4 edition of Immunocytochemical localization of actin and myosin within interphase nuclei in situ found in the catalog.
Immunocytochemical localization of actin and myosin within interphase nuclei in situ
Thesis (M.Sc.)--University of Toronto, 1993.
|Series||Canadian theses = Thèses canadiennes|
|The Physical Object|
|Pagination||2 microfiches : negative.|
The aim of this study was to show the influence of Trisenox (arsenic trioxide, ATO) on cytoplasmic and nuclear F-actin organization in HL human leukemia cell line. Changes in localization were determined with the use of fluorescence microscopy and flow cytometry. Alterations, in both cytoplasmic and nuclear actin, were observed in cells exposed to by: 4. 2. Actin cytoskeleton, myosin and the cell cycle Actin cytoskeleton in cell cycle control Actin is a highly conserved globular protein found in almost all eukaryotic cells. It forms cellular scaffold structures that pro-vide cells with their shape, tension support, intracellular vesicular.
Myosins are often referred to as molecular motors because they use energy to move. They interact with another protein called actin; actin proteins are organized into filaments to form a network (the cytoskeleton) that gives structure to cells and can act as a track for myosin to move along. Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview. by John Squire. Int. J. Mol Comparatively less is known about actin-myosin interactions within the filament lattice of muscle, where myosin by X-ray crystallography needed to explain the structure of the different actomyosin interactions observed in situ.
Kinesin and dynein work on microtubules while myosin works on actin. Conventional myosin (myosin II) consists of 2 heavy chains and 4 light chains. Each heavy chain has a globular head, then there's a neck region followed by a long tail. The tails coil around each other. The tails interacting allows for a bipolar myosin filament. The globular head part binds actin and hydrolyzes ATP. Myosin VI expression regulates instead the organization of actin networks in the cytoplasm. Using a cell‐free assay, we showed that myosin VI recruited actin at the surface of isolated melanosomes. Myosin VI is involved in the endocytic‐recycling pathway, and this pathway contributes to the transport of a melanogenic enzyme to maturing Cited by:
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J Cell Sci18 Milankov K, De Boni U () Cytochemical localization of actin and myosin aggregates in interphase nuclei in situ. Exp Cell Res19 Motlik J, Kopecny V, Travnik P, Pivko J () RNA syn- thesis in pig follicular by: In the present work, immunocytochemistry, in conjunction with confocal microscopy and ultrastructural immunogold techniques, shows that interphase nuclei of intact dorsal root ganglion neurons and of PC12 cells contain actin and myosin.
Nuclear actin was observed to be distributed throughout the nucleoplasm occurring as distinct aggregates. Frequently, prominent actin aggregates were Cited by: To determine whether dendritic spines contain actin, we evaluated the immunocytochemical localization of actin in the hippocampal formation and cerebral cortex of the rat.
Monoclonal hybridoma antibodies were prepared against adult quail breast muscle actin. The culture supernatant of two cell lines (QAB1 and QAB2) was examined.
Both antibodies bound only actin in Cited by: The interphase nuclei gave off prominent fluorescence, indicating the presence of actin in the interphase nuclei (arrow in Fig 1).Cited by: 2.
Nematodes synthesize two major classes of myosin heavy chains. These heavy chains associate to form only homodimeric myosin molecules, and these myosin homodimers are anti-genically different from one another (Schachat, Garcea and Epstein, ).
The two myosins may be designated unc myosin, since this species is altered in mutants of the unc locus, and non-unc myosin, since Cited by: The evidence presented herein indicates that actin and myosin are constituent proteins of interphase nuclei in situ of both normal mammalian and transformed mammalian cells.
Actin up in the nucleus. Cytochemical localization of actin and myosin aggregates in interphase nuclei in situ. Exp. Cell Res. – Cited by: Nuclear actin and transcription. Actin filaments, which are central to biological functions, such as muscle contraction, cell motility, cell division and vesicle transport, are rarely seen in the normal interphase nucleus, and phalloidin, which is commonly used to detect cytoplasmic actin filaments (Cooper, ), rarely stains the r, this does not exclude the presence of nuclear Cited by: Earlier, studying actin localization in interphase nuclei of two-cell mouse embryos, we have found out that after embryos treatment by antibody to the C-terminal domain, nuclear labeling was much brighter than cytoplasm fluorescence, and this signaled about predominant nuclear localization of antibody-detected by: 2.
