scholarly journals Glial Fibrillary Acidic Protein (GFAP) in Oligodendrogliomas: A Reflection of Transient GFAP Expression by Immature Oligodendroglia

1986 ◽  
Vol 13 (4) ◽  
pp. 307-311 ◽  
Author(s):  
V. Jagadha ◽  
W.C. Halliday ◽  
L.E. Becker
Keyword(s):  
White Matter ◽  
Glial Fibrillary Acidic Protein ◽  
Tumor Cells ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Immunohistochemical Staining ◽  
Neuron Specific Enolase ◽  
Acidic Protein ◽  
Gfap Expression ◽  
S 100

ABSTRACT:Fourteen pure oligodendrogliomas were studied by light- and electronmicroscopy and immunohistochemistry to examine glial fibrillary acidic protein (GFAP) positivity in the tumors. To compare the immunohistochemical staining patterns of neoplastic oligodendroglia and immature oligodendroglia, myelination glia in the white matter of eight normal brains from children under 6 months of age were studied. The tumors possessed light microscopic and ultrastructural features characteristic of oligodendrogliomas. Microtubules were found in the cytoplasm of nine tumors on electronmicroscopy. In one, intermediate filaments and microtubules were observed in occasional tumor cells with polygonal crystalline structures in the cytoplasm. Using the peroxidase-antiperoxidase technique, all specimens were stained for GFAP, vimentin, S-100 and neuron-specific enolase (NSE). In nine tumors, variable numbers of cells with an oligodendroglial morphology reacted positively for GFAP. All tumors were positive for S-100 and negative for vimentin and NSE. The myelination glia in the eight normal brains stained positively for GFAP but not for vimentin. Vimentin is expressed by developing, reactive and neoplastic astrocytes. Thus, GFAP positivity combined with vimentin negativity in both neoplastic and immature oligodendroglia suggests that GFAP positivity in oligodendrogliomas may reflect the transient expression of this intermediate filament by immature oligodendroglia.

scholarly journals Disrupted glial fibrillary acidic protein network in astrocytes from vimentin knockout mice.

1996 ◽  
Vol 133 (4) ◽  
pp. 853-863 ◽  
Author(s):  
M Galou ◽  
E Colucci-Guyon ◽  
D Ensergueix ◽  
J L Ridet ◽  
M Gimenez y Ribotta ◽  
...  
Keyword(s):  
Glial Fibrillary Acidic Protein ◽  
Intermediate Filament ◽  
Network Formation ◽  
Reactive Astrocytes ◽  
Acidic Protein ◽  
Intermediate Filament Protein ◽  
Cultured Astrocytes ◽  
Gfap Expression ◽  
Gfap Immunoreactivity ◽  
Filament Protein

Glial fibrillary acidic protein (GFAP) is an intermediate filament protein expressed predominantly in astrocytes. The study of its expression in the astrocyte lineage during development and in reactive astrocytes has revealed an intricate relationship with the expression of vimentin, another intermediate filament protein widely expressed in embryonic development. these findings suggested that vimentin could be implicated in the organization of the GFAP network. To address this question, we have examined GFAP expression and network formation in the recently generated vimentin knockout (Vim-) mice. We show that the GFAP network is disrupted in astrocytes that normally coexpress vimentin and GFAP, e.g., those of the corpus callosum or the Bergmann glia of cerebellum. Furthermore, Western blot analysis of GFAP protein content in the cerebellum suggests that posttranslational mechanisms are implicated in the disturbance of GFAP network formation. The role of vimentin in this process was further suggested by transfection of Vim-cultured astrocytes with a vimentin cDNA, which resulted in the normal assembly of the GFAP network. Finally, we examined GFAP expression after stab wound-induced astrogliosis. We demonstrate that in Vim- mice, reactive astrocytes that normally express both GFAP and vimentin do not exhibit GFAP immunoreactivity, whereas those that normally express GFAP only retain GFAP immunoreactivity. Taken together, these results show that in astrocytes, where vimentin is normally expressed with GFAP fails to assemble into a filamentous network in the absence of vimentin. In these cells, therefore, vimentin appears necessary to stabilize GFAP filaments and consequently the network formation.

scholarly journals Expression of S-100 protein, glial fibrillary acidic protein, neuron-specific enolase, and keratin in mixed tumors of skin.

