Protein Kinase C and its Brain Substrates book cover

Protein Kinase C and its Brain Substrates

Role in Neuronal Growth and Plasticity

This volume summarizes the presentations made at the third international meeting of its kind, held in Zeist, The Netherlands. The two previous conferences had witnessed the increasing importance of brain phosphoproteins in the study of the brain. The rapid acceleration in our knowledge is evident as we progress from a period of characterizing spots on a gel to considering their physiological implications from a diversity of fields: behavioral psychology, neurophysiology, pharmacology, cellular and molecular biology, each providing a view of brain phosphoprotein function from a unique perspective. The present volume retains as its primary focus the function of those nervous system proteins that are kinases or substrates for kinases, and reveals the first wave of research emerging from the cloning of the cDNA for both kinase and substrate. An incisive presentation focusing on protein kinase and its substrates is included in the volume and provides the basis for discussion for many of the subsequent contributions.

Included in series
Progress in Brain Research

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Published: December 1991

Imprint: Elsevier

ISBN: 978-0-444-81436-4

Contents

  • Preface. Participants. Section I: Structure and Characteristics of the Growth and Plasticity Associated PKC Substrate B-50/F1/GAP-43/neuromodulin. 1. B-50: structure, processing and interaction with ACTH (H. Zwiers and P.J. Coggins). 2. GAP-43: purification from a prokaryotic expression system, phosphorylation in cultured neurons, and regulation of synthesis in the central nervous system (S.K. Doster, A.M. Lozano, S.M. Shuh, S. Spencer and M.B. Willard). 3. Selective phosphorylation and dephosphorylation of the protein B-50 (L.A. Dokas, M.R. Pisano and Y.-F. Han). 4. Mutagenesis of the calmodulin binding domain of neuromodulin (E.R. Chapman, D. Au, T.A. Nicolson and D.R. Storm). Section II: Regulation of Expression of B-50/F1/GAP-43/neuromodulin. 5. Expression of the growth- and plasticity-associated neuronal protein, GAP-43, in PC12 pheochromocytoma cells (B. Costello, L.-H. Lin, A. Meymandi, S. Bock, J.J. Norden and J.A. Freeman). 6. The expression of GAP-43 in relation to neuronal growth and plasticity: when, where, how, and why? (L.I. Benowitz and N.I. Perrone-Bizzozero). 7. GAP-43 and neuronal remodeling (M.C. Fishman and D. Valenzuela). 8. Regulation of gene expression in the olfactory neuroepithelium: a neurogenetic matrix (F.L. Margolis, J. Verhaagen, S. Biffo, F. Huang and M. Grillo). Section III: Structure and Characteristics of Protein Kinases. 9. Protein kinase C family and nervous function (Y. Nishizuka, M.S. Shearman, T. Oda, N. Berry, T. Shinomura, Y. Asaoka, K. Ogita, U. Kikkawa, A. Kishimoto, A. Kose, N. Saito and C. Tanaka). 10. Protein kinase C subtypes and their respective roles (K.-P. Huang, F.L. Huang, C.W. Mahoney and K.-H. Chen). 11. Regional distribution and properties of an enzyme system in rat brain that phophorylates ppH-47, an insoluble protein highly labelled in tissue slices from the hippocampus (R. Rodnight, C.A. Gonçcalves, R. Leal, E. Rocha, C.G. Salbego and S.T. Wofchuk). 12. Molecular and cellular studies on brain calcium/calmodulin-dependent protein kinase II (T.R. Soderling, K. Fukunaga, D.A. Bricket, Y.L. Fong, D.P. Rich, K. Smith and R.J. Colbran). Section IV: Plasticity and Function of the PKC substrate B-50/F1/GAP-43/neuromodulin. 13. Protein kinase C substrate B-50 (GAP-43) and neurotransmitter release (P.N.E. de Graan, A.B. Oestreicher, P. Schotman and L.H. Schrama). 14. Transmitter release: target of regulation by protein kinase C? (L.V. Dekker, P.N.E. de Graan and W.H. Gispen). 15. Activation of protein kinase C phosphorylation pathways: a role for storage of associative memory (D.S. Lester and D.L. Alkon). 16. A tale of two contingent protein kinase C activators: both neutral and acidic lipids regulate synaptic plasticity and information storage (A. Routtenberg). 17. The neuropil and GAP-43/B-50 in normally aging and Long-term potentiation: postsynaptic activation of Ca2+-dependent protein kinases with subsequent presynaptic enhancement (R. Malinow and R.W. Tsien).

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