Direct involvement of a lamin-B-related (54 kDa) protein in the association of intermediate filaments with the postsynaptic membrane of the Torpedo marmorata electrocyte

1995 ◽  
Vol 108 (1) ◽  
pp. 153-160
Author(s):  
A. Cartaud ◽  
B.J. Jasmin ◽  
J.P. Changeux ◽  
J. Cartaud
Keyword(s):  
Acetylcholine Receptor ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Early Stage ◽  
Postsynaptic Membrane ◽  
Muscle Fibres ◽  
Motor Innervation ◽  
Torpedo Marmorata ◽  
Lamin B ◽  
Stage Of Development

Mechanisms by which motor innervation induces postsynaptic membrane differentiation and functional compartmentalization of the subneural sarcoplasm in skeletal muscle fibres are still poorly understood. However, transmembrane control of cytoskeletal activities by the nerve terminal may be considered. Here, we examine several properties of a 54 kDa protein, previously identified in the postsynaptic membrane of the Torpedo marmorata electrocyte with anti-lamin B antibodies, in order to study its role in the assembly of the subneural intermediate filament meshwork. Using a ligand blot assay, we show that this protein binds desmin, a type III intermediate filaments protein, at micromolar concentrations. Moreover, purified acetylcholine receptor-rich membrane fragments are able to generate arrays of desmin filaments in vitro. Immunofluorescence experiments indicate that the 54 kDa protein becomes associated with the acetylcholine receptor-rich membrane at an early stage of development of the electrocyte, and that a polarized desmin network develops concomitantly from the postsynaptic membrane. Taken together, these data show that, like karyoskeletal lamin B, the 54 kDa protein is involved in the organization of the subneural intermediate filament meshwork. Control of the assembly of the subneural cytoskeleton by components of the postsynaptic membrane may thus be a prerequisite for the functional compartmentalization of the muscle fibre triggered by motor innervation.

Nucleation of intermediate filaments at the postsynaptic membrane in torpedo marmorata electrocytes

1991 ◽  
Vol 73 (2-3) ◽  
pp. 4a-4a
Author(s):  
A. Cartaud ◽  
B.J. Jasmin ◽  
J.P. Changeux ◽  
J. Cartaud
Keyword(s):  
Intermediate Filaments ◽  
Postsynaptic Membrane ◽  
Torpedo Marmorata

scholarly journals Asynchronous assembly of the acetylcholine receptor and of the 43-kD nu1 protein in the postsynaptic membrane of developing Torpedo marmorata electrocyte.

1989 ◽  
Vol 108 (1) ◽  
pp. 127-139 ◽  
Author(s):  
E Kordeli ◽  
J Cartaud ◽  
H O Nghiêm ◽  
A Devillers-Thiéry ◽  
J P Changeux
Keyword(s):  
Plasma Membrane ◽  
Acetylcholine Receptor ◽  
Postsynaptic Membrane ◽  
Synaptic Membrane ◽  
Asymmetric Distribution ◽  
Subsequent Stage ◽  
Torpedo Marmorata ◽  
Intracellular Compartments ◽  
Membrane Compartments

The assembly of the nicotinic acetylcholine receptor (AchR) and the 43-kD protein (v1), the two major components of the post synaptic membrane of the electromotor synapse, was followed in Torpedo marmorata electrocyte during embryonic development by immunocytochemical methods. At the first developmental stage investigated (45-mm embryos), accumulation of AchR at the ventral pole of the newly formed electrocyte was observed within columns before innervation could be detected. No concomitant accumulation of 43-kD immunoreactivity in AchR-rich membrane domains was observed at this stage, but a transient asymmetric distribution of the extracellular protein, laminin, which paralleled that of the AchR, was noticed. At the subsequent stage studied (80-mm embryos), codistribution of the two proteins was noticed on the ventral face of the cell. Intracellular pools of AchR and 43-kD protein were followed at the EM level in 80-mm electrocytes. AchR immunoreactivity was detected within membrane compartments, which include the perinuclear cisternae of the endoplasmic reticulum and the plasma membrane. On the other hand, 43-kD immunoreactivity was not found associated with the AchR in the intracellular compartments of the cell, but codistributed with the AchR at the level of the plasma membrane. The data reported in this study suggest that AchR clustering in vivo is not initially determined by the association of the AchR with the 43-kD protein, but rather relies on AchR interaction with extracellular components, for instance from the basement membrane, laid down in the tissue before the entry of the electromotor nerve endings.

