title: Investigations into the nature of growth-related proteolysis in human fibroblasts.
abstract: Previous experiments have shown that cultured human fibroblasts possess a cell-surface proteinase (the growth-related proteinase; GRP) which is essential to cell proliferation. In the present work, proteinase inhibition in defined and complex serum-free media and in pre-conditioned normal medium, still resulted in a corresponding inhibition of cell proliferation. Proteinase inhibition also blocked the action of a range of peptide growth factors and of a phorbol ester. Elevated extracellular calcium concentrations were still mitogenic in the presence of proteinase inhibitors. Proteinase inhibition did not affect the mobilisation of intracellular calcium, nor the metabolism of inositol phosphate derivatives in response to a mitogenic stimulus.
authors.affiliation: Department of Biochemistry, University of Auckland, New Zealand.
authors.forename: G K
authors.initials: GK
authors.lastname: Scott
authors.forename: H F
authors.initials: HF
authors.lastname: Seow
authors.forename: C A
authors.initials: CA
authors.lastname: Tse
mesh_terms: D002118:Calcium / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D003470:Culture Media; D005347:Fibroblasts / Q000166:cytology* / Q000187:drug effects / Q000201:enzymology; D006133:Growth Substances / Q000494:pharmacology; D006801:Humans; D007295:Inositol Phosphates / Q000378:metabolism; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*; D000515:alpha 1-Antitrypsin / Q000494:pharmacology
chemical_list: D003470:Culture Media; D006133:Growth Substances; D007295:Inositol Phosphates; D000515:alpha 1-Antitrypsin; D010447:Peptide Hydrolases; D002118:Calcium