On the mechanisms involved in biological heme crystallization |
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Authors: | Renata?Stiebler Juliana?B?R?Correa?Soares Bruno?L?Timm José?Roberto?Silva Flavia?B?Mury Email author" target="_blank">Marilvia?Dansa-PetretskiEmail author Email author" target="_blank">Marcus?F?OliveiraEmail author |
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Institution: | (1) Present address: School of Biochemistry, Genetics, Microbiology and Plant Pathology, University of KwaZulu-Natal, P.O. Box XO1, Scottsville, 3209 Pietermaritzburg, South Africa |
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Abstract: | Blood-feeding organisms digest hemoglobin, releasing large quantities of heme inside their digestive tracts. Free heme is
very toxic, and these organisms have evolved several mechanisms to protect against its deleterious effects. One of these adaptations
is the crystallization of heme into the dark-brown pigment hemozoin (Hz). Here we review the process of Hz formation, focusing
on organisms other than Plasmodium that have contributed to a better understanding of heme crystallization. Hemozoin has been found in several distinct classes
of organisms including protozoa, helminths and insects and Hz formation is the predominant form of heme detoxification. The
available evidence indicates that amphiphilic structures such as phospholipid membranes and lipid droplets accompanied by
specific proteins play a major role in heme crystallization. Because this process is specific to a number of blood-feeding
organisms and absent in their hosts, Hz formation is an attractive target for the development of novel drugs to control illnesses
associated with these hematophagous organisms. |
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