Calcium and Cell Function

ContributorsPrefaceContents of Previous VolumesChapter 1 Peptides Recognizing Calmodulin I. Introduction II. Methods for the Determination of Peptide-Calmodulin Interaction In Vitro III. Overview of Calmodulin-Binding Peptides IV. Competitive Relationships and Stoichiometry V. Peptide Binding by Proteolytic Fragments of Calmodulin VI. Peptide Associations with Proteins Related to Calmodulin VII. Do Calmodulin and the cAMP-Dependent Protein Kinase Act on Similar Recognition Sequences? VIII. Peptides as Structural and Spectroscopic Probes of Calmodulin IX. Peptides as Useful Calmodulin Antagonists X. Summary ReferencesChapter 2 Molecular and Regulatory Properties of Calmodulin-Dependent Phosphodiesterase from Brain I. Introduction II. Enzymatic and Physical Properties of Phosphodiesterase III. Use of Calmodulin Derivatives to Probe the Mechanism of Calmodulin Activation IV. Future Directions ReferencesChapter 3 Calmodulin-Dependent Protein Phosphatase I. Introduction II. Historical Background III. Assay IV. Distribution V. Purification VI. Molecular Properties VII. Identification of the Catalytic Subunit VIII. Stimulation by Calcium and Calmodulin IX. Stimulation by Limited Trypsinization X. Regulation by Divalent Cations XI. Deactivation by Calcium and Calmodulin XII. Substrate Specificity XIII. Concluding Remarks ReferencesChapter 4 Biophysical Studies of Calmodulin I. Introduction II. Proteolytic and Chemical Modification of CaM III. Calcium-Binding Studies IV. Thermochemical Studies V. Stopped-Flow Kinetic Studies of CaM and Its Proteolytic Fragments VI. NMR and ESR Studies VII. Fluorescence and Luminescence Studies VIII. Localization of Interaction Sites on Calmodulin IX. Concluding Remarks ReferencesChapter 5 Regulation of Ca2+-Dependent Proteinase of Human Erythrocytes I. Introduction II. The Proteolytic Enzymes of Human Erythrocytes III. Physical Properties IV. Effect of High Concentrations of Calcium Ions on the Activity of Calpain V. Effect of Substrate on the Conversion of Procalpain to Active Calpain at Micromolar Ca2+ Concentrations VI. The Molecular Basis of the Conversion of Procalpain to Active Calpain VII. Mechanism of Procalpain Activation VIII. Specificity and Selectivity of Proteolytic Digestion by Calpain IX. Regulation of Human Erythrocyte Calpain X. Physiological Function of Calpain in Human Erythrocytes ReferencesChapter 6 Toxicological Implications of Perturbation of Ca2+ Homeostasis in Hepatocytes I. Introduction II. Calcium and Tissue Toxicity III. Calcium Compartmentation in the Hepatocyte IV. Methods Used to Study Calcium Compartmentation in Hepatocytes V. Perturbation of Calcium Homeostasis During Oxidative Cell Injury VI. Relationship Between Perturbation of Calcium Homeostasis and Alterations in Surface Morphology (Hepatocyte Blebbing) VII. Concluding Remarks ReferencesChapter 7 The Role of Calcium in Meiosis I. Introduction II. Oocytes and Eggs from Various Species as Model Systems III. Biochemical and Biophysical Events During Vertebrate Meiotic Divisions IV. Exogenous Calcium and Magnesium Requirements During Meiosis V. Calcium Redistribution Associated with the Resumption of Meiosis VI. Calcium Redistribution Associated with Nuclear Breakdown and Arrest at Metaphase II VII. Calcium Redistribution following Fertilization VIII. Summary Addendum ReferencesChapter 8 Calcium and the Control of Insulin Secretion I. Introduction II. Insulin Release and Extracellular Calcium III. Insulin Release and Intracellular Calcium IV. Insulin Release and Binding of Calcium to the ß-Cell Surface V. Calcium Content of the ß-Cell VI. Calcium Transport Across the Plasma Membrane VII.