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Title: Identification of cell surface dipeptidylpeptidase IV in human fibroblasts
Authors: Saison, Marc
Verlinden, J
Van Leuven, Freddy
Cassiman, Jean-Jacques
Van den Berghe, Herman #
Issue Date: Jan-1984
Series Title: The Biochemical journal. vol:216 issue:1 pages:177-83
Abstract: An antigen with dipeptidylpeptidase IV activity was identified at the surface of normal human fibroblasts. Hydrophobic interaction electrophoresis in phenyl-Sepharose revealed that the enzyme contained a hydrophobic domain, while lactoperoxidase-catalysed iodination with 125I of living cells indicated that the protein was located at the cell surface. Crossed immunoelectrophoresis with specific antibodies of acid-extracted or papain-treated cells showed a shift of the dipeptidylpeptidase IV peak to a faster mobility. The molecular properties of the fibroblast enzyme were clearly different from those described for dipeptidylpeptidase IV from other tissues and species. Fibroblast dipeptidylpeptidase IV contained two different disulphide-linked subunits, of apparent Mr values 125000 and 135000 (denatured and reduced). In gel filtration, an Mr of about 400000 was observed for the unreduced molecule. The enzymic properties of fibroblast dipeptidylpeptidase IV were very similar to those of the well-characterized pig kidney enzyme. Activity towards glycyl-L-prolyl-beta-naphthylamide was inhibited 50% by 0.023 mM-di-isopropylphosphorofluoridate. L-Alanyl-L-alanyl-beta-naphthylamide was hydrolysed ten times more slowly than glycyl-L-prolyl-beta-naphthylamide.
ISSN: 0264-6021
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Human Mutations and Polymorphisms Section (-)
Clinical Genetics Section (-)
Forensic Biomedical Sciences
Department of Human Genetics - miscellaneous
# (joint) last author

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