@article{b9266ebd41b047778004fb66fcc1aae4,
title = "Ascorbic Acid Promotes Procollagen C-Proteinase Enhancer 1 Expression, Secretion, and Cell Membrane Localization",
abstract = "Removal of the C-propeptide from fibrillar procollagens is essential for collagen fibril assembly. The reaction is catalyzed by bone morphogenetic protein-1/tolloid-like proteinases and is accelerated by procollagen C-proteinase enhancer 1 (PCPE-1), an extracellular matrix glycoprotein that binds to the procollagen C-propeptide and its expression overlaps that of collagen. Ascorbic acid (Asc) is vital for collagen hydroxylation, folding, and secretion. It also increases collagen gene expression. The role of Asc as a regulator of PCPE-1 expression is debatable. To shed further light on this matter, herein, we studied the effects of Asc on PCPE-1 expression, secretion, and cellular localization in Rat2 and/or mouse 3T3 fibroblasts. Asc increased PCPE-1 expression at the translational and transcriptional levels about two-fold. It also increased the rate of PCPE-1 secretion approximately six-fold. Endogenous PCPE-1 was found to be cell associated, and Asc increased the amount of PCPE-1 on the cell surface. In the absence of PCPE-1 hydroxylation, we propose that the dependence of PCPE-1 secretion on Asc may be related to its role in procollagen secretion. Localization of PCPE-1 to the cell membrane favors the cell-surface as a physiological site of PCPE-1 action. Anat Rec, 2019.",
keywords = "ascorbic acid, collagen biosynthesis, collagen expression, extracellular matrix, procollagen C-proteinase enhancer",
author = "Ofra Gohar and Tali Weiss and Eitan Wineman and Efrat Kessler",
note = "Publisher Copyright: {\textcopyright} 2019 Wiley Periodicals, Inc.",
year = "2020",
month = jun,
day = "1",
doi = "10.1002/ar.24182",
language = "אנגלית",
volume = "303",
pages = "1670--1679",
journal = "Anatomical Record",
issn = "1932-8486",
publisher = "John Wiley & Sons Inc.",
number = "6",
}