Abstract
The turnover of collagen, the major protein of the body, is controlled by the rate of collagen synthesis and the activity of collagenase, a highly specific protease which initiates collagen degradation. Because collagen is largely resistant to other proteases, collagenase is believed to have an important regulatory role in such normal processes as tissue remodelling, wound healing and ageing. In addition, the regulation of the activity of collagenase may be altered in diseases of connective tissue, particularly rheumatoid arthritis, and in malignant invasion and metastasis. Collagenase is an extracellular enzyme, and thus it has been necessary to study its regulation in cells maintained in tissue culture, by measuring accumulation of the secreted protein in the culture medium. In this way, collagenases have been isolated from many tissues and cells1–7. Little is known about the modulation of collagenase synthesis and secretion, but various treatments have been reported that induce its secretion in mammalian cells in monolayer culture8–17, possibly by a mechanism involving membrane perturbation. We report here the production and secretion of collagenase by BALB/c 3T3 fibroblasts. Their ability to synthesize collagen18,19 has been extensively studied, but there has been no previous report of their collagenolytic activity. During studies of collagenase activity in BALB/c 3T3 cells, we noted that certain cultures had greatly increased enzyme activity corresponding to cultures in which contamination with mycoplasmas had been detected during routine assay. Here we present evidence that infection of cultures of BALB/c 3T3 cells with mycoplasmas results in the accumulation of high levels of collagenase in the medium.
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Kluve, B., Merrick, W., Stanbridge, E. et al. Mycoplasmas induce collagenase in BALB/c 3T3 cells. Nature 292, 855–857 (1981). https://doi.org/10.1038/292855a0
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DOI: https://doi.org/10.1038/292855a0
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