Spermine stimulation of phosphoprotein dephosphorylation in the brain of Manduca sexta |
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| Institution: | 1. RCSI School of Pharmacy, 1st Floor Ardilaun House Block B, 111 St Stephen''s Green, Dublin 2, Ireland;2. RCSI Health Professions Education Centre, 123 St Stephen''s Green, Dublin 2, Ireland;3. Department of Pharmacy, 18 Science Drive 4, National University of Singapore, 117559, Singapore;1. Department of Clinical Laboratory, Key Laboratory of Laboratory Medicine of Henan Province, The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China;2. Department of Clinical Laboratory, The Third People’s Hospital of Henan Province, Zhengzhou 450050, China;3. Department of Clinical Laboratory, People′s Hospital of Zhecheng County, Shangqiu 476200, China;4. Department of Blood Transfusion, The Second Affiliated Hospital of Air Force Military Medical University of Chinese PLA, Xian 710032, China;5. Department of Blood Transfusion, The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China;6. Department of Gynaecology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China;7. Department of Clinical Laboratory, Fuwai Central China Cardiovascular Hospital, Zhengzhou 451450, China;1. State Key Laboratory of Materials Processing and Die & Mould Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China;2. Centre for Advanced Materials Technology (CAMT), School of Aerospace, Mechanical and Mechatronic Engineering, J07, The University of Sydney, Sydney, NSW 2006, Australia |
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| Abstract: | An in vitro analysis of endogenous dephosphorylation of a particulate-associated cAMP-dependent 34 kDa phosphoprotein from the brains of Manduca sexta larvae revealed the presence of phosphatase activity in the same fraction. The rate of dephosphorylation is stimulated by the polyamine spermine, is markedly inhibited by vanadate and Zn2+, and proceeds in the absence of divalent cations. The purified protein inhibitor of phosphatase 1, inhibitor-2, inhibits dephosphorylation in a dose dependent manner. The calmodulin antagonists trifluoperazine and calmidazolium also block dephosphorylation, suggesting the presence of phosphatase 2-B. This study suggests the possible co-localization of a particulate associated cAMP-dependent protein kinase and associated phosphatases with their phosphorylated protein substrates in the insect brain. |
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