Molecular cloning and primary structure of human glial fibrillary acidic protein.

Abstract

Glial fibrillary acidic protein (GFAP) is an intermediate-filament (IF) protein that is highly specific for cells of astroglial lineage, although its tissue-specific role is speculative. Determination of the primary structure of this protein should be of importance for understanding the functional role it plays in astroglia. Therefore, we isolated a cDNA clone encoding this protein and determined its nucleotide sequence. The predicted amino acid sequence indicates that GFAP shares structural similarities-particularl in the central rod domain and to a lesser degree in the carboxyl-terminal domain-with other IF proteins found in nonepithelial cell types. Considerable sequence divergence in the amino-terminal region of GFAP suggests that the tissue-specific functions ofthis IF protein might be mediated through this region of the molecule. In contrast, conservation of structural characteristics and a moderate degree of sequence conservation in the carboxyl-terminal region suggest functional similarities. Blot hybridization analysis using the GFAP cDNA as a probe failed to detect GFAP mRNA in both normal and neoplastic human tissues in which IF proteins other than GFAP are known to be expressed.

Accumulation of glial fibrillary acidic protein and histone H4 in brain storage bodies of Tibetan terriers with hereditary neuronal ceroid lipofuscinosis

“…A number of GFAP splice variants have also been reported in humans and other species (Condorelli et al 1999;Nielsen et al 2002;Singh et al 2003). Canine isoform 2 corresponds to the isoform that is normally expressed predominantly in humans (Fuchs and Weber 1994;Reeves et al 1989). Therefore, it is unlikely that Tibetan terrier NCL results from an abnormality in GFAP mRNA splicing or excessive production of a minor isoform.…”

The assembly state of the intermediate filament proteins desmin and glial fibrillary acidic protein at low ionic strength

“…Desmin resembles vimentin closely with respect to isoelectric point (pI 5.4) and size of the amino-and carboxy-end domains (approximately 100 and 55 residues, respectively) [11]. The pI of GFAP is slightly higher (pI 5.7), while the size of the amino end domain is considerably smaller (approximately 45 amino acids) than that of vimentin and desmin [12].…”

Human neurospheres: From stained sections to three-dimensional assembly

“…Note also the presence of a single larger cell with a bulging base continuing with a tiny process. [25] but also be considered as a possible marker of immature precursors and neuroblasts [26]. …”