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  • 1
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Centrosomes. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (511 pages)
    Edition: 1st ed.
    ISBN: 9780080488622
    Series Statement: Issn Series
    DDC: 572
    Language: English
    Note: Front Cover -- The Centrosome in Cell Replication and Early Development -- Copyright Page -- Contents -- Contributors -- Preface -- Chapter 1. The Centrosome and Parthenogenesis -- I. Introduction -- II. Toward a Functional Description of the Centrosome -- III. The Centrosome Organelle versus Self-Assembled Centers -- IV. Centrosome Reproduction and the Parthenogenetic Activity of the Centrosome -- V. Conclusion -- References -- Chapter 2. y-Tubulin -- I. Centrosomes and Microtubule Nucleation -- II. y-Tubulin and the Tubulin Superfamily of Proteins -- III. Distribution of y-Tubulin in Cells -- IV. Studies of y-Tubulin Function -- V. y-Tubulin and Microtubule Assembly: Current Knowledge and Unanswered Questions -- VI. Concluding Remarks -- References -- Chapter 3. y-Tubulin Complexes and Their Role in Microtubule Nucleation -- I. Introduction -- II. Biochemical and Structural Studies of y TuRC and y TuSC -- III. Evidence That y TuRC Is the Major Microtubule Nucleator at the Centrosome -- IV. The Mechanism of Microtubule Nucleation -- V. Concluding Remarks -- References -- Chapter 4. y-Tubulin of Budding Yeast -- I. Introduction -- II. Tubulins of Yeast -- III. Interactions between Tubulins -- IV. The g -Tubulin Complex in Yeast -- V. Future Directions -- References -- Chapter 5. The Spindle Pole Body of Saccharomyces cerevisiae: Architecture and Assembly of the Core Components -- I. Introduction -- II. SPB Duplication and Assembly of the Mitotic Spindle -- III. Structure of the SPB -- IV. SPB Core Components -- V. Assembly of the Core SPB Components -- VI. Transcriptional Regulation of Core SPB Components -- VII. Homologs of Spindle Pole Components in Other Organisms -- VIII. Future Directions -- References -- Chapter 6. The Microtubule Organizing Centers of Schizosaccharomyces pombe -- I. Introduction. , II. Cytoplasmic Microtubule Organizing Centers -- III. The Spindle Pole Body -- IV. Molecular Characterization of SPB Components -- V. Perspectives -- References -- Chapter 7. Comparative Structural, Molecular, and Functional Aspects of the Dictyostelium discoideum Centrosome -- I. Introduction -- II. Comparative Morphology of the Dictyostelium Centrosome -- III. Comparative Analysis of Dictyostelium Centrosome Duplication -- IV. Comparative Molecular Biology of the Dictyostelium Centrosome -- V. Conclusions -- References -- Chapter 8. Are There Nucleic Acids in the Centrosome? -- I. Introduction -- II. Do Centrioles or Centrosomes Contain DNA? -- III. Do Centrosomes Contain RNA? -- IV. Conclusions -- References -- Chapter 9. Basal Bodies and Centrioles: Their Function and Structure -- I. Introduction to Centrioles and Basal Bodies -- II. The Structure of Centrioles and Basal Bodies -- III. The Function of Basal Bodies and Centrioles as Revealed by Mutational Analysis -- IV. Basal Body/Centriole Replication -- References -- Chapter 10. Centriole Duplication and Maturation in Animal Cells -- I. Overview -- II. Centriole Lineage Patterns -- III. Structural Features of Centriole Maturation and Duplication -- IV. Centriolar Duplication, Maturation, and the Cell Cycle -- V. Centriolar Maturation and Centriolar Function -- VI. Ciliogenesis and Cell Cycle -- VII. Future Developments and Directions -- References -- Chapter 11. Centrosome Replication in Somatic Cells: The Significance of the G1 Phase -- I. Introduction -- II. The Cell Cycle in Somatic Mammalian Cells -- III. Electron Microscopic Descriptions of Centrosome Doubling, and the Cellular Events of Centrosome Replication -- IV. Spindle Pole Body Doubling in Yeast Cells -- V. Events in G1 That Trigger Centrosome Replication in Somatic Mammalian Cells -- VI. Summary -- References. , Chapter 12. The Coordination of Centrosome Reproduction with Nuclear Events during the Cell Cycle -- I. Introduction -- II. The Events of Centrosome Reproduction -- III. Controls for Centrosome Reproduction -- IV. Coordination of Centrosome Reproduction with Nuclear Events in the Cell Cycle -- References -- Chapter 13. Regulating Centrosomes by Protein Phosphorylation -- I. Introduction -- II. Protein Phosphorylation: A Major Theme in Cell Cycle Control -- III. Centrosome and Spindle Pole Body Dynamics through the Cell Cycle -- IV. In Control of Centrosome Duplication -- V. Regulating Microtubule Nucleation -- VI. Establishing a