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Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling -

Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling

Ludwig M.G.Jr. Heilmeyer (Herausgeber)

Buch | Softcover
XI, 376 Seiten
2011 | 1. Softcover reprint of the original 1st ed. 1993
Springer Berlin (Verlag)
978-3-642-78249-7 (ISBN)
CHF 149,75 inkl. MwSt
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Proceedings of the NATO Advanced Study Institute on Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling, held at Acquafredda di Maratea, Italy, September 1-12, 1992
Nearly every cellular activity, such as cell growth,
proliferation, protein synthesis, and nuclear division, is
regulated by protein phosphorylation/dephosphorylation on
tyrosine residues as initiation events.Synchronization
occurs through interaction of protein tyrosine kinases and
phosphatases.
This book unveils signal pathways that connect
extracellular signals with changes of phosphorylation state
of target proteins allowing coordinated and integrated
modulation of mitogenic signalling. Specifically, cascades
involving protein serine/threonine kinases and connections
to phosphoinositides derived second messengers are
discussed.

I. Protein Tyrosine Kinases and Protein Tyrosine Phosphate Phosphatases.- Protein tyrosine phosphorylation-dephosphorylation and cell signaling.- Regulation and functions of src-family kinases: An update.- Mitogen-activated signalling pathways.- Studies of the very early responses of a receptor tyrosine kinase to growth factor binding and their application to the purification and identification of proteins that are tyrosine phosphorylated in the growth factor response.- The role of P21ras in cell signalling.- The HGF/SF receptor kinase: Structure and function.- RET/ptc and TRK oncogenes in papillary thyroid carcinoma.- Structure-function analysis of hepatocyte growth factor and its tyrosine-ldnase receptor c-Met.- Oncogenic activation of the Met/HGF receptor tyrosine kinase is promoted by leucine zipper mediated dimerization.- Specificity of the truncated form of human T-cell protein tyrosine phosphatase toward phosphorylated synthetic peptides.- Regulation of tyrosine protein phosphatases by binding to phospholipids and covalent modification.- Localization-dependent regulation of lymphocyte tyrosine phosphatases.- Protein tyrosine phosphatases in the nematode ascaris suum.- Non-radioactive determination of phosphotyrosine phosphatase (PTPase) activity.- New protein tyrosine phosphatases from vascular smooth muscle cells: Transcript levels in tissues and in cultured cells.- Recombinant CSK expressed in E. Coli is phosphorylated on tyrosine residue(s) and undergoes in vitro phosphorylation.- Polysine activates a splenic tyrosine protein kinase encoded by the fgr protooncogene.- Protein phosphorylation in the signal transduction of the neuropeptide bombesin in swiss 3T3 cells.- Growth hormone (GH) increases lipoprotein lipase mRNA in cells transfected with the rat GH receptor cDNA.- II. The Phosphatidylinositol Signalling System.- Role of phosphatidylinositol 3-kinase in growth factor and oncogene signaling.- Isolation and characterization of phosphatidylinositol 4-kinase isoenzymes from bovine brain.- Determination of phosphoinositides and inositol phosphates. Principles and rules.- Phosphoinositides in rabbit skeletal muscle membranes.- Renaturation of phosphatidylinositol 4- and phosphatidylinositol 4-phosphate 5?-kinases following polyacrylamide gelelectrophoresis in presence of SDS. Studies on their substrate binding requirements using synthetic substrate analogues.- III. Serine/Threonine Protein Kinases.- The catalytic subunit of cAMP-dependent protein kinase.- Casein kinase I and the classification of protein kinases: What's in a name?.- Downregulation of protein kinase C is associated with phenotypic changes and enhanced proliferation of vascular smooth muscle cells.- Insulin-stimulated seryl/threonyl protein kinases in diabetic rats and the effects of vanadium treatment.- Protein phosphorylation in prokaryotes - evidence for pkc-like activities in Escherichia Coli.- Phosphorylation of creatine kinase in myogenic cells: Effects of okadaic acid and other agents affecting cellular protein phosphorylation.- Non-radioactive determination of phosphoamino acids by capillary electrophoresis.- Characterization of phosphoproteins by 31P-NMR spectroscopy.- CK-2, a multifunctional protein kinase and its role during proliferation.- IV. Protein Serine/Threonine Phosphate Phosphatases.- Molecular complexity of protein phosphatase 2A holoenzymes and delineation of their function.- Dephosphorylation in vitro inhibits ligand and DNA binding activities of human estrogen receptor.- Characterization of novel nuclear inhibitors of proteinphosphatase-1.- V. S6-Phosphorylation.- The mitogen-activated p70s6k / p85s6k.- Expression of the p70s6k / p85s6k isoforms from a single gene and activation following mitogenic stimulation.- Control of S6 phosphorylation in normal and v-src transformed cells.- The phosphorylated ribosomal protein in tetrahymena is homologous with mammalian ribosomal protein S4.- Nucleocytoplasmic transport of ribosomal protein S6.- VI. Cell-Cycle-Control.- Regulating the G2 checkpoint in the cell cycle.- CD2-dependence on the CD3-zeta-chain in T cell signalling - shown by inhibitory and modifying effects of cholera toxin.- cdc25 protein phosphatase in mammalian fibroblasts: cell cycle expression and intracellular localization.- VII. Control of Intracellular Ca2+.- The role of small molecular weight GTP-binding proteins in stimulus secretion coupling of pancreatic acinar cells.- Characterization of calcium transport ATPase isozymes in different blood cells.

Erscheint lt. Verlag 21.12.2011
Reihe/Serie Nato ASI Subseries H:
Zusatzinfo XI, 376 p. 39 illus.
Verlagsort Berlin
Sprache englisch
Maße 155 x 235 mm
Gewicht 597 g
Themenwelt Medizin / Pharmazie Medizinische Fachgebiete Onkologie
Naturwissenschaften Biologie Biochemie
Naturwissenschaften Biologie Zellbiologie
Schlagworte Amino acid • ATP • Calcium • Cell • DNA • Growth factors • hormones • Membrane • membrane receptors • Membranrezeptoren • Oncogene • Oncogenes • Onkogene • Phosphatase • phosphatse • phosphorylation • Protein • Proteinkinase • Protein Kinase • proteins • Protein synthesis • receptor • synthesis • Wachstumsfaktoren
ISBN-10 3-642-78249-3 / 3642782493
ISBN-13 978-3-642-78249-7 / 9783642782497
Zustand Neuware
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