Affiliations: Institute of Biochemistry, Institute of Molecular Medicine, University of Lisbon Medical School, Lisbon, Portugal
Note: [] Corresponding author: J.P. Lopes de Almeida, Instituto de Bioquímica, Instituto de Medicina Molecular, Faculdade de Medicina de Lisboa, Edifício Egas Moniz, Av. Prof. Egas Moniz, 1649 028 Lisboa, Portugal. Tel.: +351 91 8985450; Fax: +351 21 7999477; E-mail: [email protected]
Abstract: In the present article the authors make an approach over the applications of dithiothreitol (DTT) in its different clinical-laboratory, potential and up-to-date sources. Dithiothreitol is a chemical reagent with a wide actuation spectrum not only from a laboratorial view but also from a therapeutic standpoint, more clinical and practical. DTT (i) is frequently used in a variety of experiences that involve proteins or peptides, protecting sulfhydryl groups from oxidation and reducing disulfide bonds between cysteines; (ii) is also used in the study of disulfide exchange reactions of protein disulfides; (iii) is able to keep glutathione in the reduced state; (iv) acts as an “antidote” enabling the activity of detoxification systems; (v) participates in cellular mechanisms such as vesiculation, cell morphology, signal transduction pathways (hormone-‘like’ role), etc.; (vi) can be used in the treatment approach of diseases like cystinosis or medical conditions resulting from ion or metal toxicity. In erythrocytes, there’s literature pointing that DTT may trigger changes on the normal discoid shape following metabolic depletion, and additionally modulate the exovesiculation kinetics as demonstrated by us. The present article dissects in detail recent findings in our Unit concerning the DTT influence on human erythrocytes.
