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Estramustine-phosphate binds to a tubulin binding domain on microtubule-associated proteins MAP-2 and tau.

Artikel i vetenskaplig tidskrift
Författare D Moraga
A Rivas-Berrios
G Farías
Margareta Wallin
R B Maccioni
Publicerad i Biochimica et biophysica acta
Volym 1121
Nummer/häfte 1-2
Sidor 97-103
ISSN 0006-3002
Publiceringsår 1992
Publicerad vid Zoologiska institutionen
Sidor 97-103
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Amino Acid Sequence, Animals, Binding Sites, Brain, metabolism, Cattle, Estramustine, metabolism, Kinetics, Microtubule-Associated Proteins, chemistry, metabolism, ultrastructure, Molecular Sequence Data, Peptides, chemical synthesis, metabolism, Repetitive Sequences, Nucleic Acid, Tubulin, metabolism, tau Proteins, chemistry, metabolism, ultrastructure
Ämneskategorier Cell- och molekylärbiologi

Sammanfattning

Estramustine-phosphate (EMP), a phosphorylated conjugate of estradiol and nor-nitrogen mustard binds to microtubule-associated proteins MAP-2 and tau. It was shown that this estramustine derivative inhibits the binding of the C-terminal tubulin peptide beta-(422-434) to both MAP-2 and tau. This tubulin segment constitutes a main binding domain for these microtubule-associated proteins. Interestingly, estramustine-phosphate interacted with the synthetic tau peptides V187-G204 and V218-G235, representing two major repeats within the conserved microtubule-binding domain on tau and also on MAP-2. This observation was corroborated by the inhibitory effects of estramustine-phosphate on the tau peptide-induced tubulin assembly into microtubules. On the other hand, the nonphosphorylated drug estramustine failed to block the MAP peptide-induced assembly, indicating that the negatively charged phosphate moiety of estramustine-phosphate is of importance for its inhibitory effect. These findings suggest that the molecular sites for the action of estramustine-phosphate are located within the microtubule binding domains on tau and MAP-2.

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