Relationship to the Directionality of Flagellar Microtubule Assembly

Total Page:16

File Type:pdf, Size:1020Kb

Relationship to the Directionality of Flagellar Microtubule Assembly Published September 1, 1977 FLAGELLAR ELONGATION AND SHORTENING IN CHLA MYD OMONAS III. Structures Attached to the Tips of Flagellar Microtubules and Their Relationship to the Directionality of Flagellar Microtubule Assembly WILLIAM L. DENTLER and JOEL L. ROSENBAUM From the Department of Biology, Yale University, New Haven, Connecticut 06520. Dr. Dentler's Downloaded from current address is the Department of Physiology and Cell Biology, MeCollum Laboratories, The University of Kansas, Lawrence, Kansas 66044. ABSTRACT Two structures on the distal ends of Chlamydomonas flagellar microtubules are described. One of these, the central microtubule cap, attaches the distal ends of jcb.rupress.org the central pair microtubules to the tip of the flagellar membrane. In addition, filaments, called distal filaments, are observed attached to the ends of the A- tubules of the outer doublet microtubules. Inasmuch as earlier studies suggested that flagellar elongation in vivo occurs principally by the distal addition of subunits and because it has been shown that brain tubulin assembles in vitro primarily onto on September 10, 2014 the distal ends of both central and outer doublet microtubules, the presence of the cap and distal filaments was quantitated during flagellar resorption and elonga- tion. The results showed that the cap remains attached to the central microtubules throughout flagellar resorption and elongation. The cap was also found to block the in vitro assembly of neurotubules onto the distal ends of the central microtu- bules. Conversely, the distal filaments apparently do not block the assembly of neurotubules onto the ends of the outer doublets. During flagellar elongation, the distal ends of the outer doublets are often found to form sheets of protofilaments, similar to those observed on the elongating ends of neurotubules being assembled in vitro. These results suggest that the outer doublet microtubules elongate by the distal addition of subunits, whereas the two central microtubules assemble by the addition of subunits to the proximal ends. KEY WORDS flagella microtubules by amputating the flagella of certain protozoans microtubule assembly 9Chlamydomonas and algae, allowing them to regenerate their fla- membranes gella to half-length, and then adding a radioactive precursor, such as tritiated leucine, to the cells It has been shown by pulse labeling and light and until flagellar regeneration was completed. After electron microscope autoradiography that flagella autoradiography, most of the incorporated radio- (21, 22) and flagellar microtubules (34) assemble active precursor was observed to be in the distal in vivo principally by the addition of subunits to (tip) half of the flagellum (21, 22) or flagellar their distal ends. These observations were made microtubules (34), indicating that elongation oc- THE JOURNAL OF CELL BIOLOGY 9 VOLUME 74, 1977 9pages 747-759 747 Published September 1, 1977 curred by distal addition of subunits; however, gella terminate in a pair of filaments, called distal there was always some labeled precursor (ca. 20- filaments, which apparently do not prevent the 35%) incorporated into the proximal half of the distal assembly of brain tubulin onto the A-tubules flagellum or flagellar microtubules (21, 22, 34) of the outer doublets. Observations of the distal even after prolonged chases with the unlabeled ends of the outer doublet microtubules during precursor. It was not known whether this proximal flagellar regeneration show them frequently to ter- label represented microtubule assembly by the minate in sheets of protofilaments, similar to those proximal addition of subunits, or whether the la- observed on the ends of brain microtubules being bel was present in some microtubule-associated assembled in vitro (7, 10, 15, 16, 27). These structures added after microtubule assembly (see results suggest that the flagellar outer doublet mi- reference 34). crotubules elongate by the distal addition of sub- With the development of methods for the in units, whereas the central microtubules elongate vitro assembly of brain tubulin (3, 33), it was by the proximal addition of subunits. found that brain tubulin would assemble onto flag- A preliminary report of some of the data pre- ellar microtubules in vitro (1, 2) and that the sented in this paper has been published (8). assembly occurred principally onto the distal ends of the flagellar outer doublet and central microtu- MATERIALS AND METHODS Downloaded from bules (1,2). However, if the tubulin concentration Cell Culture was sufficiently high, neurotubules also assembled onto the proximal, nonfavored ends of the flagel- Chlamydomonas reinhardtii (strain 21 gr) were grown in 125-ml flasks to a cell density of 0.8-1.0 x 10~ cells/ lar microtubules but at a rate five to eight times ml in medium I of Sager and Granick (25). The cells slower than the assembly onto the distal ends (2). were grown with constant aeration at 25~ on a cycle of The relevance of this in vitro proximal assembly to 13 h of light and 11 h of dark. Cells were harvested by flagellar assembly during regeneration in vivo was centrifugation in 50-ml conical centrifuge tubes (IEC jcb.rupress.org unknown, as no information was available on the Model HN centrifuge, rotor number 958, 350 g, 3-5 concentration of tubulin in the cells being used. rain, room temperature) and were resuspended in fresh However, the possibility of proximal assembly oc- culture medium. The cells were aerated during the ex- curring in vivo was considered to be small be- periment either by bubbling air through the medium or cause, in addition to the fact that the distal ends of by stirring the culture with a magnetic stirring bar. both the central and outer doublet microtubules Preparation of Axonemes for on September 10, 2014 were favored for the in vitro assembly of brain tubulin, the outer doublet microtubules do not Electron Microscopy have free proximal ends but are extensions of the To attach flagella to the electron microscope grids, the basal body microtubules. On the other hand, the grids were treated with poly-L-lysine by a modification of proximal ends of the two central microtubules are the method of Mazia et al. (18). Electron microscope free, ending in or just above the basal cup (axos- grids were coated with a Formvar film, shadowed with tome) of the basal body (9, 20). Therefore, the carbon, and glow-discharged for 1-2 min in a vacuum evaporator. The glow-discharged films were then over- possibility could not be excluded that the central laid with a solution of 0.1% poly-L-lysine in water for 5- microtubules assembled in vivo from their proxi- 10 min, washed under a stream of double-distilled water, mal ends at high local tubulin concentrations even and air dried. A drop containing Chlamydomonas cells though their distal ends were favored for the in was then applied to the grid and the grid was drained by vitro assembly of brain tubulin. touching it to filter paper. The grid was then inverted In this study, it is shown that the distal ends of over a ~irop of deflagellation solution (5 mM MgSO4, the two central microtubules insert into a cap, 0.35 mM DTT, 0.5 mM EDTA, 10 mM HEPES, pH called the central microtubule cap, which is at- 7.5, 0.005-0.05% Nonidet P-40 [Shell Chemical Co., tached to the distal tip of the flagellar membrane. N. Y.]) for 5-20 s at room temperature. The concentra- It is also shown that the cap remains attached to tion of detergent and the time of extraction varied with the concentration of cells and various Chlamydomonas the central microtubules during flagellar regenera- mutants; extraction conditions were adjusted so the min- tion and resorption and that the cap prevents the imum treatment, which resulted in the removal of cell addition of brain tubulin subunits onto the distal bodies from the flagella (and from the grid) and the ends of the central microtubules. In addition, the dissolution of most of the flagellar membranes without results in this report show that the A-tubules of disruption of the structures at the flagellar tips, was used. the outer doublet microtubules of full-grown fla- After detergent treatment, the grid was rinsed with 2-5 748 THE JOURNAL OF CELL BIOLOGY 9VOLUME 74, 1977 Published September 1, 1977 drops of 2% aqueous uranyl acetate and air dried. A to remove the flagellar membrane varied with the procedure similar to this has recently been used by Sale number of cells attached to the grid and the partic- and Satir (26) to visualize the organization of radial ular strain of Chlamydomonas used. After deter- spokes in cilia. Tetrahymena gent treatment, most of the flagellar axonemes Flagellar Resorption and Regeneration remained intact except for the distal tips, which were slightly splayed (Fig. 1 B, C). The structure Chlamydomonas were induced to resorb their flagella of the microtubules is similar to that reported by by the high-salt method developed by Lefebvre et al. 1 in others (1, 2, 13, 31): dynein arms were attached which the flagella could be synchronously shortened along the A-tubule of each outer doublet and the from an average length of 12-14 to 2-3 tzm in 3 h. Flagellar regeneration subsequently was induced by har- projections attached to the central microtubules vesting the cells and resuspending them in fresh medium. were often superimposed to form an apparent Samples of cells were taken at intervals during flagellar helical coil (see references 5 and 31). Examination resorption and regeneration and were treated as de- of the tips of the axonemes at higher magnification scribed above to observe the flagellar microtubules. In (Figs. 1 C, 2, 3) revealed structures at the ends of addition, samples of cells were fixed in 2% glutaraide- the microtubules that had not been observed be- hyde in polymerization mixture (PM) and their flagellar fore in negatively stained axonemes.
