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Phorbol ester‐induced suppression of leukotriene C 4 synthase activity in human granulocytes
Author(s) -
Sjölinder Mikael,
Tornhamre Susanne,
Werga Petra,
Edenius Charlotte,
Lindgren Jan Åke
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01303-2
Subject(s) - phorbol ester , atp synthase , chemistry , leukotriene b4 , leukotriene , leukotriene c4 , biochemistry , enzyme , microbiology and biotechnology , protein kinase c , immunology , biology , inflammation , asthma
The effect of the protein kinase C activator, phorbol 12‐myristate 13‐acetate (PMA), on the metabolism of exogenous leukotriene (LT)A 4 in human granulocytes was investigated. After incubation with LTA 4 decreased levels of LTC 4 but not LTB 4 were observed in granulocyte suspensions pretreated with PMA. This finding could in part be ascribed to oxidative metabolism of LTC 4 , since PMA induced a rapid degradation of exogenously added LTC 4 . After blocking of LTC 4 metabolism with the H 2 O 2 scavenger catalase, a PMA‐provoked suppression of the conversion of LTA 4 to LTC 4 was observed, indicating PKC‐dependent regulation of LTC 4 synthase activity. This effect, as well as PMA‐induced degradation of LTC 4 was presented by specific protein kinase C inhibitors.