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Role of protein kinase C in cholinergic stimulation of lacrimal gland protein secretion
Author(s) -
Zoukhri Driss,
Hodges Robin R.,
Dicker Deanna M.,
Dartt Darlene A.
Publication year - 1994
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(94)00824-8
Subject(s) - carbachol , protein kinase c , secretion , lacrimal gland , cholinergic , endocrinology , medicine , stimulation , gene isoform , biology , chemistry , kinase , microbiology and biotechnology , biochemistry , pathology , gene
The purpose of this study was to determine the role of protein kinase C (PKC) isozymes in carbachol‐induced protein secretion in the lacrimal gland. Three isoforms of PKC are present in rat lacrimal gland: PKC‐α, ‐δ and ‐g3. Carbachol translocated PKC‐ε during 5 s incubation. Pretreatment with PdBu for 0 to 4 h down‐regulated PKC‐α by 31% at 20 min, PKC‐ε by 36% at 2 h, and PKC‐δ by 37% at 4 h. A 2 h phorbol ester treatment inhibited carbachol‐induced secretion completely at 1 min and partially at 5, and 20 min, but did not alter the carbachol‐induced increase in the intracellular [Ca 2+ ]. We conclude that PKC‐α and ‐g3, but not PKC‐δ, are implicated in cholinergic agonist‐induced protein secretion in rat lacrimal gland.