Identification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase.

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TitleIdentification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase.
Publication TypeJournal Article
Year of Publication1986
AuthorsZimmer, DB, Van Eldik, LJ
JournalJ Biol Chem
Volume261
Issue24
Pagination11424-8
Date Published1986 Aug 25
ISSN0021-9258
KeywordsAmino Acid Sequence, Animals, Brain, Calcium, Cyanogen Bromide, Enzyme Activation, Fructose-Bisphosphate Aldolase, Liver, Molecular Weight, Peptide Fragments, Rabbits, Rats, S100 Proteins
Abstract

A rat brain S100-binding protein, R40,000, has been isolated, characterized, and identified as fructose-1,6-bisphosphate aldolase. R40,000 was purified by ammonium sulfate precipitation, hydroxylapatite chromatography, dye-binding chromatography, and electroelution from sodium dodecyl sulfate-polyacrylamide gels. Microsequence analysis of a fragment of R40,000 revealed a 15-residue amino acid sequence which shows a high degree of homology to the amino acid sequence of fructose-1,6-bisphosphate aldolase from rabbit muscle and rat liver. Further characterization demonstrated that R40,000 has an amino acid composition, subunit molecular weight, and cyanogen bromide map similar to aldolase. In addition, purified aldolase interacts with S100 alpha and S100 beta by gel overlay, and aldolase enzyme activity is stimulated 2-fold in vitro by S100 alpha and S100 beta. S100 interacts predominantly with the C or brain-specific form of the enzyme in gels and stimulates the activity of the C-enriched form of the enzyme in a calcium-dependent manner. Altogether, these data suggest that fructose-1,6-bisphosphate aldolase may be an intracellular target of S100 action in brain.

Alternate JournalJ. Biol. Chem.
PubMed ID3733759
Grant ListGM33481 / GM / NIGMS NIH HHS / United States