EC Number   |
General Information |
Reference |
|---|
   3.4.21.B26 | malfunction |
complete knockout of PC5/6 is lethal between E4.5-7.5 |
718009 |
| 3.4.21.B26 | malfunction |
enzyme-knockout endometrial epithelial cells show reduced capacity to attach to trophoblast spheroids and bind to fibronectin compared with control. Knockdown of the enzyme decreases cell surface presentation of functional integrins-alpha1, alpha2, alpha5, alphaV and alphaVbeta5 |
731899 |
| 3.4.21.B26 | physiological function |
full-length alpha-dystroglycan in the human endometrial epithelium is a barrier for embryo attachment and removal of the N-terminus by proprotein convertase 5/6 regulates receptivity. Removal of alpha-dystroglycan N-terminus is an important posttranslational control of endometrial receptivity and uterine fluid |
753529 |
| 3.4.21.B26 | malfunction |
gene inactivation of PC5/6 leads to lethality at birth, the lack of PC5/6 in enterocytes results in a significantly higher tumor number in the duodenum, the absence of PC5/6 is also associated with a premature mortality of ApcMin/+ mice that harbor a heterozygote multiple intestinal neoplasia mutation in the adenomatous polyposis coli gene |
709911 |
| 3.4.21.B26 | physiological function |
involvement of PC5/6A in squamous differentiation of human nasal epithelial cells. Overexpression of PC5/6A and BMP-2 in the human nasal epithelial cell line RPMI-2650 demonstrates that PC5/6A can activate BMP-2 |
752449 |
| 3.4.21.B26 | physiological function |
involvement of the enzyme in squamous differentiation of human nasal epithelial cells possibly through up-regulation of the BMP-2/pSmad1/5/8/p38 signaling pathway |
731111 |
| 3.4.21.B26 | malfunction |
PC5/6-knockout mouse embryos show developmental abnormalities, and reduced overall mineralization |
753112 |
| 3.4.21.B26 | malfunction |
PC6 knockdown reduces removal of alpha-dystroglycan N-terminus from endometrial epithelial cell surface and blastocyst adhesion |
753529 |
| 3.4.21.B26 | physiological function |
Pcsk5/PCSK5 is temporally and spatially expressed with Opn/OPN (Spp1/SPP1) in osteoblasts and osteocytes, indicating that osteopontin could be a physiologically relevant substrate for PC5/6 or PC5/6-activated proteases in bone. Cleavage of osteopontin may modify the function of osteopontin in bone and/or modulate other enzymatic cleavages of osteopontin, leading to alterations in the bone phenotype |
753112 |
| 3.4.21.B26 | physiological function |
pro-integrins-alpha in the endometrial epithelium are post-translationally cleaved by the enzyme into functional subunits for the binding of blastocyst and adhesion of extracellular matrix proteins, the enzyme is responsible for the post-translational cleavage of pro-integrin-alpha5 and integrin-alphaV into their heavy and light chains in HEC-1-A cells. The integrins are transmembrane glycoproteins, some of which play an important role in the adhesive interactions between the trophoblast (blastocyst) and uterine epithelium at implantation |
731899 |