Recommended publications
  • Brain-Specific Expression of MAP2 Detected Using a Cloned Cdna Probe Sally A
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by PubMed Central Brain-specific Expression of MAP2 Detected Using a Cloned cDNA Probe Sally A. Lewis,* Alfredo Villasante,* Peter Sherline,* and Nicholas J. Cowan* *Department of Biochemistry, New York University Medical Center, New York, New York 10016; *Division of Endocrinology, Cornell University Medical College, New York, New York 10021 Abstract. We describe the isolation of a set of over- consistent with the coding capacity required by a lapping cDNAs encoding mouse microtubule associ- 250,000-D protein. ated protein 2 (MAP2), using an anti-MAP antiserum The MAP2-specific cloned cDNA probes were used to screen a mouse brain cDNA expression library in RNA blot transfer experiments to assay for the cloned in bacteriophage hgt 11. The authenticity of presence of MAP2 mRNA in a variety of mouse tis- these clones was established by the following criteria: sues. Though brain contained abundant quantities of (a) three non-identical clones each expressing a MAP2 mRNA, no corresponding sequences were de- MAP2 immunoreactive fusion protein were independ- tectable in RNA prepared from liver, kidney, spleen, ently isolated from the expression library; each of stomach, or thymus. We conclude that the expression these clones cross-hybridized at the nucleic acid level; of MAP2 is brain-specific. (b) anti-MAP antiserum was affinity purified using Use of the MAP2 specific cDNA probes in genomic nitrocellulose-bound fusion protein; these antibodies Southern blot transfer experiments showed the pres- detected only MAP2 in an immunoblot experiment of ence of a single gene encoding MAP2 in mouse.
    [Show full text]
  • Immunolocalization and Molecular Properties of a High Molecular Weight Microtubule-Bundling Protein (Syncolin) from Chicken Erythrocytes E Feick, R
    Immunolocalization and Molecular Properties of a High Molecular Weight Microtubule-bundling Protein (Syncolin) from Chicken Erythrocytes E Feick, R. Foisner, and G. Wiche Institute of Biochemistry, University of Vienna, 1090 Vienna, Austria Abstract. A protein of apparent molecular weight was displaced from the polymer by salt. Brain as well 280,000 (syncolin), which is immunoreactive with an- as erythrocyte microtubules, reconstituted with taxol tibodies to hog brain microtubule-associated protein from MAP-free tubulin and purified syncolin, were ag- (MAP) 2, was purified from chicken erythrocytes. Im- gregated into dense bundles containing up to 15 Downloaded from http://rupress.org/jcb/article-pdf/112/4/689/1060909/689.pdf by guest on 29 September 2021 munofluorescence microscopy of bone marrow cells microtubules, as determinedby'etectron microscopy. revealed the presence of syncolin in cells at all stages On the ultrastructural level, syncolin molecules were of erythrocyte differentiation. In early erythroblasts visualized as globular or ringlike structures, in con- syncolin was diffusely distributed throughout the trast to the thin, threadlike appearance of filamentous cytoplasm. At later stages it was found along microtu- MAPs, such as brain MAP 2. According to ultrastruc- bules of the marginal band, as confirmed by immuno- tural measurements and gel permeation chromatogra- electron microscopy. The association of syncolin with phy, syncolin's molecular weight was ,',,1 x 106. It is the marginal band was dependent on the integrity of suggested that syncolin's specific function is the cross- microtubules, as demonstrated by temperature- linking of microtubules in the marginal band and, by dependent de- and repolymerization or marginal band implication, the stabilization of this structure typical microtubules.
