@article{b192436348984291871f37d8fed73b80,
title = "The CUB domains of procollagen C-proteinase enhancer control collagen assembly solely by their effect on procollagen C-proteinase/bone morphogenetic protein-1",
abstract = "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.",
keywords = "Bone morphogenetic protein-1, Collagen assembly, Procollagen C-proteinase",
author = "Hulmes, \{David J.S.\} and Mould, \{A. Paul\} and Efrat Kessler",
note = "Funding Information: We are grateful to Dr. Yoshio Hojima and Dr. Darwin Prockop for their generous gift of highly purified chick procollagen Nand C-proteinases. We also thank Luba Biniaminov for her expert technical assistance. This work was supported by grant 89-498 (E.K.) from the United States-Israel Binational Science Foundation, Jerusalem, by fellowships (E.K.) from the European Molecular Biology Organization (EMBO) and the British Royal Society-Israel Academy of Sciences and Humanities exchange program, and by the Wellcome Trust (D.J.S.H).",
year = "1997",
month = apr,
doi = "10.1016/S0945-053X(97)90115-3",
language = "אנגלית",
volume = "16",
pages = "41--45",
journal = "Matrix Biology",
issn = "0945-053X",
publisher = "Elsevier BV",
number = "1",
}