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During the enzymatic disaggregation of human synovium, used in the process of isolating synoviocytes, a factor was liberated into the culture medium that exhibited the thymocyte mitogenic properties of interleukin-1. Like interleukin-1, this synovial-derived mitogen could be isolated using an affinity column of antihuman leukocytic pyrogen. By gel filtration and isoelectric focusing, the mitogen cofractionated with human monocyte-derived interleukin-1. Finally, the isolated mitogen was shown to exhibit other properties of interleukin-1: stimulation of the secretion of interleukin-2, enhancement of the titer of acute-phase proteins in vivo, and stimulation of the release of prostaglandin E2 from human synoviocyte cultures. These observations suggest that interleukin-1 can be derived from the human synovium.
Wood et al. (1985) studied this question.