Effects of nine synthetic putative metabolites of primaquine on activity of the hexose monophosphate shunt in intact human red blood cells in vitro

Jk, Baird; Gj, McCormick; Cj, Canfield

doi:10.1016/0006-2952(86)90145-0

Cited by 29 publications

(18 citation statements)

References 35 publications

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“…Other studies indicate that it causes mitochondrial swelling in several Plasmodium strains and stages [85][86][87], including P. falciparum gametocytes [88]. Additional reports suggest that exposure to PQ affects mitochondrial proliferation and inhibits growth on development stages that require functional mitochondria [87,[89][90][91][92][93].…”

Section: A Yet Unveiled Mechanism Of Actionmentioning

confidence: 99%

Primaquine revisited six decades after its discovery

Vale¹,

Moreira²,

Gomes³

2009

European Journal of Medicinal Chemistry

322

308

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Section: A Yet Unveiled Mechanism Of Actionmentioning

confidence: 99%

Primaquine revisited six decades after its discovery

Vale¹,

Moreira²,

Gomes³

2009

European Journal of Medicinal Chemistry

322

308

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“…The depletion is explained by the recycling mechanism, and once the glutathione is depleted, the continued formation of methemoglobin should stop [76]. The hexose monophosphate shunt was also stimulated to produce more NADPH [77]. Since in these cases the oxidized substrate can be rereduced the result is a cycle driving hemoglobin into methemoglobin (Fig.…”

Section: Acquired Methemoglobinemiamentioning

confidence: 99%

Methemoglobin—It's not just blue: A concise review

Umbreit¹

2006

American J Hematol

334

280

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Hemoglobin has functions besides carrying oxygen to the tissues, and regulates vascular tone and inflammation via a redox couple with methemoglobin. Hemoglobin has iron in the reduced valance Fe(II) and methemoglobin has iron in the oxidized valance Fe (III), with a free energy capable of producing water from oxygen. In generating methemoglobin the couple functions as a nitrite reductase. The degree of oxidation of hemoglobin senses the oxygen level in the blood and uses its ability to produce nitric oxide from nitrite to control vascular tone, increasing blood flood when the proportion of oxygenated hemoglobin falls. Additional cardiovascular damage is produced by methemoglobin mediated oxidation of light density lipoproteins, accelerating arteriosclerosis. In addition, the release of heme from methemoglobin is an important factor in inflammation. These physiologic functions are paralleled by the well-described role in the oxidation of various drugs resulting in methemoglobinemia. Am. J. Hematol. 82:134-144, 2007. V V C 2006 Wiley-Liss, Inc.

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“…23 No.11for the hemolytic toxicity of the drug to people with G6PD deficiency. The largely hypothetical 6-methoxy metabolites of PQ do exhibit relatively strong activity against P. berghei liver stages [66], and when present in an environment favoring oxidized species (like redox-challenged G6PD-deficient red blood cell cytoplasm) become potentially toxic membrane disruptors [67,68].…”

Section: The Puzzle Of Primaquine Therapymentioning

confidence: 99%