ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 95 (1974), S. 275-278 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Unusual cell surface structures found only on the symbiotic, flagellate protozoan,Pyrsonympha, are described for the first time.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1615-6102
    Keywords: Flagella ; Microspheres ; Gliding motility ; Protein dephosphorylation ; Chlamydomonas ; Plasma membrane ; Membrane protein dynamics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The biflagellate green algaChlamydomonas can exhibit substrate-associated gliding motility in addition to its ability to swim through a liquid medium. The flagella are the organelles responsible for both forms of whole-cell locomotion although the mechanism in each case is very different. In this study, we demonstrate that the binding of polystyrene microspheres to the flagellar surface ofChlamydomonas initiates clustering of the major flagellar-membrane glycoprotein, which is known to be involved in motility-associated substrate adhesion. In addition, we demonstrate that microsphere binding to the flagellar surface initiates the same transmembrane signaling pathway that is initiated by antibody- or lectin-induced crosslinking of the major flagellar-membrane glycoprotein. In each case, the signaling pathway involves the activation of a calciumdependent protein phosphatase that dephosphorylates a flagellar phosphoprotein known to be associated with the major flagellar-membrane glycoprotein. Bound microspheres are translocated along the flagellar surface at approximately the same velocity as whole-cell gliding motility. Previous observations suggest that microsphere binding and translocation along the flagellar surface may be a reflection of the same force-transducing system responsible for whole-cell gliding motility. In which case, these observations suggest that the transmembrane signaling pathway initiated by crosslinking the major flagellar-membrane glycoprotein is the same one that is activated when the cell contacts a physiological substrate by its flagellar surface.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 0886-1544
    Keywords: Chlamydomonas ; flagella ; cell surface ; adhesion ; glycoproteins ; iodination ; lactoperoxidase ; Iodogen ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The Chlamydomonas flagellar surface exhibits interesting adhesive properties that are associated with flagellar surface motility. This dynamic surface property can be exhibited as the binding and movement of small polystyrene microspheres or as the interaction of the flagellar surface with a solid substrate followed by whole cell locomotion, termed “gliding.” In order to identify flagellar surface proteins that mediate substrate interaction during flagellar surface motility, two immobilized iodination systems were employed that mimic the conditions for flagellar surface motility: small polystyrene microspheres derivatized with lactoperoxidase, and large glass beads derivatized with Iodogen. Use of these iodination conditions resulted in preferential iodination of a high-molecular-weight glycoprotein with apparent molecular weight of 300,000-350,000. These results suggest this glycoprotein as a major candidate for the surface-exposed adhesive component that directly interacts with the substrate and couples the substrate to a system of force transduction presumed to be located within the flagellum.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 4 (1984), S. 305-314 
    ISSN: 0886-1544
    Keywords: cell surface motility ; axopodia ; reticulopodia ; Allogromia ; Echinosphaerium (Actinosphaerium) nucleofilum ; surf-riding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The mechanism responsible for the energy-dependent movement of membrane components (ie, surface motility) is unknown. Recently a potentially unifying model, termed “surf-riding” [Hewitt, 1979] or “surf-boarding” [Berlin and Oliver, 1982], has been proposed to explain surface motility. Using phase-contrast light microscopy and membrane surface markers (polystyrene microspheres), we have tested the surf-riding/surf-boarding hypothesis on two protozoan systems: the axopodia of the heliozoan Echinosphaerium nucleofilum and the reticulopodial networks of the allogromiid foraminiferans Allogromia laticollaris and Allogromia sp, strain NF. Our evidence indicates that surface motility, as displayed by these organisms, does not occur by a surf-riding/surf-boarding mechanism. Previouś observations on surface motility associated with the Chlamydomonas flagellum indicate that this system is also incompatible with the surf-boarding/surf-riding hypothesis.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The termite gut flagellates are of interest because of their unusual motile organelles, their ability to digest cellulose, and their symbiotic relationship with prokaryotes inhabiting the insect gut. This report provides a detailed ultrastructural description of Pyrsonympha from the hind-gut of Reticulitermes flavipes.The motile axostyle is composed of 2,000-4,000 microtubules connected by cross-bridges. At its anterior end, the axostyle is associated with a “primary row” of microtubules which is associated with a fibrous network. The “primary row” is embedded in a large mass of amorphous, electron-dense material occupying the furthest anterior end of the cell. The basal bodies of the eight flagella are also embedded in this presumptive microtubule-organizing center. The flagella are associated with the cell surface throughout their length. Isolation and reactivation of the axostyle has demonstrated that although ATP dependent motility is inherent in the structure of the axostyle, its proper control may be mediated by the attachment of the axostyle to structures at the anterior end of the cell.Pyrsonympha lacks morphologically distinguishable mitochondria and Golgi complexes. The cell surface is covered by unique, previously underscribed, tubular specializations. Symbiotic microorganisms are observed associated with the cell surface and within the cytoplasm.Wood particles are taken up from the gut fluid by large phagocytic vacuoles formed at the posterior end of the cell. Even during the process of breakdown, the wood is always enclosed within the membrane of the phagocytic vacuole.The Pyrsonympha from Reticulitermes flavipes are not attached to the lining of the hind-gut and do not contain an attachment organelle, unlike the Pyrsonympha from other species of Reticulitermes.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 0886-1544
    Keywords: flagella ; membrane ; glycoproteins ; concanavalin A ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: As an alternative to swimming through liquid medium by the coordinated bending activity of its two flagella, Chlamydomonas can exhibit whole cell gliding motility through the interaction of its flagellar surfaces with a solid substrate. The force transduction occurring at the flagellar surface can be visualized as the saltatory movements of polystyrene microspheres. Collectively, gliding motility and polystyrene microsphere movements are referred to as flagellar surface motility. The principal concanavalin A binding, surface-exposed glycoproteins of the Chlamydomonas reinhardtii flagellar surface are a pair of glycoproteins migrating with apparent molecular weight of 350 kDa. It has been hypothesized that these glycoproteins move within the plane of the flagellar membrane during the expression of flagellar surface motility. A novel mutant cell line of Chlamydomonas (designated L-23) that exhibits increased binding of concanavalin A to the flagellar surface has been utilized in order to restrict the mobility of the concanavalin A-binding flagellar glycoproteins. Under all conditions where the lateral mobility of the flagellar concanavalin A binding glycoproteins is restricted, the cells are unable to express whole cell gliding motility or polystyrene microsphere movements. Conversely, whenever cells can redistribute their concanavalin A binding glycoproteins in the plane of the flagellar membrane, they express flagellar surface motility. Since the 350 kDa glycoproteins are the major surface-exposed flagellar proteins, it is likely that most of the signal being followed using fluorescein isothiocyanate (FITC)-concanavalin A is attributable to these high molecular weight glycoproteins. Therefore, it is likely that the 350 kDa glycoproteins are the ones that must move laterally in the plane of the flagellar membrane in order for the cell to express whole cell gliding motility and microsphere movements along the flagellar surface. This study represents one of the first demonstrations, in any cell type, that whole cell locomotion requires glycoprotein movement within the plane of the plasma membrane.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...