Secretion of unhydroxylated chick tendon procollagen

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Abstract

The secretion of unhydroxylated procollagen at 37° by isolated chick tendon fibroblasts independent of protein synthesis was examined. The data showed that intact molecules were secreted and that their degradation was an extracellular event. The kinetics of secretion indicated that most of the secreted procollagen appeared in the medium during the initial 30 min following inhibition of protein synthesis and only an additional 35% reached the extracellular space in the subsequent 90 min. The pattern of secretion suggested the existence of an intracellular binding site for the unhydroxylated molecules which was saturated during the early period of secretion. It is speculated that such a binding site could be the enzyme prolyl hydroxylase which has a high affinity for unhydroxylated procollagen at 37°.

References (16)

  • P. Dehm et al.

    Biochim, Biophys. Acta

    (1971)
  • P.B. Ramaley et al.

    Fed. Eur. Biochem. Soc. Letters

    (1971)
  • S.A. Jimenez et al.

    J. Biol. Chem

    (1973)
  • S.A. Jimenez et al.

    Biochem. Biophys. Res. Commun

    (1973)
  • R. Berg et al.

    Biochem. Biophys. Res. Commun

    (1973)
  • S.A. Jimenez et al.

    Fed. Eur. Biochem. Soc. Letters

    (1971)
  • K. Juva et al.

    Anal. Biochem

    (1966)
  • P.B. Ramaley et al.

    Fed. Eur. Biochem. Soc. Lett

    (1973)
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