Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway

A. Rubartelli, A. Bajetto, G. Allavena, E. Wollman, R. Sitia

Research output: Contribution to journalArticlepeer-review


Thioredoxin, despite its function as an intracellular disulfide reducing enzyme and its lack of a signal sequence, has been found to play some roles extracellularly. Here we show that thioredoxin is actively secreted by a variety of normal and transformed cells, including fibroblasts, airway epithelial cells, and activated B and T lymphocytes. Neither brefeldin A nor dinitrophenol, two drugs that block transport through the exocytic pathway, inhibit secretion of thioredoxin, indicating that the latter does not follow the classical ER-Golgi route. The secretory mechanism for thioredoxin shares several features with the alternative pathway described for interleukin- 1β, such as the potentiating effect on secretion of several unrelated drugs and the sensitivity to methylamine. However, unlike interleukin-1β, thioredoxin is not detected in membrane-bound compartments of secreting cells. In addition, when COS7 are transfected with plasmids encoding pro- interleukin-1β or thioredoxin, only the latter is detectable extracellularly.

Original languageEnglish
Pages (from-to)24161-24164
Number of pages4
JournalJournal of Biological Chemistry
Issue number34
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Biochemistry


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