Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 1989 Jul;86(13):5178-82.

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

Author information

1
Molecular Genetics Section, National Cancer Institute, Bethesda, MD 20892.

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--particularly 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 of this 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.

PMID:
2740350
PMCID:
PMC297581
DOI:
10.1073/pnas.86.13.5178
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center