The glyoxalase system in health and disease.

Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications.

D-lactate production in erythrocytes infected with Plasmodium falciparum.

Summary
The Leishmania major aquaglyceroporin, LmAQP1, is responsible for the transport of trivalent metalloids, arsenite and antimonite. We have earlier shown that downregulation of LmAQP1 provides resistance to trivalent antimony compounds whereas increased expression of LmAQP1 in drug-resistant parasites can reverse the resistance. In this paper we describe the biochemical characterization of LmAQP1. Expression of LmAQP1 in Xenopus oocytes rendered them permeable to water, glycerol, methylglyoxal, dihydroxyacetone and sugar alcohols. The transport property of LmAQP1 was severely affected when a critical Arg230, located inside the pore of the channel, was altered to either alanine or lysine. Immunofluorescence and immuno-electron microscopy revealed LmAQP1 to be localized to the flagellum of Leishmania promastigotes and in the flagellar pocket membrane and contractile vacuole/spongiome complex of amastigotes. This is the first report of an aquaglyceroporin being localized to the flagellum of any microbe. Leishmania promastigotes and amastigotes expressing LmAQP1 could regulate their volume in response to hypoosmotic stress. Additionally, Leishmania promastigotes overexpressing LmAQP1 were found to migrate faster towards an osmotic gradient. These results taken together suggest that Leishmania LmAQP1 has multiple physiological roles, being involved in solute transport, volume regulation and osmotaxis.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-2958.2007.05845.x

Biochemical characterization of Leishmania major aquaglyceroporin LmAQP1: possible role in volume regulation and osmotaxis.

5. Introduction: the glyoxalase system 1.1. The glyoxalase system in oncology and haematology 1.1.1. The interest for oncologists and haematologists 1.1.2. The glyoxalase system: a definition 1.2. Glyoxalase I 1.2.1. Distribution and molecular characteristics 1.2.2. Physiological substrates, kinetics and mechanism 1.2.3. The active site and catalytic mechanism 1.2.4. Genetics, polymorphism and gene cloning 1.25. Non-giyoxalase I-dependent metabolism of methylglyoxal by aldehyde reductases to lactaldehyde and hydroxyacetone 1.3. Glyoxalase II 1.3.1. Distribution and molecular characteristics 1.3.2. Substrate specificity, kinetics and mechanism 1.3.3. Genetics and polymorphism 1.3.4. D-Lactate metabolism and excretion

Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor

Kalpana Ghoshal

Papers

Methylglyoxal-catabolizing enzymes of Leishmania donovani promastigotes.