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Kinin-forming activity in rat brain.

A C Shisheva1, M P Printz, K Herman

  • 1Department of Pharmacology, University of Heidelberg, Im Neuenheimer Feld 366, 6900 Heidelberg, F.R.G.

Neurochemistry International
|May 25, 2010
PubMed
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Rat brains possess a unique kinin-forming activity, distinct from plasma kallikrein. This brain kinin activity, found in microsomal fractions, differs in inhibitor sensitivity, suggesting a non-plasma kallikrein origin.

Area of Science:

  • Neurochemistry
  • Biochemistry
  • Enzymology

Background:

  • Kinin-generating enzymes play crucial roles in physiological processes.
  • The presence and nature of kinin-forming enzymes within the brain remain incompletely understood.
  • Distinguishing brain-specific kinin pathways from circulating counterparts is essential for understanding neurological functions.

Purpose of the Study:

  • To investigate and characterize kinin-forming activity in rat brain tissue.
  • To differentiate brain kinin-forming enzymes from plasma kallikrein.
  • To determine the subcellular localization of brain kinin-forming activity.

Main Methods:

  • Acetone powder preparation from frozen rat brain tissue.
  • High-pressure liquid chromatography (HPLC) for kinin identification.

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  • Differential and sucrose gradient centrifugation for subcellular fractionation.
  • Enzyme inhibition assays using Trasylol, soybean trypsin inhibitor (SBTI), and ovomucoid.

    • Main Results:

    • Rat brain contains significant kinin-forming activity (27-175.5 ng BK/g/h), distinct from plasma kallikrein.
    • HPLC analysis confirmed the formed kinin behaved like bradykinin (BK).
    • Subcellular fractionation localized the activity primarily to microsomal fractions.
    • Differential sensitivity to inhibitors (Trasylol vs. SBTI/ovomucoid) clearly distinguished brain activity from plasma kallikrein.

    Conclusions:

    • Rat brain possesses a unique kinin-forming enzymatic activity.
    • This brain activity is biochemically and pharmacologically distinct from plasma kallikrein.
    • The findings differentiate brain kinin activity from cathepsin D-like protease activity, but do not confirm a central kinin biosynthetic pathway.