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Differences in the effect of Ca2+ on isolated microtubules from cod and cow brain.

Artikel i vetenskaplig tidskrift
Författare E Strömberg
Margareta Wallin
Publicerad i Cell motility and the cytoskeleton
Volym 28
Nummer/häfte 1
Sidor 59-68
ISSN 0886-1544
Publiceringsår 1994
Publicerad vid Zoologiska institutionen
Sidor 59-68
Språk en
Länkar dx.doi.org/10.1002/cm.970280106
Ämnesord Animals, Brain, metabolism, Calcium, pharmacology, Cations, Divalent, pharmacology, Cattle, Fishes, Microtubule-Associated Proteins, drug effects, metabolism, Microtubules, drug effects, metabolism, ultrastructure, Nephelometry and Turbidimetry, Polymers, metabolism, Temperature, Tubulin, drug effects, metabolism
Ämneskategorier Cell- och molekylärbiologi

Sammanfattning

Isolated microtubules from cod and cow brains were compared with respect to their response to calcium ions. The effect of Ca2+ on cod microtubules was found to be temperature dependent. In contrast to cow microtubules, cod microtubules assembled at 18 degrees C. At this temperature the assembly was inhibited by Ca2+ concentrations of 2 mM and higher. This was also found for cow microtubules at 37 degrees C. However, at 30 degrees C there was no effect of 2 mM Ca2+ of the amount of assembly or disassembly of cod microtubules consisting of only tubulin or of tubulin and microtubule-associated proteins (MAPs). The morphology was affected though, since some coiled ribbons formed from tubulin and MAPs. The calcium-binding calmodulin did not alter the effect of calcium on cod microtubules markedly. At higher Ca2+ concentrations (> 4 mM), coiled ribbons were formed from cod tubulin and MAPs, but mainly amorphous aggregates and very few coiled ribbons were formed from cod tubulin alone, indicating that the Ca2+ effect is modulated by cod MAPs. The modulatory effect of cod MAPs was however not species specific, since both cod and cow MAPs had the same effect on cod microtubules, in spite of a different protein composition. A MAP-dependent effect of Ca2+ was also found for cow microtubule proteins. The assembly of pure cow tubulin, as well as that of cow tubulin and MAPs, was inhibited by 2 mM Ca2+. In the presence of 10 and 20 mM Ca2+, pure cow tubulin formed amorphous aggregates, rings, and even paracrystals, while the assembly of cow tubulin and MAPs was inhibited. Our results suggest therefore that the effect of Ca2+ can be moderated by MAPs, but depends on intrinsic properties of the different tubulins.

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