Although originally characterized as a cytoplasmic protein, myosin of various classes also performs key functions in the nucleus. We review the data concerning the nuclear localization, mechanism of.
Differing requirements for actin and myosin by plant viruses for sustained intercellular movement Phillip A. Harriesa, Jong-Won Parkb, Nobumitsu Sasakic, Kimberly D.
Ballarda, Andrew J. Mauled, and Richard S. Nelsona,1 aPlant Biology Division, The Samuel Roberts Noble Foundation, Inc. Sam Noble Parkway, Ardmore, OK ; bTexas AgriLife Research, The Texas A&MCited by: Background: The assembly of an F-actin- and myosin-II-containing contractile ring (CR) is required for cytokinesis in eukaryotic cells.
Interactions between myosin II and actin in the ring are believed to generate the force that constricts the cell into two daughters. The mechanism(s) that contribute to the spatially and temporally regulated assembly and disassembly of the CR at the cell Cited by: The evidence presented herein indicates that actin and myosin are constituent proteins of interphase nuclei in situ of both normal mammalian and transformed mammalian cells.
View Show abstractAuthor: Xiaojuan Zhu. This book will appeal to research scientists seeking contemporary overviews of actin-myosin interaction and actin-based regulation. Contributors include senior scientists as well as the new breed of younger scientists. Product details. Series: Results and Problems in Cell Differentiation (Book 36) Hardcover: Format: Hardcover.
A structure of actin and myosin II that forms beneath the plasma membrane during mitosis and mediates cytokinesis. corticosteroids. Steroid hormones produced by the adrenal gland. cosmid. A vector that contains bacteriophage 훌 sequences, antibiotic resistance sequences, and an origin of replication.
It can accommodate large DNA inserts of up to 45 kb. Suprastimulation of pancreatic acinar cells with specific agonists inhibits zymogen secretion and induces the formation of large basolateral blebs.
Currently the molecular mechanisms that mediate this dramatic morphologic response are undefined. Further, it is unclear if blebbing represents a terminal or reversible event. Using computer-enhanced video microscopy of living acini we have found Cited by: More is known about the localization of cytoplasmic actin in cells than about that of myosin.
This is because there is a convenient label for actin. A fragment of myosin called heavy meromyosin (HMM) retains both the adenosine tri-phosphatase (an enzymethat catalyzes the hydrolysis of ATP)activity and the actin-binding capacity found in the Cited by: In addition, recent ultrastructural work has shown the presence of actin and myosin within nuclei of interphase cells in situ.
It was unclear, however, whether this intranuclear actin is present in the unpolymerized globular actin or the filamentous (F)-actin by: (). Cytochemical localization of actin and myosin aggregates in interphase nuclei in situ. Cytogenetic analysis by chromosome painting using DOP-PCR amplified flow-sorted chromosomes.
Cytoplasmic intermediate filaments are stably associated with nuclear matrices and potentially modulate their DNA-binding function. ().Author: Ishita Shailesh Mehta. Keywords actin, autophagy, lysosome, myosin Received 24 Marchrevised and accepted for publication 2 Mayuncorrected manuscript published online 5 Maypublished online 31 May Autophagy Macroautophagy, hereafter referred to as autophagy, is a tightly regulated pathway that sequesters cytoplas-Cited by:.
INTRODUCTION. Actin and myosin were first discovered as actomyosin by Kuhne inbut it was not until – that actin itself was isolated by Straub, Bonga and Szent-Gyorgyi, and myosin was discovered to be an ATPase by Engelhardt and Lyobimova (Szent-Gyorgyi, ).By the s, the presence of actin and myosin in nonmuscle cells had been firmly established (Hatano and Oosawa.
(). The two mutations of actin–myosin interface and their effect on the dynamics, structures, and functions of skeletal muscle actin. Journal of Biomolecular Structure and Dynamics: Vol. 37, No.
2, pp. Cited by: 1. Since ADP-bound myosin binds actin more tightly than ATP-bound myosin, this low affinity for ADP comes at the price of a very brief tight binding between myosin and actin. As a result, the duty ratio of the motor is only and dimers of myosin XI in Cited by: