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Amino Acids

, Volume 27, Issue 3–4, pp 305–311 | Cite as

Proteomic identification of collagens and related proteins in human fibroblasts

  • J. E. Oh
  • K. Krapfenbauer
  • G. Lubec
Article

Summary.

Fibroblasts are used for diagnosis of a series of metabolic diseases and are particularly suitable for the diagnosis of collagen disorders. We aimed to generate a skin fibroblast map that would be suitable for the concomitant determination of collagen and collagen-related proteins.

A human skin fibroblast cell line was cultivated, homogenised, proteins extracted and subject to two-dimensional gel electrophoresis with subsequent in-gel-digestion of protein spots and mass spectrometrical identification (MALDI-TOF).

Collagen alpha1 (I) chain precursor, collagen alpha1 (III) chain precursor, collagen alpha2 (VI) precursor and collagen modifying enzymes prolyl 4-hydroxylase alpha-2-subunit precursor, procollagen-lysine 2-oxoglutarate 5-dioxygenase 1 and 2, protein disulfide isomerase ER-60 precursor and peptidyl-prolyl cis-trans isomerase were among the abundant proteins.

The finding of collagen and collagen-related structures as well as the identification of other metabolic enzyme systems on one 2D gel may propose the use of this proteomic method for further characterization of collagen and collagen-related proteins or for preliminary screening of metabolic disorders.

Keywords: Fibroblast – Collagen – Collagen alpha1 chain – Procollagen-lysine – Prolyl 4-hydroxylase – Protein disulfide isomerase 

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Copyright information

© Springer-Verlag/Wien 2004

Authors and Affiliations

  • J. E. Oh
    • 1
  • K. Krapfenbauer
    • 2
  • G. Lubec
    • 1
  1. 1.Department of PediatricsUniversity of ViennaViennaAustria
  2. 2.Center for Medical Genomics, F. Hoffmann-La RocheBaselSwitzerland

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