Interactions of intermediate filaments with cell structures

Carmo‐Fonseca, Maria; David-Ferreira, J. F.

doi:10.1016/0892-0354(90)90017-m

Cited by 66 publications

(26 citation statements)

References 154 publications

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“…These data suggest that their assembly may be under control of some common morphogenetical factor(s). A close association of actin filaments and other cytoskeletal components is well known in somatic cells (see review in Carmo-Fonseca and David-Ferreira 1990). Their association also suggests a role in their spatial organization, as in the case of the interaction of the vimentin tail with actin-containing structures (Cary et al 1994).…”

Section: Discussionmentioning

confidence: 99%

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Escalier

Gallo²,

Schrével³

1997

J Histochem Cytochem.

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SUMMARY Among the monoclonal antibodies (MAbs) prepared against human sperm extracts, MAb 4F7 was found to be specific to the human and Macaca fascicularis sperm cytoskeletal fibrous sheath (FS). In Western blotting, MAb 4F7 stains a doublet of polypeptides of about M r 95 ϫ 10 3 in extracts of human sperm cells. These polypeptides are not recognized by the KL1 anti-cytokeratin MAb, nor by the MAbs known to bind to the carboxy terminal (IFA) and to the amino terminal (ME101) rod domain of intermediate filaments.Sequential extraction procedures shows that the FS polypeptides recognized by MAb 4F7 are exposed after treatment with 8 M urea. 4F7 immunoreactivity is lost after treatment with high ionic solutions (NaCl, KCl, KI). Immunogold electron microscopy reveals that this protein is present throughout the FS. This FS antigenic determinant first accumulates in an FS proximal body in late spermatids, then in granules extending distally along the flagellum. Staining of spermatozoa with flagellar dysgenesis reveals that this FS protein colocalizes with actin no matter what the location of their abnormal assembly. These data suggest that the transient microtubule-like spindle-shaped body of as yet unknown function could be involved in FS protein deposition and that the assembly of the FS and actin could be under the control of some common morphogenetical factor(s). MAb 4F7 should allow further investigations of this peri-axonemal structure in both normal and pathological conditions. (J Histochem Cytochem 45:909-922, 1997)

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Section: Discussionmentioning

confidence: 99%

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Escalier

Gallo²,

Schrével³

1997

J Histochem Cytochem.

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“…3C). As well, AA-treated osteoblasts were more sensitive to NH 4 Cl treatment, showing significantly reduced dispersed lysosomes, compared with AA-treated cells in Ringer's solution alone (Fig. 3C).…”

Section: Role Of Cytosolic Ph In Lysosome Distribution In Osteoblasts-mentioning

confidence: 95%

“…The major cytoskeletal component that dictates the final location of organelles is the microtubule (MT) 3 cytoskeleton (3), with intermediate filaments also playing a role for certain organelles (4). MTs are long polarized polymers that interact indirectly with organelles through motor and adaptor proteins (5).…”

mentioning

confidence: 99%

Lysosome Dispersion in Osteoblasts Accommodates Enhanced Collagen Production during Differentiation

