Premium
Effect of phorbol ester and phospholipase C on LH‐stimulated steroidogenesis in purified rat Leydig cells
Author(s) -
Papadopoulos Vassilios,
Carreau Serge,
Drosdowsky Michel A.
Publication year - 1985
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(85)80393-8
Subject(s) - leydig cell , protein kinase c , adenylate kinase , endocrinology , medicine , phorbol , stimulation , phospholipase c , testosterone (patch) , phospholipase , cyclase , protein kinase a , in vitro , chemistry , phospholipase a2 , phospholipase a , phorbol ester , biology , enzyme , biochemistry , luteinizing hormone , hormone
When the phorbol ester, 4β‐phorbol‐12‐myristate‐13‐acetate (PMA) or bacterial phospholipase C (PL‐C) is added to a preparation of purified adult rat Leydig cells, containing 2 mM CaCl 2 , a time‐ and dose‐dependent decrease of LH‐stimulated testosterone production is observed. After a 3 h stimulation with oLH (100 ), PMA (100 ) and PL‐C (1.6 ) do not affect the cell viability or the hCG specific binding, while cAMP accumulation is significantly reduced; cAMP‐stimulated steroidogenesis is diminished only in the presence of PL‐C. These observations suggest that in vitro: (i) activated Ca 2+ ‐ and phospholipid‐dependent protein kinase is implicated in the regulation of rat Leydig cell steroidogenesis by LH at a step before the adenylate cyclase; (ii) phospholipids play an important role in cAMP‐stimulated testosterone synthesis.