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Histochemical Evidence of Dipeptidylpeptidase IV Activity in the Schwann Cells Surrounding Unmyelinated Portions of Axons

  • Petr Dubový

Abstract

Dipeptidylpeptidase IV (DPP IV) is a serine exopeptidase which removes X-Pro sequences from the N-terminal of natural peptides or artificial substrates. Its biological role in peripheral nerve structures is still obscure. However, the ability of DPP IV to degrade substance P (SP) is attractive for the explanation of the function of this enzyme in peripheral nerve structures of the skin.

Keywords

Nerve Fiber Schwann Cell Artificial Substrate Natural Peptide Glabrous Skin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. Dalsgaard, C.J., Jonsson, C.E., Hökfelt, T., and Cuello, A.C., 1983, Localization of substance P-immunoreactive nerve fibers in the human digital skin, Experientia, 39, 118–120.CrossRefGoogle Scholar
  2. Dubový, P., A study of the dipeptidylpeptidase IV activity in cat fungiform papillae, Acta histochem., in press.Google Scholar
  3. Dubový, P., and Malinovský, L., 1984, Localization of DPP IV in sensory corpuscles by means of light and electron microscope, Histochem. J., 16, 473–475.PubMedCrossRefGoogle Scholar
  4. Heymann, E., and Mentlein, R., 1978, Liver dipeptidylamino peptidase IV hydrolyses substance P, FEBS Lett., 91: 360–364.PubMedCrossRefGoogle Scholar
  5. Lindner, G., 1984, On the effect of N-and C-terminal sequences of the substance P on nonneuronal cells in vitro, Z. mikrosk.-anat. Forsch., 98, 107–118.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Petr Dubový
    • 1
  1. 1.Department of Anatomy, Medical FacultyPurkyně UniversityBrnoCzechoslovakia

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