Immunological characterization of lamins in the nuclear matrix of onion cells

1993 ◽  
Vol 106 (1) ◽  
pp. 431-439 ◽  
Author(s):  
A. Minguez ◽  
S. Moreno Diaz de la Espina
Keyword(s):  
Intermediate Filaments ◽  
Nuclear Matrix ◽  
Intermediate Filament ◽  
Higher Plants ◽  
Nuclear Periphery ◽  
Immunogold Labelling ◽  
Root Cells ◽  
Intermediate Filament Proteins ◽  
Lamin B

We have used polyclonal and monoclonal antibodies against different lamins from vertebrates, and the IFA antibody recognizing all kinds of intermediate filament proteins, to investigate the lamins of the nuclear matrix of Allium cepa meristematic root cells. All the antibodies react in the onion nuclear matrix with bands in the range of 60–65 kDa, which are enriched in the nuclear matrix after urea extraction, and do not crossreact with other antibodies recognizing intermediate filaments in plants (AFB, anti-vimentin and MAC 322), ruling out crossreaction with contaminating intermediate filaments of cytoplasmic bundles. In 2-D blots the chicken anti-lamin serum reacts with one spot at 65 kDa and pI 6.8 and the anti B-type lamin antibodies with another one at 64 kDa and pI 5.75. Both crossreact with IFA. The lamin is localized at the nuclear periphery and the lamina by indirect immunofluorescence. Immunogold labelling of nuclear matrix sections reveals that the protein is not only associated with the lamina, but also with the internal matrix. Taken together these results reveal that higher plants, which do not possess an organized network of cytoplasmic intermediate filaments, nevertheless present a well-organized lamina containing lamins in which at least one of them is immunologically related to vertebrate lamin B. Our data confirm that lamins are very old members of the intermediate filament proteins that have been better conserved in plants during evolution than their cytoplasmic counterparts.

Targeting of acetylcholine receptor and 43 kDa rapsyn to the postsynaptic membrane in Torpedo marmorata electrocyte

1998 ◽  
Vol 92 (3-4) ◽  
pp. 177-181 ◽  
Author(s):  
Fabrizia Bignami ◽  
Gilles Camus ◽  
Sophie Marchand ◽  
Lise Bailly ◽  
Françoise Stetzkowski-Marden ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Postsynaptic Membrane ◽  
Torpedo Marmorata

scholarly journals Expression of the intermediate-filament-associated protein synemin in chicken lens cells.

1984 ◽  
Vol 4 (10) ◽  
pp. 1943-1950 ◽  
Author(s):  
B L Granger ◽  
E Lazarides
Keyword(s):  
Skeletal Muscle ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Early Stage ◽  
Cellular Structures ◽  
Fiber Cells ◽  
The Core ◽  
New Information ◽  
Avian Muscle ◽  
Lens Cells

Synemin, a 230-kilodalton polypeptide component of avian muscle and erythrocyte intermediate filaments, is also found in association with the vimentin filaments of lens tissue. In chicken lens cells, synemin is bound to the core vimentin polymer with the same 180-nm periodicity that it exhibits in erythrocytes. Its solubility properties are characteristic of those of intermediate filaments in general and similar to those of synemin in muscle cells and erythrocytes. Synemin appears at an early stage of lens development and undergoes a dramatic accumulation as the epithelial cells elongate and differentiate into fiber cells. In contrast to synemin in cultured skeletal muscle, lens synemin is not confined to postmitotic, terminally differentiating cells but is present in proliferative cells as well. It is lost from the fibers near the center of the lens, as are many other cellular structures including intermediate filaments. These findings provide new information about the occurrence and expression of avian synemin and new insight regarding its presumptive role as a modulator of intermediate-filament function.

