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  • 1
    Keywords: Biochemistry ; Medical laboratories ; Protein Science ; Laboratory Medicine ; Springer eBooks
    Description / Table of Contents: Using Data Mining to Explore Calmodulin Bibliography -- Deep Two-Photon Imaging In Vivo with a Red-Shifted Calcium Indicator -- High Resolution Calcium Imaging Method for Local Calcium Signaling -- Measurement of Contractility and Calcium Release in Cardiac Spheroids -- Simultaneous Recording of Subcellular Ca2+ Signals from the Cytosol and Sarco/Endoplasmatic Reticulum: Compartmentalized Dye Loading, Imaging, and Analysis -- The Use of Complementary Luminescent and Fluorescent Techniques for Imaging Ca2+ Signalling Events during the Early Development of Zebrafish (Danio rerio) -- Cellular Ca2+-Responding Nanoluciferase Reporter Gene System Directed by Tandemly Repeated Pseudo-Palindromic NFAT-Response Elements -- Designing Calcium Binding Proteins for Molecular MR Imaging -- Coordination to Divalent Cations by Calcium Binding Proteins -- Chaperoning against Amyloid Aggregation: Monitoring In Vitro and In Vivo -- Ca2+-Binding Proteins of the EF-Hand Superfamily: Diagnostic and Prognostic Biomarkers and Novel Therapeutic Targets -- Gene Transfer of Calcium Binding Proteins into Adult Cardiac Myocytes -- Expression and Purification of Calmodulin for NMR and Other Biophysical Applications -- The Use of Cre-loxP Inducible Mouse Models to Dissect the Specific Roles of Calcineurin Signalling in Myeloid Cells -- Calpain Purification through Calpastatin and Calcium: Strategy and Procedures -- Characterization of the EF-Hand Calcium-Binding Domains of Human Plastins -- Expression and Characterization of MICU2, a Ca2+ Sensor Protein -- S100 Proteins in the Innate Immune Response to Pathogens -- Targeting S100 Calcium-Binding Proteins with Small Molecule Inhibitors -- Monitoring Interactions between S100B and the Dopamine D2 Receptor Using NMR Spectroscopy -- Isolation and Characterization of S100 Protein-Protein Complexes -- The Multifaceted S100A4 Protein in Cancer and Inflammation -- Interaction of S100A6 with Target Proteins In Vitro and in Living Cells -- Preparation of the Oxidized and Reduced Forms of Psoriasin (S100A7) -- Preparation and Iron Redox Speciation Study of the Fe(II)-Binding Antimicrobial Protein Calprotectin -- Structural Analysis of S100A8 Complex with Zinc and Calcium: A General Protocol for the Study of S100 Proteins in the Presence of Divalent Cations by X-Ray Crystallography -- Analysis of Ca2+-Dependent Weibel-Palade Body Tethering by Live Cell TIRF Microscopy: Involvement of a Munc13-4/S100A10/Annexin A2 Complex -- Analysis of S100A11 in DNA Damage Repair -- Fluorine-18 Labeling of S100 Proteins for Small Animal Positron Emission Tomography -- Reviewing the Crystal Structure of S100Z and Other Members of the S100 Family: Implications in Calcium-Regulated Quaternary Structure -- High Sensitive Quantitative Binding Assays Using a Nanoluciferase-Fused Probe for Analysis of ALG-2-Interacting Proteins -- Calcium-Induced Protein Folding in Calumenin and Calmodulin -- Measuring Calumenin Impact on ER-Calcium Depletion Using Transient Calumenin Overexpression and Silencing -- Secretagogin Purification and Quality Control Strategies for Biophysical and Cell Biological Studies -- Tryptophan Scanning Mutagenesis of EF-Hand Motifs -- Mapping Calcium-Sensitive Regions in GCAPs by Site-Specific Fluorescence Labeling -- Quantification of Human Swiprosin-1/EFhd2 Expression on Protein and RNA Level -- Three-Dimensional Reconstruction Imaging Method to Study the Function of EFHD2 in Invadopodia Formation -- Characterization of Calcium-Binding Proteins from Parasitic Worms -- High-Sensitivity Troponin Assays in Clinical Diagnostics of Acute Coronary Syndrome -- Targeted Mass Spectrometry of S100 Proteins -- Clinical Use of the Calcium-Binding S100B Protein, a Biomarker for Head Injury -- Serum S100B Levels in Melanoma -- The Ca2+-Binding S100B Protein: An Important Diagnostic and Prognostic Neurobiomarker in Pediatric Laboratory Medicine -- S100A7 in Psoriasis: Immunodetection and Activation by CRISPR -- S100A8/A9 in Myocardial Infarction -- Enzyme-Linked Immunosorbent Assay to Measure S100A12 in Fecal Samples of Children and Adults -- S100 Proteins as Biomarkers in Risk Estimations for Malignant Transformation in Oral Lesions
    Abstract: This detailed volume explores protocols for studying the many facets of Ca2+-imaging, Ca2+-signaling, and Ca2+-binding along with background information on the principles and application of these techniques. The content of the book delves into 48 chapters including subjects such as data analysis and modern technologies to study calcium-binding and signaling in cells, the superfamily of calcium-binding proteins characterized by the EF-hand structural motif, as well as their use as diagnostic and prognostic biomarkers in Laboratory Medicine and novel therapeutic drug targets. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and comprehensive, Calcium-Binding Proteins of the EF-Hand Superfamily: From Basics to Medical Applications presents state-of-the-art, lab-based methods and easy-to-follow protocols for daily use, making it interesting for basic and medical researchers, cell- and molecular biologists, clinicians, clinical chemists, and the diagnostic industry
    Pages: XIX, 779 p. 175 illus., 117 illus. in color. : online resource.
