HUMAN ARTICULAR-CARTILAGE SECRETES CHARACTERISTIC METAL DEPENDENT PROTEINASES UPON STIMULATION BY MONONUCLEAR CELL FACTOR

  • 1 February 1986
    • journal article
    • research article
    • Vol. 13  (1) , 20-27
Abstract
Human articular cartilage stimulated during organ culture by the addition of human blood mononuclear cell factor concomitantly released latent proteinases and proteoglycan. Gel chromatography at pH 7.4 separated 2 distinct latent enzymes: a general proteinase which could degrade proteoglycan, casein and gelatin, and a collagenolytic activity of smaller molecular size. The general proteinase was calcium dependent and could be activated by either trypsin or 4-aminophenylmercuric acetate; the former procedure invariably generating greatest activity. The enzyme exhibited a broad bimodal pH profile against proteoglycan, with optimum activity at pH 5.5.