Molecular cloning and primary structure of human glial fibrillary acidic protein.
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.
Reeves
S A
SA
Molecular Genetics Section, National Cancer Institute, Bethesda, MD 20892.
Helman
L J
LJ
Allison
A
A
Israel
M A
MA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D002460:Cell Line; D003001:Cloning, Molecular; D005904:Glial Fibrillary Acidic Protein / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D014407:Tumor Cells, Cultured
D005904:Glial Fibrillary Acidic Protein