. Bone morphogenetic protein-1/mTLD and PCPE-1 are upregulated in corneal scars. Both proteins may therefore contribute to the process of corneal scarring.

2. procollagen C-proteinase enhancer-1 (PCPE-1) binds to heparin/heparan sulfate and has a role in interaction with cells

3. PCPE1 and PCPE2 were found to be collagen-binding proteins, capable of binding at multiple sites on the triple helical portions of fibrillar collagens and also capable of competing for such binding with procollagen C-proteinases

4. PCOLCE1 is an important determinant of bone mechanical properties and geometry and of collagen fibril morphology in mammals.