Molecular cloning and primary structure of human glial fibrillary acidic protein

S. A. Reeves, L. J. Helman, A. Allison, M. A. Israel

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)5178-5182
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number13
DOIs
StatePublished - 1989

ASJC Scopus subject areas

  • General

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