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Induction of leukotriene C4 synthase activity in differentiating human erythroleukemia cells
Stockholm University, Sweden.ORCID iD: 0000-0003-3927-4394
Linköping University, Department of Biomedicine and Surgery, Cell biology. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Biomedicine and Surgery, Cell biology. Linköping University, Faculty of Health Sciences.
1992 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 189, no 2, 1043-1049 p.Article in journal (Refereed) Published
Abstract [en]

Leukotriene (LT)C4 synthase is a membrane-bound, specific glutathione transferase which catalyzes the transformation of LTA4 to LTC4. It was originally shown to be present in rodent mastocytoma and basophilic leukemia cells as well as in macrophages. Recently, expression of human LTC4 synthase was demonstrated in platelets (Söderström, M., et al. (1992) Arch. Biochem. Biophys. 294, 70-74). The present report describes the induction of LTC4 synthase activity during differentiation of human erythroleukemia (HEL) cells by the protein kinase C stimulator 12-O-tetradecanoyl phorbol 13-acetate (TPA), ligands of the steroid-thyroid hormone receptor superfamily: all-trans-retinoic acid (RA) and 1 alpha, 25-dihydroxy-vitamin D3 and in addition dimethylsulfoxide (DMSO). TPA was the most powerful inducer of enzyme activity followed by 1 alpha, 25-dihydroxy-vitamin D3 and DMSO. RA did not induce LTC4 synthase activity.

Place, publisher, year, edition, pages
Elsevier, 1992. Vol. 189, no 2, 1043-1049 p.
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Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-99879ISI: A1992KD21900067PubMedID: 1472015OAI: oai:DiVA.org:liu-99879DiVA: diva2:658723
Available from: 2013-10-22 Created: 2013-10-22 Last updated: 2017-12-06Bibliographically approved

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Söderström, MatsHammarström, Sven

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