Calcium Binding Proteins in Normal and Transformed Cells

Paperback (Softcover reprint of the original 1st ed. 1990)
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Editorial Reviews

Booknews
Among the noteworthy items are the growing number of abundant proteins which interact with calcium and sometimes with other second messenger systems. New structure/function relationships on calbindin D9K and calmodulin have emerged from NMR and site-directed mutagenesis studies. Questions of function are raised for many calcium-binding protein families. Annotation c. Book News, Inc., Portland, OR (booknews.com)
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Product Details

  • ISBN-13: 9781468457568
  • Publisher: Springer US
  • Publication date: 3/28/2012
  • Series: Advances in Experimental Medicine and Biology Series, #269
  • Edition description: Softcover reprint of the original 1st ed. 1990
  • Pages: 224
  • Product dimensions: 7.00 (w) x 10.00 (h) x 0.48 (d)

Table of Contents

Calcium and Steady States.- Genes of Calcium Binding Protein Family.- Evolution of the “ef-Hand” Family of Calcium-Binding Proteins.- Functional Analysis of the Promoter Region of the Gene Encoding Chicken Calbindin-D28K.- Structure of the Human cDNAs and Genes coding for Calbindin-D28K and Calretinin.- Calbindin-D9K (CaBP9K) Gene: a Model for Studying the Genomic Actions of Calcitriols and Calcium in Mammals.- Structure/Function Relationships.- Protein Engineering and Structure/Function Relations in Bovine Calbindin D9k.- Mutant Analysis Approaches to Understanding Calcium Signal Transduction through Calmodulin and Calmodulin Regulated Enzymes.- Parvalbumin, Molecular and Functional Aspects.- Unique Calcium Binding Proteins in Invertebrates.- Structure of the Calcium Release Channel of Skeletal Muscle Sarcoplasmic Reticulum and its Regulation by Calcium.- Structural and Functional Investigation of p68 - a Protein of the Lipocortin/Calpactin Family.- Structure-Function Relations in Troponin C. Chemical Modification Studies.- Ca2 -Dependent Mobility Shift of Parvalbumin in one and two-Dimensional Gel Electrophoresis.- The Cytoskeleton and Calcium Binding Proteins.- Role of Calcium in Secretion and Synthesis in Bovine Adrenal Chromaffin Cells.- Ca2+-Binding Proteins as Component of the Cytoskeleton.- S-100 Proteins: Relationships with Membranes and the Cytoskeleton.- Calcium Binding Proteins In Transformed Cells.- Oncomodulin in Normal and Transformed Cells.- Perturbation of the Calmodulin System in Transformed Cells.- High Levels of oncomodulin and Calmodulin Expression in the Log Phase of Cell Growth in a Chemically Transformed rat fibroblast Cell Line.- Calmodulin and Calbindin in Pancreatic Islet Cells.- Calcium/Lipid-Binding Proteins.- Structural and Functional Characterization of Protein I (p362p112) and II (p32)-Calcium/Phospholipid Binding Proteins with Homologies to Lipocortin I.- Possible Role for two Calcium-Binding Proteins of the S-100 Family, Co-Expressed in Granulocytes and Certain Epithelia.- Phosphorylation of the Calcium-Binding Protein, p68, in the Submembranous Cytoskeleton of Human Placental Syncytiotrophoblast.- Calcyclin-Like Protein from Ehrlich Ascites Tumour Cells - Ca2 - Binding Prpperties, Distribution and Target Protein.- Calcium Binding Proteins Substrates.- Interactions of S-100 Proteins with Proteins Kinases Substrates. Biological implication.- Novel and Selective Inhibitors of CaM-KinaseII and other Calmodulin-Dependent Enzymes.- Structural Details of the Interaction of Calmodulin with the Plasma Membrane Ca2-ATPase.- Erythrocyte Ca2 -ATPase: Activation by Enzyme Oligomerization versus by Calmodulin.- Calpain I Activates Ca2 Transport by the Human Erythrocyte Plama Membrane Calcium Pump.- Inhibitory Regulation by Calcium Ion of Myosin ATPase Activity: Binding of Calcium Ion and Phosphorylation of Myosin.- Immunohishemistry of Calbindin and Calretinin.- Parvalbumin Expression in Normal and Mutant Xenopus Embryos.- Calretinin and other CaBPs in the Nervous System.- Immunohishemical Detection of 28KDa Calbindin in Human Tissues.- Comparison Between Rat Brain Calbindin and Calretinin Immunoreactivities.- Contributors.

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