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Hydroxylated kininogens and kinins.

H Kato1, K Enjyoji

  • 1National Cardiovascular Center Research Institute, Osaka, Japan.

Agents and Actions. Supplements
|January 1, 1992
PubMed
Summary

Hydroxyprolyl-3-bradykinin, a modified form of bradykinin, was found in human high molecular weight kininogen. This post-translational modification by proline-4-hydroxylase occurs only in the kinin portion, not the protein chains.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Enzymology

Background:

  • High molecular weight kininogen (HMWK) is a precursor to bradykinin.
  • Bradykinin is a peptide hormone involved in various physiological processes.
  • Post-translational modifications can alter protein function.

Purpose of the Study:

  • To identify and characterize hydroxyprolyl-3-bradykinin in human HMWK.
  • To investigate the site and extent of hydroxyproline presence in HMWK.
  • To determine the enzyme responsible for hydroxyproline modification in HMWK.

Main Methods:

  • Purification of human HMWK.
  • Digestion of HMWK with plasma kallikrein.
  • Analysis of peptide fragments using biochemical assays.

Main Results:

  • Hydroxyprolyl-3-bradykinin was identified in digested HMWK.
  • Hydroxyproline was absent in the heavy and light chains of HMWK.
  • The proportion of hydroxyprolyl-3-bradykinin in HMWK varied significantly (14-64%) between individuals.

Conclusions:

  • Human HMWK contains a post-translationally hydroxylated kinin moiety.
  • Proline-4-hydroxylase is responsible for the hydroxylation of proline in the kinin portion of HMWK.
  • This modification is specific to the kinin part and not the HMWK protein chains.

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