    [Show full text]
  • And High-Molecular-Weight Forms of MAP2 in the Developing Cerebellum
    The Journal of Neuroscience, December 1999, 8(12): 4503-4512 The Sequential Appearance of Low- and High-Molecular-Weight Forms of MAP2 in the Developing Cerebellum R. P. Tucker,’ L. I. Binder,’ C. Viereck,’ B. A. Hemmings,’ and A. I. Matus’ ‘Friedrich Miescher Institute, CH-4002 Basel, Switzerland, and *Department of Cell Biology and Anatomy, School of Medicine and Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294 Mammalian microtubule-associated protein 2 (MAPS) exists shown that a number of MAPS promote the assemblyof tubulin in high-molecular-weight (M, -280,000) and low-molecular- into microtubulesand stabilize the resulting microtubulesagainst weight (M, -70,000) forms, with the latter protein being more the depolymerizing effects of cold and various pharmacological abundant in embryonic brain homogenates than in prepa- agents(Olmsted, 1986; Matus, 1988). The most abundant MAP rations from mature brain (Riederer and Matus, 1985). In the in the mammalian CNS, MAP2, displays each of these char- current study, we have shown that avian MAP2 also exists acteristics: (1) There are 2 closely related high-molecular-weight as both high- (M, -260,000) and low-molecular-weight (M, (HMW) forms of MAP2, MAP2a, and MAP2b, which change -65,000) forms whose relative abundance changes during in relative abundanceduring development (Binder et al., 1984; brain maturation, indicating a conserved function for these Burgoyne and Cummings, 1984);(2) MAP2 is found in dendrites proteins during vertebrate neuronal morphogenesis. Using and only rarely in axons (e.g., Cacereset al., 1984; DeCamilli indirect immunohistochemistry, we have determined the cel- et al., 1984; Huber and Matus, 1984b); and (3) MAP2 stabilizes lular distribution of the high- and low-molecular-weight forms and promotes the assembly of microtubules in vitro (Murphy of MAP2 in the developing avian cerebellum.
    [Show full text]
  • Evidence for Conformational Change-Induced Hydrolysis of Β-Tubulin-GTP
    bioRxiv preprint doi: https://doi.org/10.1101/2020.09.08.288019; this version posted September 10, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Evidence for conformational change-induced hydrolysis of β-tubulin-GTP Mohammadjavad Paydar1 and Benjamin H. Kwok1† 1 Institute for Research in Immunology and Cancer (IRIC), Département de médecine, Université de Montréal, P.O. Box 6128, Station Centre-Ville, Montréal, QC H3C 3J7, Canada. † Corresponding author: B. H. Kwok: [email protected] Keywords: Kinesin, Kif2A, MCAK, motor protein, microtubules, tubulin, GTP hydrolysis Abbreviations NM: Neck+Motor MD: Motor domain MT: Microtubule Running title: Tubulin GTP hydrolysis 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.09.08.288019; this version posted September 10, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. ABSTRACT Microtubules, protein polymers of α/β-tubulin dimers, form the structural framework for many essential cellular processes including cell shape formation, intracellular transport, and segregation of chromosomes during cell division. It is known that tubulin-GTP hydrolysis is closely associated with microtubule polymerization dynamics. However, the precise roles of GTP hydrolysis in tubulin polymerization and microtubule depolymerization, and how it is initiated are still not clearly defined. We report here that tubulin-GTP hydrolysis can be triggered by conformational change induced by the depolymerizing kinesin-13 proteins or by the stabilizing chemical agent paclitaxel. We provide biochemical evidence that conformational change precedes tubulin-GTP hydrolysis, confirming this process is mechanically driven and structurally directional.
    [Show full text]
  • Axonal Transport and the Eye
    Br J Ophthalmol: first published as 10.1136/bjo.60.8.547 on 1 August 1976. Downloaded from Brit. 7. Ophthal. (1976) 60, 547 Editorial: Axonal transport and the eye Since the earliest days of histology, it has been and proteins, and are predominantly found in the known that the neurons have a large amount of particulate fraction of nerve homogenates. The basophilic material in the cell body. More recently slower transported material is mainly soluble this has been shown to be due to masses of rough protein (McEwen and Grafstein, I968; Kidwai and endoplasmic reticulum which are responsible for a Ochs, I969; Sj6strand, 1970). Much of the former high rate of protein synthesis of neurons. Since the and more than 6o per cent of the latter is probably earliest days of the microscopy of living cells in neurotubular protein (tubulin), and the neurotubules vitro, particulate movement within these cells has are thought to play a major part in axonal transport been recognized, particularly in neurons (Nakai, (Schmitt and Samson, I968). The neurotubules I964). The last 30 years have seen the gradual have a similar structure to actin, and are linked to accumulation of the knowledge required to explain high-energy phosphate compounds. Myosin-like these two observations. In the last io years in proteins are also found in axoplasm. It is suggested particular, the development of radioactive tracer that moving material might in part roll along the techniques has revealed much information on the neurotubules, or that the neurotubules themselves movement of protein and other substances within might move by a mechanism involving myosin- axons, a process termed axonal transport (Barondes, guanosine triphosphate-neurotubule cross bonds I967).
