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Biological Evaluation of Simplified Analogs of Protein Kinase C Inhibitor Staurosporine
Author(s) -
Rolph Carly,
Pelkey Erin,
Mowery Patricia
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.721.14
Subject(s) - staurosporine , protein kinase c , kinase , serine , protein kinase a , phosphorylation , chemistry , small molecule , pharmacology , microbiology and biotechnology , biochemistry , cancer research , biology
PKC, or protein kinase C, is an enzyme in the family of serine/threonine kinases that is involved in a variety of cell signaling pathways throughout the body. It plays a role in a multitude of diseases and disorders such as diabetes, heart failure, Parkinson's disease, Alzheimer's disease, bipolar disorder, dementia and cancer. PKC is a promising therapeutic target using small molecule inhibitors. One of the best characterized inhibitors is staurosporine, an indolocarbazole derivative, that binds the ATP pocket of PKC and limits its phosphorylation activity. Numerous simplified derivatives of staurosporine have been synthesized, which have promising structural features for inhibiting PKC. An initial screening using an MTT assay has shown that planar analogs have different IC 50 values than non‐planar ones, but testing will need to be continued to further determine cytotoxicity.