Science · 1989 · 162 citations · 28 references
Life SciencesBiochemistryMolecular BiologyEnzymologyImmunopathologyProtein BiochemistryAutocrine SignalingExtracellular MatrixFibrous ProteinsProtein SynthesisAmyloidogenic ProteinsPolyacrylamide Gel ElectrophoresisRemodelingSerum Amyloid A ProteinSerum-free Cell CultureSerum-free CultureSerum-free Culture MediaSynovial Fibroblasts
Two autocrine proteins of 14 and 12 kilodaltons that induce the synthesis of rabbit fibroblast collagenase were identified. The proteins were purified from serum-free culture medium taken from rabbit synovial fibroblasts stimulated with phorbol myristate acetate. The amino-terminal sequences of the 14- and 12-kilodalton species were approximately 60 to 80 percent homologous with serum amyloid A and beta 2 microglobulin, respectively. The polyacrylamide gel-eluted proteins retained the ability to induce collagenase synthesis in rabbit and human fibroblasts. These autocrine proteins may provide a means to modulate collagenase synthesis in normal remodeling as well as in inflammation and disease states.
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Jean‐Michel Dayer, Bruce Beutler, Anthony Cerami · The Journal of Experimental Medicine · 1985 · 1.2K citations · Full text
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
Phyllis Ponte, P. Gonzalez DeWhitt, J. Miller et al. · Nature · 1988 · 1K citations