Bipolar Mitotic Spindle -- VII. Creating the Zygotic Centrosome -- VIII. Loss of Phosphorylation Control: Cancer Implications -- IX. Perspectives: Into the Next Millennium -- References -- Chapter 14. The Role of the Centrosome in the Development of Malignant Tumors -- I. Introduction -- II. Centrosome Defects and Abnormal Mitoses in Cancer -- III. Amplified Centrosomes and Aneuploidy -- IV. Excess Pericentriolar Material Is Associated with High Frequency of Abnormal Mitoses -- V. Centrosome-Associated Kinases and Cancer -- VI. Tumor Suppressor Proteins and the Centrosome -- VII. Maintenance of Cell and Tissue Polarity Minimizes Tumor Aggression in Model Systems -- VIII. Conclusions -- References -- Chapter 15. The Centrosome-Associated Aurora/Ipl-like Kinase Family -- I. Introduction -- II. The Aurora and Ipl-like Family: Structure, Regulation and Substrates -- III. Summary -- References -- Chapter 16. Centrosome Reduction during Mammalian Spermiogenesis -- I. Introduction -- II. Overview of Mammalian Spermiogenesis -- III. Stages of Centrosome Reduction during Spermiogenesis -- IV. Conclusions -- References. , Chapter 17. The Centrosome of the Early C. elegans Embryo: Inheritance, Assembly, Replication, and Developmental Roles -- I. Why C. elegans? -- II. Origin and Replication of the Zygotic Centrosomes -- III. The Central Role of the Centrosome-Pronucleus Complex in Specifying AP Polarity -- IV. Nuclear Positioning -- V. Concluding Remarks -- References -- Chapter 18. The Centrosome in Drosophila Oocyte Development -- I. Introduction -- II. The Germarium: Centrosomes Are Anchored to Achieve Polarized Cell Divisions -- III. The Oocyte MTOC -- IV. Meiosis -- V. Summary -- References -- Chapter 19. The Centrosome in Early Drosophila Embryogenesis -- I. Introduction -- II. Ultrastructure -- III. Composition -- IV. Duplication and Separation -- V. Fertilization and the First Mitotic Division -- VI. Precortical Divisions -- VII. Cortical Divisions -- References -- Chapter 20. Centrosome Maturation -- I. Introduction -- II. Centrosome Maturation -- III. Centrosome Structure and Microtubule Nucleation Potential -- IV. The Role of the Centriole -- V. The Procentrosome -- VI. Paternal versus Maternal Centrosomes -- VII. Summary -- References -- Index -- Contents of Previous Volumes.
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  • 2
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Centrosomes. ; Spindle (Cell division). ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (392 pages)
    Edition: 1st ed.
    ISBN: 9780080496627
    Series Statement: Issn Series ; v.Volume 67
    DDC: 571.844
    Language: English
    Note: Cover -- Contents -- Contributors -- Preface -- Chapter 1. Purification and Reconstitution of Drosophila y-Tubulin Complexes -- I. Introduction -- II. Isolation of γ -Tubulin-Containing Complexes from Drosophila Embryo Extracts -- III. γTuSC Reconstitution in Sf9 Cells -- IV. Functional Assays for Isolated γTuSC or γTuRC -- V. Concluding Remarks -- References -- Chapter 2. Using Rapid Freeze and Freeze-Substitution for the Preparation of Yeast Cells for Electron Microscopy and Three-Dimensional Analysis -- I. Introduction -- II. How Rapid Freezing and Freeze-Substitution Work -- III. Rapid Freezing Techniques -- IV. Freeze-Substitution Protocols -- V. Embedding Protocols -- VI. Sectioning and Imaging -- VII. Immunolabeling for Electron Microscopy -- VIII. Three-Dimensional Modeling of Spindle Pole Bodies and Other Organelles -- IX. Conclusion -- References -- Chapter 3. Digital Fluorescence Microscopy of Cell Cytoplasts with and without the Centrosome -- I. Introduction -- II. Experimental Procedures -- References -- Chapter 4. Methods for the Study of Pericentrin in Centrosome Assembly and Function -- I. Introduction -- II. Pericentrin Localization to Centrosomes -- III. Pericentrin Recruitment to Centrosomes -- IV. Obtaining Enriched Fractions of Pericentrin -- V. Artificial Elevation of Pericentrin Levels -- VI. Pericentrin Staining to Detect Centrosome Defects in Tumor Tissues and Cell Lines -- References -- Chapter 5. Molecular Dissection of Yeast Spindle Pole Bodies by Two Hybrid, in Vitro Binding, and Co-purification -- I. Introduction -- II. The Two-Hybrid Approach -- III. Immuno- and Affinity Precipitation of Spindle Pole Body Components -- IV. In Vitro Binding of Spindle Pole Body Proteins -- References -- Chapter 6. Genetic Analysis of Yeast Spindle Pole Bodies -- I. Introduction -- II. Dosage-Dependent Suppressor Screen. , III. Extragenic Suppressor Screen -- IV. Synthetic Lethal Screen -- V. Synthetic Dosage Lethality -- VI. Conclusions -- References -- Chapter 7. Methods for the Study of Centrosomes in Drosophila during Embryogenesis -- I. Introduction -- II. Materials -- III. Methods -- References -- Chapter 8. Methods for Identification of Centrosome-Associated Proteins -- I. Introduction -- II. Preparation of Centrosomes and Anticentrosomal Antibodies -- III. Molecular Cloning of cDNA Encoding Centrosome-Associated Proteins -- IV. Evaluation of Clone Specificity -- V. Identification of a Novel 135-kDa Centrosomal Protein, Cep135 -- References -- Chapter 9. Reconstitution of Centrosome Microtubule Nucleation in Drosophila -- I. Introduction -- II. Preparation of Extracts and Centrosomes from Drosophila Embryos -- III. In Vitro Reconstitution of Microtubule Nucleation by Salt-Inactivated Centrosomes -- IV. Conclusions -- References -- Chapter 10. Reconstitution of Centrosome Microtubule Nucleation in Spisula -- I. Introduction -- II. Preparations -- III. Disassembly and Reassembly of Microtubule Nucleation Potential -- IV. Fractionation of Extracts -- V. Summary -- References -- Chapter 11. In Vitro Approaches for the Study of Microtubule Nucleation at the Fission Yeast Spindle Pole Body -- I. Introduction -- II. Protocol for Permeabilization -- III. Protocol for Microtubule Nucleation -- IV. Results -- References -- Chapter 12. Gamma Tubulin and Microtubule Nucleation in Mammalian Cells -- I. Introduction -- II. Interference with γ -Tubulin Function in Mammalian Cells Abrogates Microtubule Nucleation -- III. Overexpression of γ -Tubulin in Mammalian Cells Causes Ectopic Microtubule Nucleation -- IV. Conclusion -- References -- Chapter 13. Gamma Tubulin in Plant Cells -- I. Introduction -- II. Microtubule Arrays in Plant Cells. , III. Methods for Cloning Plant γ -Tubulin cDNAs and Genes -- IV. Methods for Localizing γ -Tubulin in Plant Cells -- V. Functional Studies of γ -Tubulin in Plants -- VI. Future Prospects -- References -- Chapter 14. Centrosomes and Parthenogenesis -- I. Introduction -- II. Parthenogenetic Test in Xenopus -- III. Coupling between Egg Cell Cycle and Centrosome Duplication Pathway -- IV. Species Barrier Specificity -- V. Active or Inactive Centrosomes from the Same Species -- VI. Prospects -- References -- Chapter 15. In Vitro Approaches for the Study of Molecular Motors in Aster Formation -- I. Introduction -- II. Microtubule Aster Formation -- III. Examination of Microtubule Motor Function in Aster Assembly -- IV. Concluding Remarks -- References -- Chapter 16. Methods for the Study of Centrosome-Independent Spindle Assembly in Xenopus Extracts -- I. Introduction -- II. Preparation of Xenopus Egg Extract and Necessary Reagents -- III. Microtubule Polymerization Assays in Extract -- IV. Spindle Assembly Assays -- V. Studying Proteins Involved in Spindle Assembly -- VI. Methods to Observe Spindle Assembly -- VII. Conclusions -- References -- Chapter 17. Methods for the Study of Centrosome Reproduction in Mammalian Cells -- I. Introduction -- II. Induction of Centrosome Overproduction in Cultured Mammalian Cells -- III. Preparation of Extracts from Hydroxyurea-Arrested Chinese Hamster Ovary Cells -- IV. Analysis of Centrosome Protein Function Using Mammalian Cell Extracts and Salt-Stripped Centrosome Remnants -- V. Conclusions and Prospects -- References -- Chapter 18. Centrosome Reproduction in Xenopus Lysates -- I. Introduction -- II. Reagents and Equipment -- III. Methods -- References -- Chapter 19. Centrosome Reproduction in Vitro: Mammalian Centrosomes in Xenopus Lysates -- I. Introduction -- II. Logic of the Assay -- III. Duplication Assay. , IV. Major Pitfalls -- V. Discussion -- VI. Prospects -- References -- Chapter 20. Identification of Centrosome Kinases -- I. Introduction -- II. Subcellular Localization of Previously Characterized Protein Kinases -- III. Isolation of Novel Centrosome Kinases -- IV. Functional Analysis of Centrosome Kinases -- V. Identifying Substrates for Centrosome Kinases -- VI. Perspectives -- References -- Chapter 21. Methods for the Analysis of Centrosome Reproduction in Cancer Cells -- I. Introduction -- II. Tissue Procurement and Storage -- III. Preparation and Storage of Xenopus Egg Extract -- IV. Reaction Mixture Composition and Use -- V. Experimental Design and Data Analysis -- VI. Summary -- VII. Appendices -- References -- Chapter 22. Isolation of Centrosomes from Dictyostelium -- I. Introduction -- II. Isolation of Dictyostelium Centrosomes -- III. Analysis of Isolated Dictyostelium Centrosomes -- IV. Generation of Monoclonal Antibodies against Dictyostelium Centrosomes -- V. Conclusions -- References -- Index -- Volumes in Series.