    [Show full text]
  • Tubulin Requires Tau for Growth Onto Microtubule Initiating Sites (Flagella/In Vitro Assembly/Electron Microscopy) GEORGE B
    Reprinted from Proc. Natl. Acad. Sci. USA Vol. 73, No. 11, pp. 4070-4074, November 1976 Cell Biology Tubulin requires tau for growth onto microtubule initiating sites (flagella/in vitro assembly/electron microscopy) GEORGE B. WITMAN, DON W. CLEVELAND, MURRAY D. WEINGARTEN, AND MARC W. KIRSCHNER The Departments of Biology and Biochemistry, Princeton University, Princeton, New Jersey 08540 Communicated by J. T. Bonner, August 9, 1976 ABSTRACT Tubulin purified by phosphocellulose chro- ether)-N,N'-tetraacetic acid (EGTA), 1 mM GTP, 0.5 mM matography and free of accessory proteins will not form mi- MgCl2, and 1 mM mercaptoethanol]. A high-speed supernatant crotubules in the absence or presence of micrdtubule initiating sites (flagellar microtubules). The capacity for growth onto of depolymerized microtubules was prepared by cooling the pre-existing "seeds" can be restored by the addition of small protein at 5 mg/ml in the above buffer at 0° for 30 min and quantities of partially purified tau protein. Larger quantities sedimenting the solution at 190,000 X g for 2 hr. Phosphocel- restore the capacity for spontaneous assembly. These results lulose-purified tubulin was prepared as described (4, 8). Mi- suggest that tubulin requires tau for both initiation and growth crotubule protein in purification buffer was repolymerized and of microtubules and that tau is incorporated into the microtu- centrifuged at 100,000 X g for 40 min at 280. The resulting bule throughout its length. pellets were resuspended in Mes-EDTA buffer (25 mM Mes, pH 6.4,0.5 mM MgCl2, 0.1 mM EDTA, and 1 mM mercapto- The development of procedures for the assembly of microtu- ethanol) to a final concentration of 8-10 mg/ml.
    [Show full text]
  • Axon Growth: Roles of Microfilaments and Microtubules* Kenneth M
    Proceedings of the JVational Academy of Sciences Vol. 66, No. 4, pp. 1206-1212, August 1970 Axon Growth: Roles of Microfilaments and Microtubules* Kenneth M. Yamada, Brian S. Spooner, and Norman K. Wessellst DEPARTMENT OF BIOLOGICAL SCIENCES, STANFORD UNIVERSITY, STANFORD, CALIFORNIA Communicated by Colin S. Pittendrigh, April 27, 1970 Abstract. The motile tips of elongating axons consist of growth cones from which microspikes protrude. Cytochalasin B causes retraction of microspikes, rounding-up of growth cones, and cessation of axon elongation. Drug with- drawal is followed by resumption of growth cone and microspike activity and of axon elongation. In contrast, colchicine causes shortening and retraction of axons, but it does not initially affect the tips. Growth cones and microspikes of elongating axons contain a network of 50 A microfilaments, the pattern of which is altered by cytochalasin treatment. These experiments indicate that both structural integrity of the axon and continuing function of its motile tip are essential elements in axonal elongation. The tips of elongating axons consist of expanded regions called "growth cones" from which project long slender microspikes (filopodia). These microspikes continually wave about, extend, and retract as the growth cone moves over a substratum.1 Although it is assumed that growth cones and microspikes play a significant role in axon extension, it has not been previously possible to analyze their functions. We have investigated the effects of cytochalasin B on axon elongation since this drug halts cell movement,2 a process similar in many respects to growth cone movement. Cytochalasin B is also known to inhibit cytokinesis3 and morpho- genetic movements,4 apparently by disrupting contractile 50 A microfilaments.