    ISBN: 9781493990306
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  • 2
    Keywords: Life sciences ; Biochemistry ; Life sciences ; Protein Science ; Protein Structure ; Springer eBooks
    Abstract: A major direction in medical research leading to clinical applications℗ targets the regulation of intracellular calcium and the various human diseases associated with an altered homeostasis of this global second messenger. These diseases include, for example: cardiomyopathy, inflammation, brain disorders, diabetes and cancer. In Calcium Binding Proteins and RAGE: from Structural Basics to Clinical Applications, expert researchers in the field detail many of the methods which are now commonly used to study calcium binding proteins. These methods and techniques, such as calcium-measurements, screening methods, clinical chemistry, and therapy, are generally applicable to many other areas of basic and medical research as well as to diagnostics. Written in the highly successful Methods in Molecular Biologý„Ø series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. ℗ Authoritative and practical, Calcium Binding Proteins and RAGE: from Structural Basics to Clinical Applications underlines the diagnostic and clinical importance of this family of proteins in human diseases and as drug targets
    Pages: XIV, 423 p. 85 illus., 56 illus. in color. : digital.
    ISBN: 9781627032308
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  • 3
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  S100 proteins are calcium-binding proteins of the EF-hand superfamily and are involved in the regulation of a number of cellular processes. The present study deals with the immunohistochemical expression of S100A1 and S100A6 in the rat submandibular and sublingual glands during postnatal development from day 0 to 12 weeks. Expression of S100A1 was particularly concentrated in pillar and transition cells in the granular convoluted tubule (GCT) and in striated duct cells of the submandibular gland age 4 weeks to maturity. None or only weak staining for S100A1 was observed in the duct segment at 0–5 days. On the contrary, immunostaining of S100A6 was present in proacinar cells in undifferentiated submandibular gland at age 3 days to 2 weeks. S100A6 immunoreactivity in rat submandibular gland coexisted with chromogranin reactivity. It is possible that S100A6 regulates secretion of chromogranin in proacinar cells. Secretion of growth factors and biologically active peptides in the GCT are regulated by calcium signals, and S100A1 may be involved in the secretory mechanism of granular cells. S100A1 and S100A6 are potentially of great importance in secretory functions of granular cells and proacinar cells, as well as in rat salivary glands.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The bifunctional protein PCD/DCoH is both a pterin-4α-carbinolamine dehydratase (PCD) involved in the recycling of tetrahydrobiopterin (BH4) and a dimerisation cofactor (DCoH) of the hepatic nuclear factor 1α (HNF-1α). An antiserum raised against rat PCD/DCoH was used to localise the protein in peripheral organs. In liver, all the hepatocytes but not the other cell types are immunoreactive. In kidney, the protein is prevalent in the proximal and distal convoluted tubules. In adrenals, all the cells of the medulla are labelled. Positive nerve cells occur in myenteric ganglia of the whole gastrointestinal tract and in the intestinal submucous ganglia. Many positive endocrine cells are present in the epithelium. The immunoreactivity is either cytoplasmic (hepatocytes, convoluted tubules of the kidney and part of the gastrointestinal endocrine cells) or prominently nuclear (kidney collecting tubules, adrenals, intestinal neural plexuses and part of the gastrointestinal endocrine cells). Our results show that PCD/DCoH is present in cells expressing enzymes that use BH4 as a cofactor and/or HNF-1α. In addition, PCD/DCoH is present in other cells, for example, neurons in the submucosal plexus. This fact and the prominent nuclear immunoreactivity found in all the positive cells derived from the neural crests argue in favour of a new, still unknown function for the protein.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1106