Nabavi

Urukova

Cardelli

et al. 2008

Journal of Biological Chemistry

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Lysosomes are essential organelles for intracellular degradation and are generally sequestered near the cell center to receive vesicles with contents targeted for destruction. During ascorbic acid (AA)-induced differentiation of osteogenic cells (Beck, G. R., Jr., Zerler, B., and Moran, E. (2001) Cell Growth Differ. 12, 61-83), we saw a marked increase in total lysosome organelles in osteoblastic cells, in addition to an enhanced endocytic rate. Interestingly, lysosomes were dispersed toward the cell periphery in differentiating osteoblasts. We determined that lysosome dispersion in differentiated osteoblasts required intact microtubules for long range transport and was dependent on kinesin motors but did not involve cytosolic acidification. Impairment of lysosome dispersion markedly reduced AA-induced osteoblast differentiation. Lysosomes were not secreted in differentiated osteoblasts, implicating them instead in intracellular degradation. We assayed the degradative capacity and saw a significant increase in DQ-ovalbumin fluorescence in differentiated osteogenic cells compared with undifferentiated control cells. Osteogenic cells are specialized for type I collagen production, and we noted enhanced secreted and intracellular collagen in AA-differentiated osteoblasts versus control cells. Importantly, osteoblasts displayed procollagen-containing vesicles that were distributed throughout the cytoplasm, a portion of which colocalized with lysosomes. Treatment of cells with 2,2-dipyridyl to inhibit procollagen trimerization enhanced colocalization of lysosomes with procollagen-containing organelles, implicating dispersed lysosomes in collagen processing in osteogenic cells.Proper organelle positioning is essential in all eukaryotic cells for inter-organelle trafficking, protein targeting, cellular homeostasis, and response to extracellular stimuli (2). The intracellular organellar architecture is dictated by the protein scaffold of the cell, namely the cytoskeleton. The major cytoskeletal component that dictates the final location of organelles is the microtubule (MT) 3 cytoskeleton (3), with intermediate filaments also playing a role for certain organelles (4). MTs are long polarized polymers that interact indirectly with organelles through motor and adaptor proteins (5). The relative abundance and/or activity of motor proteins on the organelles is believed to determine whether the organelle will be positioned in the cell center (toward the MT minus ends) or toward the plasma membrane (at MT plus ends). Organelles, such as mitochondria and melanosomes, are held toward the cell periphery through the actions of the kinesin motor (6, 7), whereas the minus end-directed motor, dynein, is responsible for holding the nucleus, Golgi complex, lysosomes, and recycling endosomes within the cell interior (8).Although most eukaryotic cells have a similar spatial organization of organelles, there are cell-specific differences in organelle quantities and positioning. The relative abundance of organelles can vary from cell to ce...

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“…The cytoskeleton, via a interfilamentous network of vimentin, connects molecules at the cell surface to lamin-B on the outer surface of the nuclear envelope (Ingber 1993;Carmo-Fonseca and David-Ferreira, 1990;Steinert and Roop 1988;Georgatos and Blobel 1987). In turn, this interacts with the nuclear matrix, forming a continuous fibrous network that ultimately ends up at specific sites on chromosomes (Puck and Krystosek 1992;Geiger 1987).…”

Section: Discussionmentioning

confidence: 99%

Insulin-like Growth Factor I (IGF-I) Induces Unique Effects in the Cytoskeleton of Cultured Rat Glomerular Mesangial Cells

Berfield

Aspray

Abrass

1997

J Histochem Cytochem.

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SUMMARYResident glomerular mesangial cells (MCs) have complex cytoskeletal organizations that maintain functional and structural integrity. The ability of cells to replicate, coordinate movement, change shape, and interact with contiguous cells or extracellular matrix depends on cytoskeletal organization. MCs synthesize insulin-like growth factor (IGF-I), express IGF-I receptors, and respond to IGF-I with increased proliferation. We noted that IGF-I treatment of mesangial cells was associated with a change in morphology. Therefore, these studies were undertaken to define specific IGF-I-mediated changes in cytoskeletal protein organization. Rat MCs were propagated from birth in culture without supplemental insulin. Quiescent, subconfluent cultures were treated with IGF-I (100 nM) for 1 hr. Rearrangements in f-actin, ␣ -smooth muscle actin, ␤ -actin, vimentin, and vinculin were seen by fluorescence microscopy. As the cytoskeleton rearranged, ␣ -smooth muscle actin dissociated from the f-actin bundles and ␤ -actin became polymerized under the leading lamellar edge. Ultrastructural changes were consistent with increased membrane turnover and metabolic activity. The normally sessile mesangial cell was induced by IGF-I to express a woundhealing phenotype characterized by movement and increased pinocytosis. These changes are different from those induced by insulin and have important implications for mesangial cell function. ( J Histochem Cytochem 45:583-593, 1997)

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Interactions of intermediate filaments with cell structures

Cited by 66 publications

References 154 publications

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Immunochemical Characterization of a Human Sperm Fibrous Sheath Protein, Its Developmental Expression Pattern, and Morphogenetic Relationships with Actin

Lysosome Dispersion in Osteoblasts Accommodates Enhanced Collagen Production during Differentiation

Insulin-like Growth Factor I (IGF-I) Induces Unique Effects in the Cytoskeleton of Cultured Rat Glomerular Mesangial Cells

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