Reorganization of the centrosome and associated microtubules during the morphogenesis of a mouse cochlear epithelial cell

1994 ◽  
Vol 107 (2) ◽  
pp. 589-600 ◽  
Author(s):  
C.G. Henderson ◽  
J.B. Tucker ◽  
M.A. Chaplin ◽  
J.B. Mackie ◽  
S.N. Maidment ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Cell Surface ◽  
Organ Of Corti ◽  
The Other ◽  
Cell Junctions ◽  
Microtubule Bundle ◽  
Microtubule Organizing Centres ◽  
A Cell ◽  
Basal Portion ◽  
Mouse Organ

Reorganization of centrosomal microtubule-organizing centres and the minus ends of microtubules occurs as the centrosomal ends of large microtubule bundles are repositioned and anchored to cell junctions in certain epithelial cells called inner pillar cells in the mouse organ of Corti. The microtubule bundle that assembles in each cell consists of two distinct microtubule arrays that run closely alongside each other. Both arrays are attached to the cell surface at their upper and lower ends. One of the arrays spans the entire length of a cell but the other is confined to its lower portion. Initially, about 3,000 microtubules elongate downwards from an apically situated centrosome in each cell. Subsequently, the minus ends of these microtubules, and the centrosome and its two centrioles, migrate for about 12 microns to the tip of a laterally directed projection. Then, a meshwork of dense material accumulates to link microtubule minus ends and the centrosome to cell junctions at the tip of the projection. Pericentriolar satellite bodies, which form after the initial burst of microtubule nucleation, may represent a condensed and inactive concentration of microtubule-nucleating elements. Surprisingly, as a cell matures, about 2,000 microtubules are eliminated from the centrosomal end of the microtubule bundle. However, about 2,000 microtubules are added to the basal portion of each bundle at levels that are remote with respect to the location of the centrosome. Possibly, these microtubules have escaped from the centrosome. If this is the case, then both the plus and minus ends of most of the errant microtubules are captured by sites at the cell surface where the ends are finally anchored. Alternatively, each cell possesses at least one other major microtubule-nucleating site (which does not possess centrioles) in addition to its centrosome.

scholarly journals Three microtubule-organizing centres collaborate in a mouse cochlear epithelial cell during supracellularly coordinated control of microtubule positioning

1995 ◽  
Vol 108 (1) ◽  
pp. 37-50 ◽  
Author(s):  
C.G. Henderson ◽  
J.B. Tucker ◽  
M.M. Mogensen ◽  
J.B. Mackie ◽  
M.A. Chaplin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Basement Membrane ◽  
Cell Surface ◽  
Basilar Membrane ◽  
Apical Cell ◽  
Organ Of Corti ◽  
Large Cell ◽  
Cell Junctions ◽  
Microtubule Bundle ◽  
Microtubule Organizing Centres

Large cell surface-associated microtubule bundles that include about 3,000 microtubules assemble in certain epithelial cells called inner pillar cells in the mouse organ of Corti. Microtubule-organizing centres (MTOCs) at both ends and near the middle of each cell act in concert during control of microtubule positioning. In addition, the three cell surface-associated microtubule-organizing centres are involved in coordinating the connection of bundle microtubules to cytoskeletal components in neighbouring cells and to a basement membrane. The precisely defined locations of the three MTOCs specify the cell surface regions where microtubule ends will finally be anchored. The MTOCs are modified as anchorage proceeds. Substantial fibrous meshworks assemble at the surface sites occupied by the MTOCs and link microtubule ends to cell junctions. This procedure also connects the microtubule bundle to cytoskeletal arrays in neighbouring cells at two of the MTOC sites, and to the basilar membrane (a substantial basement membrane) in the case of the third site. A fourth meshwork that is not positioned at a major MTOC site is involved in connecting one side of the microtubule bundle to the cytoskeletons of two other cell neighbours. The term surfoskelosome is suggested for such concentrations of specialized cytoskeletal materials and junctions at cell surface anchorages for cytoskeletal arrays. The large microtubule bundle in each cell is composed of two closely aligned microtubule arrays. Bundle assembly begins with nucleation of microtubules by a centrosomal MTOC that is attached to the apical cell surface. These microtubules elongate downwards and the plus ends of many of them are apparently captured by a basal MTOC that is attached to the plasma membrane at the bottom of the cell. In the lower portion of the cell, the microtubule bundle also includes a basal array of microtubules but these elongate in the opposite direction. This investigation provides evidence that they extend upwards from the basal MTOC to be captured by a medial MTOC which is attached to the plasma membrane and situated near the mid-level of the cell. However, there are substantial indications that the basal array's microtubules are also nucleated by the apically situated centrosomal MTOC, but escape from it, and are translocated downwards for capture of their plus ends by the basal MTOC. If this is the case, then these microtubules continue to elongate after translocation and extend back up to the medial MTOC, which captures their minus ends.

