Oceanography and Marine Environment of the Basque Country. Elsevier Oceanography Series 70. Edited by A. Borja and M. Collins (2004) Elsevier B.V., Amsterdam. ISBN 0-444-51581-X. ISSN 0422-9894 (Series).

This is not a book that you probably start reading from thefirst page. Its 24 review chapters have informative titles andare organised in seven sections that together with a four-pagelocation index and an eight-page subject index invites you todive for your favourite subjects. The editors have succeededto structure the book in ways that makes easy navigation amongstits     

Redox modulation of tau and microtubule-associated protein-2 by the glutathione/glutaredoxin reductase system

Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative diseases including Alzheimer's and Parkinson's. We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Oxidation and reduction of cysteines in tau and microtubule-associated protein-2 were quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Reduction of disulfide bonds in the microtubule-associated proteins by the glutaredoxin reductase system restored their ability to promote the assembly of microtubules composed of purified porcine tubulin. Thiol-disulfide exchange between oxidized glutathione and the microtubule-associated proteins was detected by monitoring protein oxidation and was quantitated by measuring reduced glutathione by HPLC.     

Cysteine oxidation of tau and microtubule-associated protein-2 by peroxynitrite: modulation of microtubule assembly kinetics by the thioredoxin reductase system

Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative conditions including Alzheimer and Parkinson diseases. We report that peroxynitrite- and hydrogen peroxide-induced disulfides in the neuron-specific microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the ubiquitous thioredoxin reductase system composed of thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH. Tau and microtubule-associated protein-2 cysteine oxidation and reduction were quantitated by monitoring the incorporation of 5-iodoacetamidofluorescein, a thiol-specific labeling reagent. Cysteine oxidation of tau and microtubule-associated protein-2 to disulfides altered the ability of the proteins to promote the assembly of microtubules from purified porcine tubulin. Treatment of tau and microtubule-associated protein-2 with either the thioredoxin reductase system or small molecule reductants fully restores the ability of the MAPs to promote microtubule assembly. Thus changes in the redox state of microtubule-associated proteins may regulate microtubule polymerization in vivo.