Hulmes D J, Mould A P, Kessler E
Department of Biochemistry, University of Edinburgh, UK.
Matrix Biol. 1997 Apr;16(1):41-5. doi: 10.1016/s0945-053x(97)90115-3.
Procollagen C-proteinase enhancer (PCPE) is a 55 kDa glycoprotein that increases the activity of procollagen C-proteinase (PCP)/bone morphogenetic protein-1 (BMP-1) during C-terminal processing of fibrillar collagen precursors. Here we show that the 36 kDa, active fragment of PCPE enhances the activity of both the short (mouse) and long (chick) forms of PCP/BMP-1. The activity of PCPE is not associated with the formation of sedimentable procollagen aggregates. In addition, PCPE (36 kDa) has no effect in vitro on N-terminal procollagen processing by highly purified procollagen N-proteinase. Finally, when the amount of PCP is adjusted so that the rate of C-terminal processing remains constant, PCPE (36 kDa) has no effect on the assembly of collagen or pN-collagen in vitro following C-terminal processing of the corresponding precursors.
前胶原C蛋白酶增强子（PCPE）是一种55 kDa的糖蛋白，在纤维状胶原前体的C末端加工过程中可增加前胶原C蛋白酶（PCP）/骨形态发生蛋白-1（BMP-1）的活性。在此我们表明，PCPE的36 kDa活性片段可增强短型（小鼠）和长型（鸡）PCP/BMP-1的活性。PCPE的活性与可沉降的前胶原聚集体的形成无关。此外，PCPE（36 kDa）在体外对高度纯化的前胶原N蛋白酶进行的N末端前胶原加工没有影响。最后，当调整PCP的量以使C末端加工速率保持恒定时，PCPE（36 kDa）在体外对相应前体进行C末端加工后胶原或pN-胶原的组装没有影响。
