Aortic Protocollagen Proline Hydroxylase

  • K. Grasedyck
  • J. Lindner
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 82)

Abstract

Hydroxyproline and hydroxylysine are not utilized for collagen synthesis by smooth muscle cells as well as by fibro-, chondro-, osteoblasts and other collagen synthesizing cells. First, the peptide chain containing proline and lysine is synthesized. The hydroxylation of these amino acids begins during the assembly and is continued after the release of the polypeptide. Protocollagen proline hydroxylase (PPH) and protocollagen lysine hydroxylase (PLH) are involved in this hydroxylation process. Figure 1 demonstrates the role of these two enzymes although their activity levels do not run parallel to the total collagen synthesis. Therefore they are regarded as key enzymes although their activity levels do not run parallel to the total collagen synthesis in any case. The above subject was discussed in some detail elsewhere (GRASEDYCK et al., 1974).

Keywords

Proline Lysine Polypeptide Fibril Epinephrine 

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References

  1. GRASEDYCK, K., M. HELLE, J. LINDNER, K. LANGNESS: Kriterien der Aktivität einer pathologischen Bindegewebsvermehrung bei chronischen Lebererkrankungen. Verh. Dtsch. Ges. Inn. Med. 80, 503–506 (1974).PubMedGoogle Scholar
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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • K. Grasedyck
    • 1
  • J. Lindner
    • 1
  1. 1.I. Med. Clinic and PathologicalInstitute University of HamburgHamburgGermany

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