Vimentin intermediate filaments in fish melanophores

1987 ◽  
Vol 88 (5) ◽  
pp. 649-655
Author(s):  
F.K. Gyoeva ◽  
E.V. Leonova ◽  
V.I. Rodionov ◽  
V.I. Gelfand
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Polyclonal Antibodies ◽  
Cell Types ◽  
Immunofluorescence Staining ◽  
Intermediate Filament Protein ◽  
Transmission Electron ◽  
Filament Protein ◽  
Pterophyllum Scalare ◽  
Cell Centre

The distribution and chemical composition of intermediate filaments in cultured melanophores of two teleost species - Gymnocorymbus ternetzi and Pterophyllum scalare - were studied by immunofluorescence staining and immunoblotting techniques. The immunofluorescence staining of the melanophores with monoclonal and polyclonal antibodies to the intermediate filament protein vimentin revealed a system of fibrils radiating from the cell centre. These fibrils were resistant to 0.6 M-KCl and nocodazole treatments as has been found in other cell types. Transmission electron microscopy confirmed the presence of intermediate filaments in melanophores. Immunoblotting experiments showed the presence of the intermediate filament protein vimentin in melanophore lysates. Therefore, teleost melanophores possess a developed radial system of vimentin intermediate filaments.

Interactions between peripherin and neurofilaments in cultured cells: disruption of peripherin assembly by the NF-M and NF-H subunits

1999 ◽  
Vol 77 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Jean-Martin Beaulieu ◽  
Janice Robertson ◽  
Jean-Pierre Julien
Keyword(s):  
Nervous System ◽  
Peripheral Nervous System ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Cultured Cells ◽  
Intermediate Filament Protein ◽  
Physiological Conditions ◽  
Filament Protein ◽  
Filament Network ◽  
Filament Type

Neurofilaments are the principal intermediate filament type expressed by neurons. They are formed by the co-assembly of three subunits: NF-L, NF-M, and NF-H. Peripherin is another intermediate filament protein expressed mostly in neurons of the peripheral nervous system. In contrast to neurofilaments, peripherin can self-assemble to establish an intermediate filament network in cultured cells. The co-expression of neurofilaments and peripherin is found mainly during development and regeneration. We used SW13 cells devoid of endogenous cytoplasmic intermediate filaments to assess the exact assembly characteristics of peripherin with each neurofilament subunit. Our results demonstrate that peripherin can assemble with NF-L. In contrast, the co-expression of peripherin with the large neurofilament subunits interferes with peripherin assembly. These results confirm the existence of interactions between peripherin and neurofilaments in physiological conditions. Moreover, they suggest that perturbations in the stoichiometry of neurofilaments can have an impact on peripherin assembly in vivo.Key words: peripherin, neurofilament, SW13 cells, intermediate filament.

scholarly journals Autoimmune sequence of streptococcal M protein shared with the intermediate filament protein, vimentin.

1989 ◽  
Vol 169 (2) ◽  
pp. 481-492 ◽  
Author(s):  
W Kraus ◽  
K Ohyama ◽  
D S Snyder ◽  
E H Beachey
Keyword(s):  
Intermediate Filament ◽  
Mesangial Cells ◽  
Polyclonal Antibodies ◽  
M Protein ◽  
Intermediate Filament Protein ◽  
Glomerular Mesangial Cells ◽  
Western Blots ◽  
Autoimmune Antibodies ◽  
Streptococcal M Protein ◽  
Filament Protein

The crossreactivity of antibodies against a renal autoimmune epitope of Streptococcus pyogenes M protein with glomerular mesangial cells was investigated. The antibodies directed against the amino acid sequence Ile-Arg-Leu-Arg of the nephritogenic type 1 M protein reacted in a fibrillar pattern with mesangial cells cultured from isolated glomeruli. In Western blots of urea-extracted mesangial proteins, the antibodies reacted with a 56-kD protein. Monoclonal and polyclonal antibodies identified the 56-kD mesangial protein as vimentin. Two synthetic peptides of human vimentin containing the sequence Arg-Leu-Arg reacted with the autoimmune antibodies raised against a streptococcal M protein peptide. These results provide evidence that the intermediate filament protein vimentin shares autoimmune epitopes with streptococcal M protein.

scholarly journals A novel intermediate filament-associated protein, NAPA-73, that binds to different filament types at different stages of nervous system development.

