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Current Topics in Cellular Regulation, Volume 21 examines the advances in the general area of cellular regulation. This book discusses the roles of eukaryotic initiation factor 2 ancillary factors in the regulation of eukaryotic protein synthesis initiation and phosphorylation state of eIF-2. The monoclonal antibodies to cap-binding proteins, criteria for establishment of the biological significance of ribosomal protein phosphorylation, and comparison with casein kinases from mammary gland are also elaborated. This text likewise covers the regulation of phosphoprotein phosphatases, poly(ADP-ribosyl)ation reactions in vitro, and induced commitment to terminal erythroid differentiation. Other topics include the turnover characteristics of lactate dehydrogenase and role of urea synthesis in the removal of metabolic bicarbonate and regulation of blood pH. This volume is useful to biologists and researchers interested in basic mechanisms involved in the regulation of diverse cellular activities.
Language
Place of publication
Publishing group
Elsevier Science & Techn.
ISBN-13
978-1-4832-1720-8 (9781483217208)
Schweitzer Classification
List of ContributorsRoles of Eukaryotic Initiation Factor 2 Ancillary Factors in the Regulation of Eukaryotic Protein Synthesis Initiation I. Introduction II. eIF-2 III. Co-eIF-2A IV. Co-eIF-2B V. Co-eIF-2C VI. eIF-2 Kinases VII. RF VIII. A Proposed Mechanism for Regulation of the Early Steps in Peptide Chain Initiation in Reticulocyte Lysates by eIF-2 Ancillary Factors IX. Concluding Remarks ReferencesThe Role of Phosphorylation in the Regulation of Eukaryotic Initiation Factor 2 Activity I. Introduction II. Translational Control in Rabbit Reticulocyte Lysate III. Phosphorylation State of eIF-2 IV. Is Ternary Complex Formation the Only Initiation Step Affected in Hemin-Deficient Lysate? V. Other Modifications of eIF-2 Which Provide Insights into the Regulation of Its Activity VI. Role of Phosphorylation in the Regulation of eIF-2 Activity VII. Summary ReferencesProbing the Function of the Eukaryotic 5'-Cap Structure Using Monoclonal Antibodies to Cap-Binding Proteins I. Introduction II. Monoclonal Antibodies to Cap-Binding Proteins III. Reaction of Monoclonal Antibodies with High-Molecular-Weight Proteins Antigenically Related to the 24-Cap-Binding Protein IV. ATP-Mg2+-Dependent Cross-Linking of Cap-Binding Proteins to mRNA V. Effect of Anti-Cap-Binding Protein Monoclonal Antibodies on Protein Synthesis VI. Cap-Binding Proteins and the Cytoskeleton VII. Summary ReferencesCriteria for Establishment of the Biological Significance of Ribosomal Protein Phosphorylation I. Introduction II. Methodology III. Changes in Vivo IV. Signaling Systems V. Reconstruction in Vitro ReferencesCasein Kinases-Multipotential Protein Kinases I. Introduction II. Physicochemical Characterization III. Substrate Specificity IV. Comparison with Casein Kinases from Mammary Gland V. Regulation VI. Phosphorylation of Endogenous Proteins VII. Criteria for Classification of Casein Kinases VIII. Conclusions ReferencesPhosphoprotein Phosphatases I. Introduction II. Multiple Forms and Substrate Specificity of Phosphoprotein Phosphatases III. Purification and Properties of the Mr = 35,000 Phosphoprotein Phosphatases IV. Relationship Between Phosphoprotein Phosphatases and Alkaline Phosphatases V. Heat-Stable Protein Effectors VI. High-Molecular-Weight Forms of Type I Phosphoprotein Phosphatase VII. Regulation of Phosphoprotein Phosphatases VIII. Conclusion References Note Added in ProofADP-Ribosylation Reactions I. Mono(ADP-Ribosyl)ation and Poly(ADP-Ribosyl)ation II. Poly(ADP-Ribosyl)ation Reactions in Vitro III. Poly(ADP-Ribosyl)ation and DNA Repair IV. Conclusions ReferencesCommitment to Terminal Differentiation and the Cell Cycle I. Introduction II. Induced Commitment to Terminal Erythroid Differentiation III. Characteristics of the Commitment Process IV. Inducer Effects in Relation to the Cell Division Cycle V. Relation of the Cell Cycle to the Replication of a- and ß-Globin DNA Sequences in Erythroleukemia Cells VI. Summary ReferencesThe Turnover Characteristics of Lactate Dehydrogenase I. Introduction II. Methodological Considerations III. Isozyme Turnover IV. Physiological Variations V. Biodegradation and Its Regulation VI. Concluding Comments ReferencesThe Role of Urea Synthesis in the Removal of Metabolic Bicarbonate and the Regulation of Blood pH I. Introduction II. The Problem: Need for Disposal of HCO3- III. The Solution: Acquisition of Proton from NH4+ IV. The Role of the Kidney V. Regulation VI. Discussion VII. Summary VIII. Appendix A: Equations for Relevant Catabolic Reactions or Processes IX. Appendix B: Necessity for Disposal of HCO3- ReferencesIndexContents of Previous Volumes