Lysine hydroxylation of collagen in a fibroblast cell culture system.

Journal Article (Journal Article)

The lysine (Lys) hydroxylation pattern of type I collagen produced by human fibroblasts in culture was analyzed and compared. Fibroblasts were cultured from normal human skin (NSF), keloid (KDF), fetal skin (FDF), and skin tissues of Ehlers-Danlos syndrome type VIA and VIB patients (EDS-VIA and -VIB). The type I collagen alpha chains with or without non-helical telopeptides were purified from the insoluble matrix and analyzed. In comparison with NSFs, KDF and FDF showed significantly higher Lys hydroxylation, particularly in the telopeptide domains of both alpha chains. Both EDS-VIA and -VIB showed markedly lower Lys hydroxylation in the helical domains of both alpha chains whereas that in the telopeptides was comparable with those of NSFs. A similar profile was observed in the tissue sample of the EDS-VIB patient. These results demonstrate that the Lys hydroxylation pattern is domain-specific within the collagen molecule and that this method is useful to characterize the cell phenotypes in normal/pathological connective tissues.

Full Text

Duke Authors

Cited Authors

  • Uzawa, K; Yeowell, HN; Yamamoto, K; Mochida, Y; Tanzawa, H; Yamauchi, M

Published Date

  • June 6, 2003

Published In

Volume / Issue

  • 305 / 3

Start / End Page

  • 484 - 487

PubMed ID

  • 12763018

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/s0006-291x(03)00799-x


  • eng

Conference Location

  • United States