(prō-prō'tēnz, tē-inz),
Inactive protein precursors; for example, proinsulin.
References in periodicals archive ?
Cleavage by SPCs activates a variety of proproteins, including hormones, growth factors, clotting factors, matrix-degrading metalloproteinases, receptors, and adhesion molecules.
Combinatorial Environmental Stress and Subtilisin-like Proprotein Convertase Expression.
A variety of proproteins have been shown to be the substrates of furin (12, 13); however, the concept of furin involved in the processing of human proBNP is currently based on a set of indirect observations (14, 15).
Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface.
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.
While all substrates contain this sequence, each widely expressed SPC has unique substrate preferences and many proproteins are processed differentially by these enzymes.
These enzymes activate a diverse array of proproteins that transit the secretary pathway.
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.
Partial Purification and Characterization of Secreted Proprotein Convertase Furin and PACE4.