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  • 3
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 13 (1989), S. 9-20 
    ISSN: 0886-1544
    Keywords: carotenoid droplet ; intermediate filament ; microfilament ; microtubule ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The cytoskeleton of goldfish xanthophores contains an abundance of unique dense structures (400 nm in diameter) that are absent in goldfish nonpigment cells and are probably remnants of pterinosomes. No major difference in protein composition between xanthophores and nonpigment cells (without these structures) was found that could account for these structures. In xanthophores, these structures are foci of radiating filaments. The addition or withdrawal of ACTH causes a radical rearrangement of the xanthophore Cytoskeleton accompanying redistribution of carotenoid droplets, namely, the virtual exclusion of these dense bodies with associated filaments from the space occupied by the carotenoid droplet aggregate vs. a relatively even cytoplasmic distribution of these structures when the carotenoid droplets are dispersed. These changes in cytoskeletal morphology are not accompanied by any major changes in the protein or phosphoprotein composition of the cytoskeleton.
    Additional Material: 8 Ill.
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  • 5
    ISSN: 0886-1544
    Keywords: pigment organelle ; xanthophore ; microtubule ; F-actin ; intermediate filament ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In goldfish xanthophores, the formation of pigment aggregate requires: (1) that a pigment organelle (carotenoid droplet) protein p57 be in the unphosphorylated state; (2) that self-association of pigment organelles occur in a microtubule-independent manner; and (3) that pigment organelles via p57 associate with microtubules. In the fully aggregated state, the pigment organelles are completely stationary. Pigment dispersion is initiated by activation of a cAMP-dependent protein kinase, which phosphorylates p57 and allows pigment dispersion via an active process dependent on F-actin and a cytosolic factor. This factor is not an ATPase, and its function is unknown. However, its abundance in different tissues parallels secretory activity of the tissues, suggesting a similarity between secretion and pigment dispersion in xanthophores. The identity of the motor for pigment dispersion is unclear. Experimental results show that pigment organelles isolated from cells with dispersed pigment have associated actin and ATPase activity comparable to myosin ATPase. This ATPase is probably an organelle protein of relative molecular mass ∼72,000, and unlikely to be an ion pump. Isolated pigment organelles without associated actin have 5× lower ATPase activity. Whether this organelle ATPase is the motor for pigment dispersion is under investigation. The process of pigment aggregation is poorly understood, with conflicting results for and against the involvement of intermediate filaments.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0886-1544
    Keywords: kinases ; microtubules ; organelle protein ; pigment aggregate ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Triton-insoluble cytoskeleton of nonpigment cells has bound protein kinase that phosphorylates, with or without added cAMP, tubulins and the intermediate filament proteins p60, p56, p53, and p45a to give multiple charge variants. In the absence of 8-Br-cAMP, Triton-insoluble cytoskeletons from xanthophores also phosphorylate p60, p56, and p45a, but not p53; tubulin phosphorylation may also be reduced. In the presence of 8-Br-cAMP, p53, as well as several other peptides, are phosphorylated. One of these latter peptides was identified as the carotenoid droplet (pigment organelle) protein p57, whose phosphorylation and dephosphorylation precede pigment dispersion and aggregation respectively (Lynch et al.: J. Biol. Chem. 261:4204-4211, 1986). The amount of pp57 produced depends on the state of pigment distribution in the xanthophores used to prepare the cytoskeletons for labeling. With cytoskeletons from xanthophores with aggregated pigment, pp57 is a major labeled phosphoprotein seen in two-dimensional gels. With cytoskeletons prepared from xanthophores with dispersed pigment, the yield of labeled pp57 is greatly reduced (by at least 90%). Together with earlier results, we propose that, in the aggregated state, p57 serves to bind carotenoid droplets to the cytoskeletons, most likely the microtubules. The significance of other cAMP-dependent phosphorylation reactions is unknown but may be related to cAMP-induced cytoskeleton rearrangement in intact xanthophores.