A cell surface-associated centrosomal layer of microtubule-organizing material in the inner pillar cell of the mouse cochlea

1992 ◽  
Vol 102 (2) ◽  
pp. 215-226 ◽  
Author(s):  
J.B. Tucker ◽  
C.C. Paton ◽  
G.P. Richardson ◽  
M.M. Mogensen ◽  
I.J. Russell
Keyword(s):  
Cell Surface ◽  
Cultured Cells ◽  
Organ Of Corti ◽  
Microtubule Assembly ◽  
Apical Surface ◽  
Large Numbers ◽  
Pericentriolar Material ◽  
A Cell ◽  
Mouse Organ

This investigation provides evidence that pericentriolar material is divorced from the immediate vicinities of centrioles and becomes functionally associated with the plasmalemma during the differentiation of a mammalian cell type. Such events occur prior to the assembly of large transcellular microtubule bundles in columnar epithelial cells called inner pillar cells in the mouse organ of Corti. The microtubules do not radiate from a typical centrosome and its centrioles. They elongate from a microtubule-organizing centre (MTOC), which is deployed as a subapical cell surface-associated layer in each cell. Most of the dense material of this layer, and the tops of most of the microtubules, are initially concentrated around the sides of a cell about 1 microns below its apical surface. In addition, a pair of centrioles is located above the layer, which acts as if it is a pericellular concentration of the pericentriolar material of a modified centrosome. Although microtubule nucleation takes place in a centrosome-like region, 13 protofilament fidelity is not exercised. Most of the microtubules have 15 protofilaments. Microtubule assembly progresses in these cells after the organ of Corti has been isolated for in vitro culture. However, large numbers of microtubules elongate from pericentriolar material juxtaposed against the centrioles. Hence, there is some reversion by the centrosomes of cultured cells to the operational configuration regarded as typical for animal tissue cells in general.

scholarly journals The MDCK epithelial cell line expresses a cell surface antigen of the kidney distal tubule.

1982 ◽  
Vol 93 (2) ◽  
pp. 269-277 ◽  
Author(s):  
D A Herzlinger ◽  
T G Easton ◽  
G K Ojakian
Keyword(s):  
Monoclonal Antibody ◽  
Epithelial Cell ◽  
Cell Surface ◽  
Cell Line ◽  
Surface Antigen ◽  
Mdck Cells ◽  
Distal Tubule ◽  
Cell Surface Antigen ◽  
Thick Ascending Limb ◽  
A Cell

Monoclonal antibodies were prepared against the Madin-Darby canine kidney (MDCK) cell line to identify epithelial cell surface macromolecules involved in renal function. Lymphocyte hybrids were generated by fusing P3U-1 myeloma cells with spleen cells from a C3H mouse immunized with MDCK cells. Hybridomas secreting anti-MDCK antibodies were obtained and clonal lines isolated in soft agarose. We are reporting on one hybridoma line that secretes a monoclonal antibody that binds to MDCK cells at levels 20-fold greater than background binding. Indirect immunofluorescence microscopy was utilized to study the distribution of antibody binding on MDCK cells and on frozen sections of dog kidney and several nonrenal tissues. In the kidney the fluorescence staining pattern demonstrates that the antibody recognizes an antigenic determinant that is expressed only on the epithelial cells of the thick ascending limb of Henle's loops and the distal convoluted tubule and appears to be localized on the basolateral plasma membrane. This antigen also has a unique distribution in non-renal tissues and can only be detected on cells known to be active in transepithelial ion movements. These results indicate the probable distal tubule origin of MDCK and suggest that the monoclonal antibody recognizes a cell surface antigen involved in physiological functions unique to the kidney distal tubule and transporting epithelia of nonrenal tissues.

Cytoskeletal involvement in the sequential capping of rat thymocyte surface glycoproteins

1988 ◽  
Vol 89 (3) ◽  
pp. 309-319
Author(s):  
C.E. Turner ◽  
M.R. Newton ◽  
D.M. Shotton
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Cytoskeletal Proteins ◽  
The Other ◽  
A Cell ◽  
Major Surface ◽  
Surface Glycoproteins

The independent capping of the three major rat thymocyte glycoproteins, the leucocyte-common (L-C) antigen, the leucocyte sialoglycoprotein (LSGP) and Thy-1, was investigated using specific monoclonal antibodies. The capping of each antigen did not require redistribution of the other major surface glycoproteins, and was accompanied by a partial co-capping of the cytoskeletal proteins fodrin and actin, but not of tubulin. A study of the ability of a cell that already possesses one glycoprotein cap to cap a second different glycoprotein showed that this was possible in all cases to varying degrees, the second cap always forming at the same position on the cell surface as the first. Colchicine failed to perturb this observed sequential capping polarity, indicating that microtubules did not direct this second capping event.

scholarly journals Teratocarcinoma stem cell adhesion: the role of divalent cations and a cell surface lectin.

