Intermediate filament protein synemin is present in human reactive and malignant astrocytes and associates with ruffled membranes in astrocytoma cells

Glia ◽  
2005 ◽  
Vol 50 (2) ◽  
pp. 107-120 ◽  
Author(s):  
Runfeng Jing ◽  
Gianpaolo Pizzolato ◽  
Richard M. Robson ◽  
Giulio Gabbiani ◽  
Omar Skalli
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Astrocytoma Cells ◽  
Filament Protein

scholarly journals Intermediate filament protein synemin contributes to the migratory properties of astrocytoma cells by influencing the dynamics of the actin cytoskeleton

2008 ◽  
Vol 22 (9) ◽  
pp. 3196-3206 ◽  
Author(s):  
Yihang Pan ◽  
Runfeng Jing ◽  
Aaron Pitre ◽  
Briana Jill Williams ◽  
Omar Skalli
Keyword(s):  
Actin Cytoskeleton ◽  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Astrocytoma Cells ◽  
Filament Protein

scholarly journals Reexpression of glial fibrillary acidic protein rescues the ability of astrocytoma cells to form processes in response to neurons.

1994 ◽  
Vol 127 (3) ◽  
pp. 813-823 ◽  
Author(s):  
W J Chen ◽  
R K Liem
Keyword(s):  
Glial Fibrillary Acidic Protein ◽  
Intermediate Filament ◽  
Nervous System Development ◽  
Acidic Protein ◽  
Stable Processes ◽  
Intermediate Filament Protein ◽  
Granule Neurons ◽  
Astrocytoma Cells ◽  
Filament Protein ◽  
U251 Cells

Astroglial cells play an important role in orchestrating the migration and positioning of neurons during central nervous system development. Primary astroglia, as well as astrocytoma cells will extend long stable processes when co-cultured with granule neurons. In order to determine the function of the glial fibrillary acidic protein (GFAP), the major intermediate filament protein in astroglia and astrocytoma cells, we suppressed the expression of GFAP by stable transfection of an anti-sense GFAP construct in human astrocytoma U251MG cells. The resulting AS2-U251 cells can no longer extend stable processes in the presence of granule neurons. To show that this effect is due specifically to the absence of GFAP, we reintroduced a fully encoding rat brain GFAP cDNA into these AS2-U251 cells. The resulting rat GFAP appeared as a filamentous network and the reexpression of GFAP rescued the ability of these astrocytoma cells to form stable processes when co-cultured with neurons. From these results, it is clear that the glial specific intermediate filament protein, GFAP, is required for process extension of these astrocytoma cells in response to granule neurons.

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

scholarly journals The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate

2005 ◽  
Vol 280 (17) ◽  
pp. 16882-16890 ◽  
Author(s):  
Svetlana Ermakova ◽  
Bu Young Choi ◽  
Hong Seok Choi ◽  
Bong Seok Kang ◽  
Ann M. Bode ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Epigallocatechin Gallate ◽  
Intermediate Filament Protein ◽  
Filament Protein

A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein

1993 ◽  
Vol 104 (4) ◽  
pp. 1263-1272 ◽  
Author(s):  
C.A. Bossie ◽  
M.M. Sanders
Keyword(s):  
Drosophila Melanogaster ◽  
Intermediate Filament ◽  
Blot Analysis ◽  
Polytene Chromosomes ◽  
Intermediate Filament Protein ◽  
Chromosome 2 ◽  
Cross Hybridization ◽  
Intermediate Filament Proteins ◽  
Nuclear Lamins ◽  
Filament Protein

A novel intermediate filament cDNA, pG-IF, has been isolated from a Drosophila melanogaster embryonic expression library screened with a polyclonal antiserum produced against a 46 kDa cytoskeletal protein isolated from Kc cells. This 46 kDa protein is known to be immunologically related to vertebrate intermediate filament proteins. The screen resulted in the isolation of four different cDNA groups. Of these, one has been identified as the previously characterized Drosophila nuclear lamin cDNA, Dm0, and a second, pG-IF, demonstrates homology to Dm0 by cross hybridization on Southern blots. DNA sequence analysis reveals that pG-IF encodes a newly identified intermediate filament protein in Drosophila. Its nucleotide sequence is highly homologous to nuclear lamins with lower homology to cytoplasmic intermediate filament proteins. pG-IF predicts a protein of 621 amino acids with a predicted molecular mass of 69,855 daltons. In vitro transcription and translation of pG-IF yielded a protein with a SDS-PAGE estimated molecular weight of approximately 70 kDa. It contains sequence principles characteristic of class V intermediate filament proteins. Its near neutral pI (6.83) and the lack of a terminal CaaX motif suggests that it may represent a lamin C subtype in Drosophila. In situ hybridization to polytene chromosomes detects one band of hybridization on the right arm of chromosome 2 at or near 51A. This in conjunction with Southern blot analysis of various genomic digests suggests one or more closely placed genes while Northern blot analysis detects two messages in Kc cells.

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