    Additional Material: 5 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 18 (1991), S. 304-318 
    ISSN: 0886-1544
    Keywords: mitosis ; spindle ; chromosome ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Mitotic spindles isolated from sea urchin eggs can be reactivated to undergo mitotic processes in vitro. Spindles incubated in reactivation media containing sea urchin tubulin and nucleotides undergo pole-pole elongation similar to that observed in living cells during anaphase-B. The in vitro behavior of spindles isolated during metaphase and anaphase are compared. Both metaphase and anaphase spindles undergo pole-pole elongation with similar rates, but only in the presence of added tubulin. In contrast, metaphase but not anaphase spindles increase chromosome-pole distance in the presence of exogenous tubulin, suggesting that in vitro, tubulin can be incorporated at the kinetochores of metaphase but not anaphase chromosomes. The rate of spindle elongation, ultimate length achieved, and the increase in chromosome-pole distance for isolated metaphase spindles is related to the concentration of available tubulin. Pole-pole elongation and chromosome-pole elongation does not require added adenosine triphosphate (ATP). Guanosine triphosphate (GTP) will support all activities observed. Thus, the force generation mechanism for anaphase-B in isolated sea urchin spindles is independent of added ATP, but dependent on the availability of tubulin. These results support the hypothesis that the mechanism of force generation for anaphase-B is linked to the incorporation of tubulin into the mitotic apparatus. (If, in addition, a microtubule-dependent motor-protein(s) is acting to generate force, it does not appear to be dependant on ATP as the exclusive energy source).
    Additional Material: 8 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 197-209 
    ISSN: 0886-1544
    Keywords: GTP ; ATP ; tubulin ; spindle reactivation media ; birefringence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Spindles may be isolated from sea urchin eggs so that some mitotic processes can be reactivated in vitro. The isolation media allow spindles to remain stable for days. Transfer of the spindles to reactivation media results in loss of birefringence and breakdown of the matrix within which the microtubules function. If, however, tubulin and either guanosine triphosphate or adenosine triphosphate are present in these media so that tubulin can cycle, the spindles do not break down but grow in size and birefringence and show some of the movements of in vivo spindles. The most prominent is that of anaphase B if the mitotic apparatuses (MAs) have been isolated at a time when anaphase was initiated. When isolated during metaphase, MAs either do not show chromosome movement or, if they do, it is a random movement which causes redistribution of the chromosomes on the spindle surface. In either case, such metaphase spindles grow in size and birefringence. Thus under the proper conditions, cycling microtubules can interact with the spindle matrix to induce chromosome movements which resemble those seen in in vivo cells in the case of anaphase B and show some aspects of anaphase A in at least half the spindles isolated at metaphase, although such movements are not coordinated to show a true anaphase movement.
    Additional Material: 7 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 25 (1993), S. 336-344 
    ISSN: 0886-1544
    Keywords: MTOC ; dendrites ; neurite extension ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Centrosomes are unique cytoplasmic structures which serve as microtubule organizing centers (MTOC). In most animal cells centrosomes consist of one or more pair of centrioles surrounded by electron dense amorphous pericentriolar material (PCM) responsible for nucleation of microtubules. In the present study we analyzed the pattern of induction and localization of proteins of the PCM at different stages of neuronal development in cell cultures prepared from the embryonic hippocampus. For this purpose we used a human polyclonal antibody that recognizes two proteins of the PCM (100 kd and 60 kd, respectively). The results indicate that in mature neurons, pericentriolar immunoreactive material is preferentially localized in dendritic processes, and that throughout the course of neurite development and differentiation it is systematically excluded from the neuron's axon. Western blot analysis showed that during neuronal development in situ, there is an increase in he immunoreactivity for both proteins recognized by this antibody. In contrast, in hippocampal pyramidal neurons that develop in culture, there is an increase in the 60 kd polypeptide, while the 100 kd one is not detected after 7 days in vitro. © 1993 Wiley-Liss, Inc.
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