Open AccessInduction of exocytosis in permeabilized pituitary cells by alpha- and beta-type protein kinase C.
Author(s) -
Zvi Naor,
Hana Dan-Cohen,
Jacob Hermon,
Rona Limor
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.12.4501
Subject(s) - protein kinase c , digitonin , endocrinology , medicine , secretion , biology , exocytosis , pkc alpha , protein kinase a , gonadotropin , stimulation , gonadotropin releasing hormone , luteinizing hormone , hormone , kinase , microbiology and biotechnology , biochemistry , enzyme
Protein kinase C is now recognized to comprise a family of closely related subspecies (PKCs). When cultured rat pituitary cells were permeabilized by digitonin for 5 min in the absence of Ca2+, endogenous PKC activity was decreased by 72%. PKC depletion was also achieved by prior treatment (24 hr) with high concentrations of phorbol 12-myristate 13-acetate (PMA). When purified activated brain PKCs were added for 30 min to PMA-pretreated, digitonin-permeabilized cells, only alpha- and beta- but not gamma-type PKC stimulated luteinizing hormone release. Since PKC was implicated as a mediator of gonadotropin secretion, gonadotropin-releasing hormone might utilize alpha- and beta-type PKCs for stimulation of gonadotropin secretion; alpha- and beta-type PKCs might participate also in other exocytotic responses in diverse biological systems in which PKC was implicated.