Disease relevance of GFAP

• Although small numbers of tetanus toxin-binding, A2B5+, GFAP+ cells were present in suspensions of freshly dissected, neonatal optic nerves, most of the type 2 astrocytes in cultures of such optic nerves developed from tetanus toxin-binding, A2B5+, GFAP- cells, which were induced to express GFAP by the culture conditions [1].
• The cytoplasm and fibrous component in the differentiated fibrillary astrocytoma were strongly positive for S-100 protein and GFAP [2].
• Immunohistochemically, the intracranial MPNST was strongly positive for S-100 protein and vimentin, and in places weakly positive for glial fibrillary acid protein (GFAP) [2].
• This tumor expressing both NF and GFAP may be histogenetically related to brain tumors of pluripotential cell origin in calves [3].
• Using this cDNA as a probe we investigated the levels of GFAP expression in ten human glioma cell lines [4].

Psychiatry related information on GFAP

• We discuss the relationship between the anti-GFAP autoantibody and the pathogenesis of Alzheimer's disease and suggest that the evaluation of anti-GFAP autoantibody level may be useful in diagnosing Alzheimer's disease [5].

High impact information on GFAP

• Electron microscopy demonstrated that alpha-crystallin particles could bind to intermediate filaments in a regular fashion, the spacing coinciding with the molecular length of GFAP [6].
• We find that the alpha-crystallins dramatically inhibit the in vitro assembly of GFAP and vimentin in an ATP-independent manner [6].
• Glial fibrillary acidic protein (GFAP) is a component of glial filaments specific to astroglia [7].
• We now report the spatial and temporal distributions of four phosphorylated sites in the GFAP molecule during mitosis of astroglial cells, determined by antibodies which can distinguish phosphorylated epitopes from non-phosphorylated-epitopes [7].
• Using galactocerebroside as a marker of oligodendrocyte differentiation and glial fibrillary acidic protein as a marker of astrocyte differentiation, we show that the acquisition of these marker molecules occurs rapidly in culture and requires both RNA and protein synthesis [8].

Biological context of GFAP

• The phosphorylation site was determined as Ser-12 of porcine GFAP [9].
• Computer-assisted analysis of the GFAP sequence revealed several EF-hand-like areas which could be the calcium binding sites [10].
• The kinetics and dynamics of glial fibrillary acidic protein (GFAP) assembly was explored by a fluorescence energy transfer assay method [11].
• Analysis of species specificity and of the epitope, determined using synthetic phosphopeptides, indicated that this antibody recognized the local phosphorylation-site sequence Thr-phosphoSer-Ala-Ala-Arg-Arg (residues 7-12 of GFAP) [12].
• Confluent monolayers of astrocytes (85% astroglial as assessed by GFAP immunoreactivity) were subcultured at low cell density and after 2-3 days growth were rendered quiescent by shifting them to low serum medium (0.25%) for several days [13].

Anatomical context of GFAP

• Neoplastic epithelial cells were positive immunohistochemically for pancytokeratin and S-100, and negative for GFAP [14].
• It was shown that MAb E501 cross-reacts with glial fibrillary acidic protein (GFAP), the class III intermediate filament protein found in astrocytes and other related glial elements [15].
• Use of a heterologous monoclonal antibody for cloning and detection of glial fibrillary acidic protein in the bovine ventricular ependyma [15].
• We have previously shown that enriched preparations of oligodendrocytes from either mature bovine brain or 30-d-old rat brain, when cultured in serum-free medium, yield mixed cultures of oligodendrocytes and astrocytes even though no GFAP+ cells were present after 24 hr in culture (Norton et al., 1986, 1988) [16].
• F-BPE reduced immunolabeling for L-NGFR but increased expression of both GFAP and the major peripheral myelin protein, P0 [17].

Associations of GFAP with chemical compounds

• The binding of S-100 protein to GFAP was investigated by fluorescence spectroscopy using acrylodan-S-100 protein and cross-linking experiments using the bifunctional cross-linker, disuccinimidyl suberate [18].
• Purified GFAP was stoichiometrically labeled at a single cysteine residue with fluorescein-maleimide [11].
• Pretreatment with DDC potentiated the effect of MPTP in striatum and resulted in substantially greater dopamine depletion, as well as a more pronounced elevation in GFAP [19].
• 4. After removal of unbound 45Ca2+, GFAP was observed to bind calcium [10].
• Systemically administered MPP+ decreased heart norepinephrine, but did not alter the striatal levels of dopamine or GFAP, and pretreatment with DDC did not alter these effects, but did increase lethality [19].

Physical interactions of GFAP

• Annexin II also cosediments with GF and binds to GFAP, although to much smaller extents [20].

Other interactions of GFAP

• Viral antigen was present in vacuolated NF 200-, GFAP- and fibronectin-positive cells [21].
• Muller cells displayed no immunoreactivity, but SPARC was present in retinal astrocytes that were identified by the astrocyte marker glial fibrillary acidic protein (GFAP) [22].
• Nuclear runoff assays showed that the effect of TNF on GFAP mRNA was at the posttranscriptional level [23].
• These analyses revealed the presence of GFAP mRNA in the cultures of cortical and leptomeningeal cells and of protein in all cell types; Von Willebrand factor mRNA was detectable in HUV-EC cells but undetectable in cortical, leptomeningeal and bovine aortic endothelial cells [24].
• The samples were examined for the presence of central nervous system (CNS)-specific proteins (syntaxin 1B and/or glial fibrillary acidic protein (GFAP), as indicators of contamination with CNS tissue [25].

Analytical, diagnostic and therapeutic context of GFAP

• In situ hybridization experiments failed to detect GFAP transcripts in SCO ependymocytes, confirming the abscence of immunoreactivity in these cells [15].
• The method is based on the detection of ruminant glial fibrillary acidic protein (GFAP) mRNA by applying real-time RT-PCR [26].
• Immunofluorescence microscopy showed that approximately 80% of the cells were positive for glial fibrillary acidic protein (GFAP) and greater than 80% were stained with an antiserum to the molecular weight 58,000 fibroblast intermediate filament protein (vimentin) [27].
• To locate the calcium-binding regions, GFAP peptides were examined for calcium binding by calcium-45 autoradiography [10].
• Rocket immunoelectrophoresis showed that the 51,000 astrocyte protein reacted with an antiserum to bovine GFAP, but the 58,000 and 42,000 proteins failed to react [27].

References