1987 ◽  
Vol 20 (5) ◽  
pp. 477-487 ◽  
Author(s):  
YOHKO NODA ◽  
HIROYUKI OOSUMI ◽  
HIDEMOTO HORIKE ◽  
HIROSHI MITANI ◽  
TAKAHIRO TSUJIMURA ◽  
...  
Keyword(s):  
Glial Fibrillary Acidic Protein ◽  
Neuron Specific Enolase ◽  
Acidic Protein ◽  
S 100 ◽  
Mixed Tumors

scholarly journals Expression of nestin and vimentin in gliomatosis cerebri

2006 ◽  
Vol 64 (3b) ◽  
pp. 781-786 ◽  
Author(s):  
Arlete Hilbig ◽  
Lígia Maria Barbosa-Coutinho ◽  
Nadima Toscani ◽  
Marlise de Castro Ribeiro ◽  
Bartira Silveira Campos da Cunha
Keyword(s):  
Glial Fibrillary Acidic Protein ◽  
Tumor Cells ◽  
Nervous Tissue ◽  
Immunohistochemical Analysis ◽  
Gliomatosis Cerebri ◽  
Acidic Protein ◽  
Rare Form ◽  
Tumor Mass ◽  
Undifferentiated Cells ◽  
High Degree

Gliomatosis cerebri (GC) is a rare form of CNS neoplasia in which there is diffuse involvement of the nervous tissue with or without the presence of tumor mass. The origin of the tumor is unknown, nor whether it represents a disease with diffuse onset or infiltration from a neoplastic focus. Here we studied the histopathologic characteristics of 6 cases with a diagnosis of GC and performed an immunohistochemical analysis using glial fibrillary acidic protein (GFAP), synaptophysin, nestin and vimentin. Most tumor cells were negative for GFAP, even though there were foci of positivity for this marker in all cases. We detected the presence of many positive cells for nestin and vimentin in all studied samples. The presence of these cells may indicate origin of the tumor from undifferentiated cells with a high degree of mobility.

scholarly journals Anomalous placement of introns in a member of the intermediate filament multigene family: an evolutionary conundrum.

1986 ◽  
Vol 6 (5) ◽  
pp. 1529-1534 ◽  
Author(s):  
S A Lewis ◽  
N J Cowan
Keyword(s):  
Glial Fibrillary Acidic Protein ◽  
Intermediate Filament ◽  
Multigene Family ◽  
Protein Gene ◽  
Sequence Data ◽  
Complete Sequence ◽  
Acidic Protein ◽  
Type I ◽  
Neurofilament Protein ◽  
Gene Encoding

The origin of introns and their role (if any) in gene expression, in the evolution of the genome, and in the generation of new expressed sequences are issues that are understood poorly, if at all. Multigene families provide a favorable opportunity for examining the evolutionary history of introns because it is possible to identify changes in intron placement and content since the divergence of family members from a common ancestral sequence. Here we report the complete sequence of the gene encoding the 68-kilodalton (kDa) neurofilament protein; the gene is a member of the intermediate filament multigene family that diverged over 600 million years ago. Five other members of this family (desmin, vimentin, glial fibrillary acidic protein, and type I and type II keratins) are encoded by genes with six or more introns at homologous positions. To our surprise, the number and placement of introns in the 68-kDa neurofilament protein gene were completely anomalous, with only three introns, none of which corresponded in position to introns in any characterized intermediate filament gene. This finding was all the more unexpected because comparative amino acid sequence data suggest a closer relationship of the 68-kDa neurofilament protein to desmin, vimentin, and glial fibrillary acidic protein than between any of these three proteins and the keratins. It appears likely that an mRNA-mediated transposition event was involved in the evolution of the 68-kDa neurofilament protein gene and that subsequent events led to the acquisition of at least two of the three introns present in the contemporary sequence.

scholarly journals The molecular cloning of glial fibrillary acidic protein in Gekko japonicus and its expression changes after spinal cord transection

2010 ◽  
Vol 15 (4) ◽  
Author(s):  
Dehong Gao ◽  
Yongjun Wang ◽  
Yan Liu ◽  
Fei Ding ◽  
Xiaosong Gu ◽  
...  
Keyword(s):  
Spinal Cord ◽  
White Matter ◽  
Glial Fibrillary Acidic Protein ◽  
Acidic Protein ◽  
Time Interval ◽  
Short Time Interval ◽  
Specific Marker ◽  
Class Iii ◽  
Intermediate Filament Proteins ◽  
Gekko Japonicus

AbstractThe glial fibrillary acidic protein (GFAP) is an astrocyte-specific member of the class III intermediate filament proteins. It is generally used as a specific marker of astrocytes in the central nervous system (CNS). We isolated a GFAP cDNA from the brain and spinal cord cDNA library of Gekko japonicus, and prepared polyclonal antibodies against gecko GFAP to provide useful tools for further immunochemistry studies. Both the real-time quantitative PCR and western blot results revealed that the expression of GFAP in the spinal cord after transection increased, reaching its maximum level after 3 days, and then gradually decreased over the rest of the 2 weeks of the experiment. Immunohistochemical analyses demonstrated that the increase in GFAP-positive labeling was restricted to the white matter rather than the gray matter. In particular, a slight increase in the number of GFAP positive star-shaped astrocytes was detected in the ventral and lateral regions of the white matter. Our results indicate that reactive astrogliosis in the gecko spinal cord took place primarily in the white matter during a short time interval, suggesting that the specific astrogliosis evaluated by GFAP expression might be advantageous in spinal cord regeneration.

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