Procollagen C-endopeptidase enhancer 2 (PCPE2)

Procollagen C-endopeptidase enhancer 2 (PCPE2) is a secreted extracellular matrix protein that binds to the C-terminal propeptide of types I and II procollagen, regulating the cleavage and maturation of collagen molecules primarily by potentiating or modulating the activity of the metalloprotease bone morphogenetic protein-1 (BMP1) and related enzymes. PCPE2 exhibits distinct glycosylation and stronger heparin affinity than its paralog PCPE1, and is particularly expressed in nonossified cartilage and adult heart tissue. Beyond its role in collagen maturation, PCPE2 is implicated in lipid metabolism by facilitating the correct processing of pro-apolipoprotein AI and contributing to the assembly of high-density lipoprotein (HDL). Recent studies indicate it may function as a fine-tuner or endogenous inhibitor of certain metalloproteinases (BTPs), rather than a generalized enhancer, with a nuanced impact on extracellular matrix remodeling and potential protein–protein interaction networks relevant to cardiovascular health.

Other names

PCPE2PCOC2_HUMANPCOLCE2Procollagen C-proteinase enhancer 2

Acts as a modulator/enhancer (or under some contexts, inhibitor) of bone morphogenetic protein-1 (BMP1) and related metalloproteinases (BMP1/tolloid-like proteinases, BTPs) for the C-terminal cleavage of procollagen. Facilitates formation of mature collagen fibrils by enhancing propeptide removal; may also fine-tune activity of BTPs in certain contexts by direct binding and inhibition. Accelerates processing of pro-apolipoprotein AI in conjunction with BMP1, impacting HDL assembly.