Publications by authors named "Macarena Rodriguez-Walker"

The genomes of most protozoa encode families of variant surface antigens. In some parasitic microorganisms, it has been demonstrated that mutually exclusive changes in the expression of these antigens allow parasites to evade the host's immune response. It is widely assumed that antigenic variation in protozoan parasites is accomplished by the spontaneous appearance within the population of cells expressing antigenic variants that escape antibody-mediated cytotoxicity.

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Giardia lamblia encodes several families of cysteine-rich proteins, including the Variant-specific Surface Proteins (VSPs) involved in the process of antigenic variation. Their characteristics, definition and relationships are still controversial. An exhaustive analysis of the Cys-rich families including organization, features, evolution and levels of expression was performed, by combining pattern searches and predictions with massive sequencing techniques.

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Article Synopsis
  • * The monoclonal antibody MC-813-70 was studied, showing it binds to SSEA-4 on triple-negative breast cancer cells and is rapidly internalized into the cells, accumulating in lysosomes.
  • * The MC-813-70 antibody can effectively deliver the saporin toxin to SSEA-4-expressing cancer cells, reducing their viability, and could be a promising targeted therapy option in combination with traditional chemotherapy.
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At the outer leaflet of the plasma membrane, gangliosides are found with other glycosphingolipids, phospholipids, and cholesterol in glycolipid-enriched microdomains, in which they interact with signaling molecules including receptor tyrosine kinases and signal transducers. The role of gangliosides in the regulation of signal transduction has been reported for many cases and in different cell types. The biosynthesis of gangliosides involves specific enzymes, mainly glycosyltransferases that control together with glycohydrolases, the steady state of gangliosides at the cell surface.

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Membrane-bound sialidase Neu3 is involved in the catabolism of glycoconjugates, and plays crucial roles in numerous biological processes. Since the mechanism of its association with membranes is still not completely understood, the aim of this work was to provide further information regarding this aspect. Human Neu3 was found to be associated with the plasma membrane and endomembranes, and it was not released from the lipid bilayer under conditions that typically release peripheral membrane proteins.

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Gangliosides are sialic acid-containing glycosphingolipids mainly expressed at the outer leaflet of the plasma membrane. Sialidase NEU3 is a key enzyme in the catabolism of gangliosides with its up-regulation having been observed in human cancer cells. In the case of CME (clathrin-mediated endocytosis), although this has been widely studied, the role of NEU3 and gangliosides in this cellular process has not yet been established.

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Article Synopsis
  • Altered gene regulation networks significantly impact cancer development, influencing protein activity and cell metabolism, including enzymes responsible for glycolipid metabolism.
  • The abnormal glycosylation of glycolipids on cancer cell surfaces is increasingly recognized as a target for immunotherapy, leading to various promising treatment options in clinical trials.
  • This review discusses the metabolic pathways of glycolipids in both healthy and cancerous cells, highlighting sialosylated glycolipids and current therapeutic strategies involving these molecules in cancer treatment.
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