title: Aminopeptidase activity profile in cultured human osteoblasts.
abstract: Aminopeptidases (APs) are enzymes involved in a wide variety of biological processes and present in a variety of different cell populations. The authors studied these enzymes in primary cultured human osteoblasts in order to establish an activity profile and thereby contribute to knowledge of bone tissue. The authors used 13 different substrates (N-terminal amino acids) and a fluorimetric assay to examine AP activity associated with the membranes of cultured osteoblasts. The authors demonstrated activity > 10 pmol/min/10(4) cells when glycine, alanine, leucine, arginine, phenylalanine, methionine, and lysine were used as substrates. The activity was markedly lower (<1.6 pmol/min/10(4) cells) when the other N-terminal amino acids were used. Puromycin and bestatin inhibited AP activity, though not completely, when we used AlaNA or LeuNA as substrates. Further studies are warranted to determine the role of these enzymes in bone tissue physiology.
authors.affiliation: Institute of Neurosciences, University of Granada, Spain.
authors.forename: Gema
authors.initials: G
authors.lastname: Lucena
authors.forename: Candela
authors.initials: C
authors.lastname: Reyes-Botella
authors.forename: Olga
authors.initials: O
authors.lastname: García-Martínez
authors.forename: Lourdes
authors.initials: L
authors.lastname: Díaz-Rodríguez
authors.forename: Francisco
authors.initials: F
authors.lastname: Alba
authors.forename: Concepción
authors.initials: C
authors.lastname: Ruiz
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism*; D002478:Cells, Cultured; D006801:Humans; D010006:Osteoblasts / Q000166:cytology / Q000201:enzymology*
chemical_list: D000626:Aminopeptidases