Postsynaptic densities contain a subtype of protein kinase C |
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| Authors: | M Wolf S Burgess U K Misra N Sahyoun |
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| Institution: | 1. Department of Chemistry, Graduate School of Science and Engineering, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Japan;2. Department of Laboratory Medicine, Shimane University School of Medicine, Izumo, Japan;3. Advanced Research Support Center, Ehime University, 2-5 Bunkyo-cho, Matsuyama 790-8577, Japan;4. Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803-1804, USA;1. Uppsala University, Department of Chemistry – Ångström Laboratory, Lägerhyddsvägen 1, Box 538, 75120 Uppsala, Sweden;2. Seco Tools AB, Björnbacksvägen 2, 73782 Fagersta, Sweden;3. AB Sandvik Coromant, Lerkrogsvägen 19, 12679 Hägersten, Sweden |
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| Abstract: | Protein kinase C or an isoenzyme thereof appears to be a significant component of postsynaptic densities (PSDs) from rat brain. This cytoskeletal organelle binds 4 beta-phorbol 12,13-dibutyrate (PDBu) with a Bmax of about 20 pmol/mg protein and an apparent Kd of 3.3 nM. Ca2+ and phosphatidyl serine (PS) stimulated the endogenous phosphorylation of a subset of PSD polypeptides with Mr values between 16,000 and 22,000. Finally, a monospecific protein kinase C antibody reacted with a Mr 70,000 PSD polypeptide which migrated on SDS-PAGE slightly ahead of the Mr 77,000 purified enzyme. These data suggest that protein kinase C or a similar enzyme can be integrated into a cytoskeletal system and may play an important role in postsynaptic function. |
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