1986 ◽  
Vol 102 (1) ◽  
pp. 246-251 ◽  
Author(s):  
G Ciment ◽  
A Ressler ◽  
P C Letourneau ◽  
J A Weston
Keyword(s):  
Monoclonal Antibody ◽  
Intermediate Filament ◽  
System Development ◽  
Cell Types ◽  
Embryonic Cell ◽  
Nervous System Development ◽  
Intermediate Filament Protein ◽  
Mature Neurons ◽  
Filament Protein ◽  
Vimentin Intermediate Filament

The antigen recognized by the E/C8-monoclonal antibody is expressed in various avian embryonic cell types known also to express neurofilament (NF) immunoreactivity. To determine whether the E/C8-antigen corresponds to any of the known NF components, we compared their subcellular locations, immunocross-reactivities, and electrophoretic behaviors. We found that the E/C8-antibody binds to NF bundles in electron microscope preparations of neurons, but does not correspond to any of the known NF proteins by immunological or electrophoretic criteria. Immunoadsorption with the monoclonal antibody resulted in co-purification of a 73,000-D protein with one of the known NF proteins in homogenates from 20-d embryonic chick brains, but with vimentin intermediate filament protein in similarly prepared homogenates from 4-d embryonic chicks. We suggest that the E/C8-antigen is an intermediate filament-associated protein that binds to different filament types at different stages of development. We have named it NAPA-73, an acronym for neurofilament-associated protein, avian-specific, 73,000 D, on the basis of its binding specificity in mature neurons.

scholarly journals Intermediate filaments EXC-2 and IFA-4 Maintain Luminal Structure of the Tubular Excretory Canals in Caenorhabditis elegans

2018 ◽  
Author(s):  
Hikmat I. Al-Hashimi ◽  
David H. Hall ◽  
Brian D. Ackley ◽  
Erik A. Lundquist ◽  
Matthew Buechner
Keyword(s):  
Caenorhabditis Elegans ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Light And Electron Microscopy ◽  
Intermediate Filament Protein ◽  
Apical Surface ◽  
Intermediate Filament Proteins ◽  
Canal Diameter ◽  
Excretory Canals ◽  
Filament Protein

ABSTRACTThe excretory canals of Caenorhabditis elegans are a model for understanding the maintenance of apical morphology in narrow single-celled tubes. Light and electron microscopy shows that mutants in exc-2 start to form canals normally, but these swell to develop large fluid-filled cysts that lack a complete terminal web at the apical surface, and accumulate filamentous material in the canal lumen. Here, whole-genome sequencing and gene rescue show that exc-2 encodes intermediate filament protein IFC-2. EXC-2/IFC-2 protein, fluorescently tagged via CRISPR/Cas9, is located at the apical surface of the canals independently of other intermediate filament proteins. EXC-2 is also located in several other tissues, though the tagged isoforms are not seen in the larger intestinal tube. Tagged EXC-2 binds via pulldown to intermediate filament protein IFA-4, which is also shown to line the canal apical surface. Overexpression of either protein results in narrow but shortened canals. These results are consistent with a model whereby three intermediate filaments in the canals, EXC-2, IFA-4, and IFB-1, restrain swelling of narrow tubules in concert with actin filaments that guide the extension and direction of tubule outgrowth, while allowing the tube to bend as the animal moves.Article SummaryThe C. elegans excretory canals form a useful model for understanding formation of narrow tubes. exc-2 mutants start to form normal canals that then swell into fluid-filled cysts. We show that exc-2 encodes a large intermediate filament (IF) protein previously not thought to be located in the canals. EXC-2 is located at the apical (luminal) membrane, binds to another IF protein, and appears to be one of three IF proteins that form a flexible meshwork to maintain the thin canal diameter. This work provides a genetically useful model for understanding the interactions of IF proteins with other cytoskeletal elements to regulate tube size and growth.

scholarly journals Phosphorylation of the peripherin 58-kDa neuronal intermediate filament protein

1989 ◽  
Vol 264 (8) ◽  
pp. 4619-4627
Author(s):  
J M Aletta ◽  
M L Shelanski ◽  
L A Greene
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Filament Protein
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