    [Show full text]
  • Neurons and Associated Cells
    CH02.p3 3/11/05 8:41 AM Page 11 2 Neurons and Associated Cells Neuroplasticity Organelles and Components Neurotrophic Factors and Tropic Factors Structure of Peripheral Nerves and Ganglia Neuroglia (GLIA) Paraneurons Nerve Regeneration Plasticity and Axonal Sprouting resulting excitation rapidly to other portions of NEUROPLASTICITY the nerve cell, and to influence other neurons, muscle cells, and glandular cells. Neurons are Some 100–200 billion ([1–2] × 1011) neu- so specialized that most are incapable of repro- rons (nerve cells), as well as many more glial ducing themselves and they lose viability if cells, are integrated into the structural and denied an oxygen supply for more than a few functional fabric that is the brain. They exhibit minutes. a wide diversity of form and sizes. The neuron is the basic unit of the nervous system and is composed of four structurally defined regions: a cell body (soma) that emits a single nerve ORGANELLES AND COMPONENTS process called an axon, which ends at presy- naptic terminals, and a variable number of Each neuron consists of a large nucleus, a branching processes called dendrites (Figs. 2.1 plasma (cell) membrane and cytoplasm con- and 2.2). Each axon, including its collateral sisting of cytosol (fluid phase of cytoplasm), branches, usually terminates as an arbor of fine and a number of organelles, including the fibers; each fiber ends as an enlargement called endoplasmic reticulum, Nissl substance, Golgi a bouton,which is part of a synaptic junction. apparatus, mitochondria, lysosomes and cyto- At the other end of the neuron, there is a three- skeleton (Figs.
    [Show full text]
  • Cyclic AMP-Dependent Endogenous Phosphorylation of a Microtubule-Associated Protein (Protein Phosphorylation/In Vitro Assembly) ROGER D
    Proc. Nat. Acad. Sci. USA Vol. 72, No. 1, pp. 177-181, January 1975 Cyclic AMP-Dependent Endogenous Phosphorylation of a Microtubule-Associated Protein (protein phosphorylation/in vitro assembly) ROGER D. SLOBODA, STEPHEN A. RUDOLPH, JOEL L. ROSENBAUM, AND PAUL GREENGARD Department of Biology, Kline Biology Tower, Yale University and Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06610 Communicated by Aaron B. Lerner, October 21, 1974 ABSTRACT Microtubules prepared from chick brain were homogenized in a motor-driven glass-Teflon homogenizer homogenates by successive cycles of assembly-disassembly at 00 in 1 ml of polymerization mixture buffer [1 mM MgSO4, were found to contain two high-molecular-weight pro- ether)-N,N'-tetra- teins, designated microtubule-associated protein, and 2 mM ethyleneglycol bis(#-aminoethyl microtubule-associated proteins. Microtubule-associated acetate (EGTA), 1 mM GTP, 100 mM piperazine-N,N'-bis(2- protein2 (apparent molecular weight 300,000 by sodium ethanesulfonic acid) (Pipes) (pH 6.9)] per g wet weight, and dodecyl sulfate-polyacrylamide gel electrophoresis) was the homogenate was centrifuged at 130,000 X g for 1 hr at 40 the preferred substrate for an endogenous cyclic AMP- to yield a crude high-speed supernatant. This supernatant was dependent protein kinase which appeared to be an integral component of the microtubules. The initial rate of phos- diluted with an equal volume of polymerization mixture buffer phorylation of microtubule-associated protein2 was en- containing 8 M glycerol, and incubated at 370 for 30 min to hanced 4- to 6-fold by cyclic AMP, with half-maximal assemble microtubules.