scholarly journals Expression of the intermediate-filament-associated protein synemin in chicken lens cells

1984 ◽  
Vol 4 (10) ◽  
pp. 1943-1950
Author(s):  
B L Granger ◽  
E Lazarides
Keyword(s):  
Skeletal Muscle ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Early Stage ◽  
Cellular Structures ◽  
Fiber Cells ◽  
The Core ◽  
New Information ◽  
Avian Muscle ◽  
Lens Cells

Synemin, a 230-kilodalton polypeptide component of avian muscle and erythrocyte intermediate filaments, is also found in association with the vimentin filaments of lens tissue. In chicken lens cells, synemin is bound to the core vimentin polymer with the same 180-nm periodicity that it exhibits in erythrocytes. Its solubility properties are characteristic of those of intermediate filaments in general and similar to those of synemin in muscle cells and erythrocytes. Synemin appears at an early stage of lens development and undergoes a dramatic accumulation as the epithelial cells elongate and differentiate into fiber cells. In contrast to synemin in cultured skeletal muscle, lens synemin is not confined to postmitotic, terminally differentiating cells but is present in proliferative cells as well. It is lost from the fibers near the center of the lens, as are many other cellular structures including intermediate filaments. These findings provide new information about the occurrence and expression of avian synemin and new insight regarding its presumptive role as a modulator of intermediate-filament function.

scholarly journals Matching of muscle properties and motoneurone firing patterns during early stages of development

1985 ◽  
Vol 115 (1) ◽  
pp. 113-123 ◽  
Author(s):  
G. Vrbova ◽  
R. Navarrete ◽  
M. Lowrie
Keyword(s):  
Muscle Fibre ◽  
Early Stage ◽  
Activity Patterns ◽  
Muscle Fibres ◽  
Functional Requirements ◽  
Muscle Properties ◽  
Fibre Properties ◽  
Early Stages ◽  
Stage Of Development ◽  
Further Development

In adults, muscle fibres match the functional requirements of the motoneurone that supplies them. During early stages of postnatal development of the rat neither muscle fibre properties, nor activity patterns of motoneurones supplying fast and slow muscles have completed their differentiation. Nevertheless, even at this early stage of development the muscles have characteristic properties that are well matched to the activity patterns of immature motoneurones. With further development differentiation of motoneurone activity and muscle fibre properties goes hand in hand. If during this period of linked differentiation, connections between the motoneurones and muscle fibres are disrupted, the development of fast muscles is permanently impaired.

The Application of UX Research in New Energy Vehicle Innovation

2019 ◽  
Vol 1 (1) ◽  
Author(s):  
Menghan TAO ◽  
Ning XIAO ◽  
Xingfu ZHAO ◽  
Wenbin LIU
Keyword(s):  
Early Stage ◽  
Rapid Expansion ◽  
The Other ◽  
Innovative Product ◽  
Stage Of Development ◽  
New Energy ◽  
New Energy Vehicle ◽  
The One ◽  
New Energy Vehicles ◽  
Degree Of Innovation

New energy vehicles(NEV) as a new thing for sustainable development, in China, on the one hand has faced the rapid expansion of the market; the other hand, for the new NEV users, the current NEVs cannot keep up with the degree of innovation. This paper demonstrates the reasons for the existence of this systematic challenge, and puts forward the method of UX research which is different from the traditional petrol vehicles research in the early stage of development, which studies from the user's essence level, to form the innovative product programs which meet the needs of users and being real attractive.

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