    Keywords: Parvalbumin ; GABA ; Nonpyramidal cell ; Monoclonal antibody ; Lectin ; Cerebral cortex ; Proteoglycan ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Monoclonal antibody (MAb) 473 is shown to outline selectively a subpopulation of GABAergic neurons containing a specific calcium-binding protein parvalbumin (PV) in the adult rat parietal cortex, using preembedding immunocytochemistry at the light microscopic level. About 90% of MAb 473 stained cells in the rat parietal cortex were PV immunoreactive. Thus we compared MAb 473 staining with that of three chemical probes, previously shown to stain selectively a subpopulation of PV-containing GABAergic neurons in this brain region, namely, a lectin, Vicia villosa agglutinin (VVA), with a specific affinity for terminal N-acetylgalactosamine, MAb 3B3 which is specific for chondroitin sulfate proteoglycan and MAb HNK-1 which is specific for some types of carbohydrate epitope containing a sulfated derivative of glucuronic acid. About 85% of MAb 473 immunoreactive cells were shown to be stained with VVA. Furthermore about 90% of MAb 473 immunoreactive cells were also stained with MAb 3B3. Thus MAb 473 positive cells were almost included into VVA and/or MAb 3B3 positive cells. On the other hand only about 34% of MAb 473 positive cells were HNK-1 positive, whereas about 44% of HNK-1 positive cells were MAb 473 positive. Thus these two MAbs defined different, though partially overlapping, subsets of PV-containing GABAergic neurons in the rat parietal cortex.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-2307
    Keywords: Key words Ca2+-binding S-100 proteins ; Epithelial tumours ; Skin ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The Ca2+-binding proteins S100A1, S100A2, S100A4, S100A6 and S100B were evaluated immunohistochemically in normal skin and skin appendage tumours. Epidermal basal cells, epithelial cells of sebaceous glands, hair follicle sheet epithelia and eccrine duct reacted strongly with an antiserum against human S100A2 but were nonreactive or weakly reactive to S100A1, S100A4, S100A6 and S100B. Varying types of skin appendage tumours and most peripheral cells in tumour nests of basal cell carcinoma and squamous cell carcinoma showed positive S100A2 immunoreactivity in neoplastic cells corresponding to basal cells but were nonreactive or faintly reactive for other S100 proteins. Langerhan’s cells and melanocytes were labelled by S100B. Basophilic cells of calcifying epithelioma were occasionally stained with S100A2 antiserum. Eccrine poroma did not react with any S100 antiserum. Mixed tumours of the skin containing neoplastic myoepithelial cells stained strongly for S100A2 and S100B but only faintly for S100A1, S100A4, S100A6. This is the first report on selective evaluation of different S100 proteins in normal skin. These antibodies are valuable tools for better characterization of skin appendage tumours.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 715-721 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The Ca2+-binding S-100 proteins are involved in the regulation of a number of cellular processes and an altered expression has been reported in several neoplastic tissues. Tissue specimens of normal salivary glands (n = 23). pleomorphic adenomas (n=60). basal cell adenomas (n=6). canalicular ademomas (n=2), myoepitheliomas (n = 2). adenoid cystic carcinomas (n=26) and adenocarcinomas NOS (n=11) were evaluated for the expression of S-100A1, S-100A2. A-100A4, S-100A6 and S-100B by using highly specific polyclonal and monoclonal antibodies generated against the recombinant human protein. In normal salivary glands, the ductal cells showed mild to intense immunoreactivity for S-100A 1, S-100A2. S-100A4and S-100A6, while S-100B was observed in nerve fibers in the connective tissue. The normal myoepithelial cells were unreactive. In pleomorphic adenoma, the luminal tumor cells of the duct-like structures showed moderate to intense immunoreactivity for S-100A2. while reactivity for S-100A 1. S-100A4 and S-100A6 was relatively weak. The non-luminal cells, also termed neoplastic myoepithelial cells, showed immunoreactivity for S-100B, while tumor cells in the solid, myxoid and chondroid areas were immunoreactive for S-100A 1. S-100A4, S-100A6 and S-100B. The non-luminally located tumor cells in basal cell adenomas and canalicular adenomas, and numerous tumor cells in clusters in myoepitheliomas were intensely reactive for S-100A2. In adenoid cystic carcinomas and in adenocarcinomas not otherwise specified, the luminal cells forming the tubular or cribriform structures were markedly positive for S-100A2 and/or S-100A6. Squamous metaplastic cells in salivary tumors showed intense immunoreactivity for S-100A2. The results of the present study suggest that the majority of the tumor ceils in salivary neoplasms, despite the most heterogeneous tumor cell differentiation, express S-100 proteins more heterogeneously than the normal glandular ducts. The salivary ducts in normal glands, the luminal tumor cells and squamous metaplastic cells in the neoplastic lesions were intensely immunoreactive for S-100A2 as compared to S-100A1, S-100A4orS-100A6. In contrast, the non-luminal tumor cells showed a rather heterogeneous expression of the S-100 proteins.
    Type of Medium: Electronic Resource
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