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  • 1
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The precise specification of left–right asymmetry is an essential process for patterning internal organs in vertebrates. In mouse embryonic development, the symmetry-breaking process in left–right determination is initiated by a leftward extraembryonic fluid flow on the surface of the ...
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 376 (1995), S. 274-277 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The MT surface has been decorated with K340 (ref. 9), which contains the 340 N-terminal residues of the mouse kinesin heavy chain10. Until now, studies of the three-dimensional structure of the kinesin head-MT complex have been limited9'11'12 because most MTs have a seam line along the ...
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  • 3
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] In cells, molecular motors operate in polarized sorting of molecules, although the steering mechanisms of motors remain elusive. In neurons, the kinesin motor conducts vesicular transport such as the transport of synaptic vesicle components to axons and of neurotransmitter receptors to ...
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Macmillian Magazines Ltd.
    Nature 411 (2001), S. 439-445 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Kinesin motors are specialized enzymes that use hydrolysis of ATP to generate force and movement along their cellular tracks, the microtubules. Although numerous biochemical and biophysical studies have accumulated much data that link microtubule-assisted ATP hydrolysis to kinesin motion, the ...
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Macmillian Magazines Ltd.
    Nature 424 (2003), S. 574-577 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Conventional isoforms of the motor protein kinesin behave functionally not as ‘single molecules’ but as ‘two molecules’ paired. This dimeric structure poses a barrier to solving its mechanism. To overcome this problem, we used an unconventional kinesin KIF1A (refs ...
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 343 (1990), S. 479-482 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We injected cultured dorsal root ganglion (DRG) cells with fluorescein-labelled tubulin and actin. Low-light level video microscopy enabled us to obtain sequential images of the fluorescence in the axon. To bleach a region of the axon, we applied an intense laser-beam pulse. Although prolonged ...
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 162 (1975), S. 119-130 
    ISSN: 1432-0878
    Keywords: Adrenal Gland ; Mouse ; X zone ; Castration ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The secondary X zone induced by castration in the adrenal cortex of adult male mice was examined by electron microscopy and radioautography with 3H-thymidine. 10–15 days after castration a thin layer of small eosinophilic cells is formed in the inner-most cortex. Such eosinophilic cells contain irregulary shaped nuclei and spherical or ellipsoidal mitochondria with tubulolamellar cristae, 20–25 days after castration a prominent zone of small eosinophilic cells was clearly identified as the secondary X zone. The typical secondary X zone cells were characterized by the formation of peculiar mitochondrial complexes and whorled sER. The X zone cells with their characteristic organelles incorporated 3H-thymidine. The ultrastructure and formation of the secondary X zone were very similar to those of the primary X zone which appears during normal postnatal development. We demonstrate here the capacity of reticularis cells of adult male mice to transform into typical X zone cells following castration.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 649-655 
    ISSN: 0886-1544
    Keywords: axonal transport ; lymphocyte capping ; spectrin ; fodrin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Fodrin is an actin/calmodulin-binding protein with similarities to spectrin (erythrocytes) and TW 260/240 (brush border). It is concentrated beneath the plasma membranes of neurons and other cells. We have observed translocations of fodrin in both neurons and lymphocytes. Newly synthesized, radiolabeled fodrin moves down axons at a maximum velocity (about 50 mm/day) that is slower than the most rapidly axonally transported proteins (group I). A portion of fodrin appears to move more slowly at velocities (1-10 mm/day) resembling those of actin and myosin (group IV) and tubulin and neurofilament proteins (group V). In lymphocytes, when certain surface antigens are induced by cross-linking agents to migrate to one pole of the cell and form a cap, fodrin redistributes beneath the membrane and forms a subcap. The movements of fodrin in lympohocyte capping and in the axonal transport of group IV polypeptides have certain similarities. In both cases, the redistribution of fodrin is accompanied by concomitant redistributions of actin, myosin, and calmodulin, and both processes proceed at similar velocities. We consider the possibilities that these two processes are related, both being driven by a submembrane force-generating system comprising in part actin, myosin, and fodrin, and that fodrin serves to link various organelles or proteins to this system.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 9 (1988), S. 299-311 
    ISSN: 0886-1544
    Keywords: myosin ; fodrin ; TW 260/240 ; terminal web ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: At the terminal web of the chicken intestinal epithelial cell, the actin bundles are cross-linked by a fine filamentous network of actin-associated cross-linkers. Myosin, fodrin, and TW 260/240 have been identified as major components of the cross-linkers. We studied the development of the cross-linkers by quick-freeze, deep-etch electron microscopy, and the expression of cross-linker proteins (myosin, fodrin 240, and TW 260) by immunofluorescence and immunoblotting analysis during the embryogenesis. Microvilli start to form at 5-7 days, and the rootlets begin to elongate at 10 days. At an early stage of the development of the terminal web (13 days), fodrin 240 and a small amount of myosin are expressed, and a few actin-associated cross-linkers are present between the rootlets. However, TW 260 is not expressed at this stage. At an intermediate stage (19 days), the amount of myosin increases, and TW 260 begins to be expressed. The number of cross-linkers associated with the unit length of the rootlets is 24/μm. At the final stage of the terminal web formation (2 days after hatching), the amount of fodrin 240, myosin, and TW 260 is similar to the adult level, and the number of the actin-associated cross-linkers per unit length of the rootlet is 27/μm (∼85% of the adult). These results suggest that the synthesis of cross-linker proteins may be intricately regulated to achieve the desired density of cross-linkages at each developmental stage: at early and intermediate stages, sufficient and not an excess of cross-linkages are formed; and at a final stage, a higher complexity of cross-linkages is achieved. In addition, there is a differential expression of the components of the actin-associated cross-linkers: myosin and fodrin could be early components of the cross-linkers involved in the basic stabilization of the terminal web structure, whereas TW 260/240 becomes incorporated later, possibly involved in the stabilization preparatory to the rapid elongation of microvilli, which occurs after the formation of the terminal web.
    Additional Material: 12 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 264-272 
    ISSN: 0886-1544
    Keywords: rotary shadowing ; microtubules ; cytoplasmic movement ; conformation change ; two-headed molecule ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The molecular structure of bovine adrenal kinesin was studied by electron microscopy using the low-angle rotary shadowing technique. Adrenal kinesin exhibited either a folded or an extended configuration; the ratio of the two is dependent on the salt concentration. Almost all adrenal kinesin molecules were folded in a low-ionic solution, and the ratio of extended molecules increased to 40-50% in a solution containing 1 M ammonium acetate. Kinesin in the extended configuration displayed a rod-shaped structure with a mean length of about 80 nm. The morphologies of the ends were different; one end was composed of two globular particles, similar to the two-headed structure of myosin, while the other end had a more ill-defined structure, appearing either as a globular particle, an aggregate of two to four small granules, or a frayed, fan-like structure. The folded kinesin molecule possessed a hinge region in the middle of the rod, at about 32 nm from the neck of the two heads. In our preparations, the majority of adrenal kinesin molecules were folded at physiological salt concentrations. Adrenal kinesin bound to microtubules in the presence of adenylyl imidodiphosphate (AMP-PNP) also displayed a folded morphology.
    Additional Material: 7 Ill.
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