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Inhibition of lung surfactant secretion by KN‐62, a specific inhibitor of the calcium‐ and calmodulin‐dependent protein kinase II
Author(s) -
Liu Lin
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203252
Subject(s) - secretion , protein kinase a , camk , protein kinase c , pulmonary surfactant , chemistry , western blot , phorbol , microbiology and biotechnology , calmodulin , terbutaline , kinase , biology , biochemistry , enzyme , immunology , autophosphorylation , asthma , gene
A role of Ca2+‐ and calmodulin‐dependent protein kinase II (CaMK II) in lung surfactant secretion was evaluated using KN‐62, a specific inhibitor of CaMK II. KN‐62 caused a dose‐dependent inhibition of Ca2+ iononphore A23187‐stimulated phosphatidylcholine (PC) secretion from cultured alveolar type II cells. Concentration effecting 50% inhibition was ∼4 μM. However, KN‐62 only slightly influenced PC secretion from type II cells stimulated by phorbol 12‐myristate 13‐acetate, terbutaline and ATP that are known to increase surfactant secretion via the protein kinase C and protein kinase A pathways. KN‐62 also inhibited the activity of CaMK II in type II cells. A 55 kDa protein was detected in type II cells by Western blot analysis using an antibody against the β‐subunit of CaMK II. The results suggest that CaMK II participates in A23187‐stimulated lung surfactant secretion.