    [Show full text]
  • NERVE TISSUE Neuron – Nerve Cell
    Department of Histology and Embryology, P. J. Šafárik University, Medical Faculty, Košice NERVE TISSUE: Sylabus for foreign students Author: doc. MVDr. Iveta Domoráková, PhD. Revised by: prof. MUDr. Eva Mechírová, CSc. NERVE TISSUE FUNCTION: Reception, transmission, processing of nerve stimuli. Coordination of all functional activities in the body: - motor function (body movement) - sensory (rapid response to external stimuli) - visceral, endocrine and exocrine glands - mental functions, memory, emotion A) Anatomically nervous system consists of: 1. CNS (central nervous system) – brain, spinal cord 2. PNS (peripheral nervous system) – peripheral nerves and ganglia B) Functionally nervous system is divided into the: 1. Somatic nervous system (sensory and motor innervation) 2. Autonomic nervous system (involuntary innervation of smooth muscles, glands) C) Microscopic structure of the nerve tissue - two types of cells: 1. Nerve cells – neurons 2. Glial cells (supporting, electrical insulation, metabolic function) Neuron – nerve cell - is the structural and functional unit of the nerve tissue - receives stimuli from other cells - conducts electrical impulses to another cells by their processes - chainlike communication - ten bilion of neurons in humans A. Neurons according the shape: Pyramidal (E) star-shaped (D) pear-shaped (G) oval (B) B. Types of neurons according number of the processes 1. multipolar (D,E,G)) 2. bipolar (A) 3. pseudounipolar (B) 4. unipolar C. Neurons - according the function Motor (efferent) neurons – convey impulses
    [Show full text]
  • Ultrastructural Study of the Persistence of Colchicine-Induced Cytological Changes in Harding-Passey Melanoma1
    [CANCER RESEARCH 38. 168-176, January 1978] Ultrastructural Study of the Persistence of Colchicine-induced Cytological Changes in Harding-Passey Melanoma1 Kenneth R. Loader and Edward J. H. Nathaniel2 Department ol Anatomy, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba, Canada ABSTRACT and characterizing the differentiated state. Since they are not always concordant, it becomes important to recognize Electron microscopic observations were undertaken on the significance of each, and to specify criteria when one Harding-Passey melanoma in control tumors, colchicine- is characterizing differentiation. Cells may be said to be treated tumors, and tumors that were passed through differentiated by morphological, behavioral, chemical or five transplantations in mice subsequent to colchicine developmental criteria." treatment. Evidence of submicroscopic differentiation is observed The untreated Harding-Passey melanoma tumor was in both the nucleus and the cytoplasm. These changes are composed of pleomorphic cells the cytoplasm of which more conspicuous in the cytoplasm (13). Morphological contained tubulovesicular mitochondria and numerous changes in the nucleus during the course of development free and membrane-attached ribosomes. Type A virus have been described by several investigators (3, 22). How particles were observed in both mitotic and interphase ever, the site of functional realization of the cell, together cells. Colchicine-treated tumors exhibited several typical with the respective structural arrangement, resides within colchicine mitotic cells arrested in metaphase. A most the cytoplasm, the primary area of submicroscopic differ significant feature of the colchicine administration was entiation. During differentiation, changes in cellular organ- the appearance of microfilaments in both interphase and elles take place. mitotic cells, a feature not observed in cells of the un The appearance of microfilaments in the tumor cells of treated tumor.
    [Show full text]
  • Estramustine Phosphate Inhibits Germinal Vesicle Breakdown and Induces Depolymerization of Microtubules in Mouse Oocyte Hélène Rime, Catherine Jessus, R
    Estramustine phosphate inhibits germinal vesicle breakdown and induces depolymerization of microtubules in mouse oocyte Hélène Rime, Catherine Jessus, R. Ozon To cite this version: Hélène Rime, Catherine Jessus, R. Ozon. Estramustine phosphate inhibits germinal vesicle breakdown and induces depolymerization of microtubules in mouse oocyte. Reproduction Nutrition Développe- ment, 1988, 28 (2A), pp.319-334. hal-00898793 HAL Id: hal-00898793 https://hal.archives-ouvertes.fr/hal-00898793 Submitted on 1 Jan 1988 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Estramustine phosphate inhibits germinal vesicle breakdown and induces depolymerization of microtubules in mouse oocyte Hélène RIME Catherine JESSUS R. OZON Laboratoire de Physiologie de la Reproduction, Groupe Stéroides, UA-CNRS 555, Université Pierre et Marie Curie, 4, place Jussieu, 75252 Paris Cedex 05, France. Summary. The first meiotic cell division (meiotic maturation) of the dictyate stage of mouse oocytes, removed from the follicle, resumes spontaneously in vitro. This study indicates that estramustine phosphate reversibly blocks meiotic maturation by inhibiting germinal vesicle breakdown. Oocyte cryostat sections were stained with anti-tubulin and two antibodies (anti-MAP1 : JA2 and 5051) which decorated the metaphase spindle during meiotic maturation.
    [Show full text]