1983 ◽  
Vol 96 (6) ◽  
pp. 1532-1537 ◽  
Author(s):  
L B Grabel ◽  
M S Singer ◽  
G R Martin ◽  
S D Rosen
Keyword(s):  
Stem Cells ◽  
Stem Cell ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Divalent Cations ◽  
Intercellular Adhesion ◽  
The Other ◽  
Calcium Dependent ◽  
A Cell

We describe two additive systems of intercellular adhesion in teratocarcinoma stem cells (Nulli cell line). One component is divalent cation-dependent (Ca++ or Mg++) and the other involves a cell surface fucan/mannan-specific lectin, previously identified on stem cells by an erythrocyte rosetting assay. The existence of these two systems is inferred from the observation that reaggregation of stem cells was partially inhibited by the removal of divalent cations or by the presence of lectin inhibitors such as fucoidan, but reaggregation was completely blocked when the two conditions were combined. Our results are related to recent work describing a calcium-dependent system of intercellular adhesion in teratocarcinoma stem cells.

scholarly journals Chemotactic reorientation of granulocytes stimulated with micropipettes containing fMet-Leu-Phe

1981 ◽  
Vol 52 (1) ◽  
pp. 1-10
Author(s):  
G. Gerisch ◽  
H.U. Keller
Keyword(s):  
Cell Surface ◽  
Temporal Change ◽  
The Other ◽  
Left Hand ◽  
Surface Areas ◽  
Right Hand ◽  
Human Granulocytes ◽  
A Cell ◽  
Attractant Concentration

Human granulocytes were stimulated by means of a micropipette, with an orifice of about 0.2 micrometer in diameter, which contained fMet-Leu-Phe at a concentration of 10(−5) M. The cells were reorientated by extending lamellipodia towards the source of the attractant, often within less than 10 s. Any part of the granulocyte, from the front to the tip of the tail, could be stimulated to produce new lamellipodia. Usually, but not always, this response occurred at the side of the cell nearest to the micropipette. Cells stimulated from behind responded in one of the following ways: (1) Cells that maintained their polarity extended new lamellipodia at one side of the leading front and reorientated by moving in a U-turn towards the micropipette. Occasionally, the leading front was split because one part of the front tried to make a left-hand and the other a right-hand turn. (2) Formation of lamellipodia at the leading front was arrested and new lamellipodia were formed at the tail instead, indicating reversal of polarity. The result was an immediate change in the direction of locomotion by about 180 degrees. (3) A combination of the first 2 forms of behaviour was observed occasionally. Transiently, lamellipodia were extended from cell surface areas both close to and distant from the micropipette. These observations show that parts of a cell can respond independently to chemotactic gradients by extending lamellipodia towards the source of the attractant. The phenomenon can easily be explained by assuming that a temporal change of attractant concentration is recognized.

scholarly journals A Cell Junctional Protein Network Associated with Connexin-26

2018 ◽  
Vol 19 (9) ◽  
pp. 2535 ◽  
Author(s):  
Ana Batissoco ◽  
Rodrigo Salazar-Silva ◽  
Jeanne Oiticica ◽  
Ricardo Bento ◽  
Regina Mingroni-Netto ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Organ Of Corti ◽  
Adaptor Protein ◽  
Cell Junctions ◽  
Connexin 26 ◽  
Affinity Capture ◽  
C Terminus ◽  
Family Protein ◽  
A Cell ◽  
Junctional Protein

GJB2 mutations are the leading cause of non-syndromic inherited hearing loss. GJB2 encodes connexin-26 (CX26), which is a connexin (CX) family protein expressed in cochlea, skin, liver, and brain, displaying short cytoplasmic N-termini and C-termini. We searched for CX26 C-terminus binding partners by affinity capture and identified 12 unique proteins associated with cell junctions or cytoskeleton (CGN, DAAM1, FLNB, GAPDH, HOMER2, MAP7, MAPRE2 (EB2), JUP, PTK2B, RAI14, TJP1, and VCL) by using mass spectrometry. We show that, similar to other CX family members, CX26 co-fractionates with TJP1, VCL, and EB2 (EB1 paralogue) as well as the membrane-associated protein ASS1. The adaptor protein CGN (cingulin) co-immuno-precipitates with CX26, ASS1, and TJP1. In addition, CGN co-immunoprecipitation with CX30, CX31, and CX43 indicates that CX association is independent on the CX C-terminus length or sequence. CX26, CGN, FLNB, and DAMM1 were shown to distribute to the organ of Corti and hepatocyte plasma membrane. In the mouse liver, CX26 and TJP1 co-localized at the plasma membrane. In conclusion, CX26 associates with components of other membrane junctions that integrate with the cytoskeleton.

Infection of Escherichia coli with bacteriophages

1969 ◽  
Vol 27 ◽  
pp. 370-371
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Cell Surface ◽  
Virus Type ◽  
Infection Process ◽  
Adsorption Site ◽  
The Other ◽  
Specific Receptors ◽  
Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

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