Such multibasic motifs typically mark the cleavage sites of proproteins from the mature molecule during the secretory process through the action of proprotein convertases (Steiner, 1998; Seidah and Chretien, 1999).
Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides.
Endoproteases of the Subtilisin-like Proprotein Convertase (SPC) family cleave substrate proproteins on the carboxy terminal side of a conserved sequence described as N-Arginine-X-X-Arginine-C.
Paired Basic Amino Acid Cleaving Enzyme 4 (PACE4) is a eukaryotic endoprotease in the subtilisin-like proprotein convertase (SPC) family.
Subtilisin-like proprotein convertases (SPCs) arc capable of processing a number of proproteins in the secretory pathway known to affect nervous system development and synaptogenesis.
The Effect of Vision Loss on Subtilisin-like Proprotein Convertase Expression in the Brain.
Furin is a subtilisin-like endoprotease involved in processing a diverse array of proproteins
within the secretory and endocytic pathways of a wide variety of organisms and mammalian cell types.
While closely related to furin, the most well characterized member of this family, PACE4 has a restricted substrate range compared to furin, as PACE4 can process some, but not all, of the proproteins
furin can process.
Combinatorial Environmental Stress and Subtilisin-like Proprotein
convertases, furin and corin, are considered the most likely proBNP processing enzymes.
Partial Purification and Characterization of Secreted Proprotein
Convertase Furin and PACE4.
Generation of Chinese Hamster Ovary Cells Stably Overexpressing Proprotein