Chloroquine lysosomal degradation

Discussion in 'International Pharmacy' started by zistiancasose, 25-Feb-2020.

  1. mamon Guest

    Chloroquine lysosomal degradation


    In MDA-MB-231 cells, immunolocalization and brefeldin A protein transport blocking studies revealed that there was a propensity for newly synthesized Cx43 to be transported to lysosomes. On the other hand, light and electron microscopic analysis of BICR-M1R cells showed that Cx43 gap junctions were prevalent with a subpopulation of intracellular Cx43 localized to lysosomes.

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    Degraded by the non-lysosomal pathways. 4. Chloroquine and methylamine, which accumulate in lysosomes by virtue of their weak base properties, inhibited hepatocytic protein degradation to the same extent as ammonia, with no additivity. These compounds therefore seem to block the lysosomal pathway of protein degradation The effects of chloroquine as a retinopathic agent, as observed by lysosomal dysfunction and RPE degradation, have been demonstrated in various animal models 21–24. We use the ability of chloroquine to increase pH 25 to both understand the general effects of chloroquine on ARPE-19, and as a model for lysosomal inhibition. I am trying to block lysosomal degradation in tubular epithelial cells derived from mice kidneys. To that end, I am treating these cells with 100 micromolar Chloroquine 16hours. chloroquine.

    Interestingly, lactacystin inhibition of proteosomal degradation in MDA-MB-231 cells resulted in a marked increase in phosphorylated Cx43 at the expense of non-phosphorylated Cx43, and this change corresponded with an increase in “oversized” gap junction plaques. In both cell types, Western blots revealed a notable increase in total cellular Cx43 in response to lysosome inhibitors.

    Chloroquine lysosomal degradation

    The Lysosomal Protein Saposin B Binds Chloroquine - Huta., Chloroquine treatment of ARPE-19 cells leads to lysosome.

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  4. Lysosomal degradation mechanisms are crucial for the formation, differentiation, and degradation of epithelial cell junctions. Epithelial cells use selective autophagy to degrade claudin-2, in response to the stimulation with the epidermal growth factor.

    • Lysosomal Degradation of Junctional Proteins IntechOpen.
    • Questions with answers in CHLOROQUINE Science topic.
    • Chloroquine - an overview ScienceDirect Topics.

    However, the incidence of gap junction plaques did increase by 61–88% when lysosomal and proteasomal degradation were simultaneously inhibited Fig. 6, D, F, and H, double arrows, and I, suggesting that it was proteasomal, but not lysosomal, inhibition that was responsible for the increase in number of gap junction plaques in MDA-MB-231vCx43. Chloroquine and methylamine, which accumulate in lysosomes by virtue of their weak base properties, inhibited hepatocytic protein degradation to the same extent as ammonia, with no additivity. These compounds therefore seem to block the lysosomal pathway of protein degradation selectively and completely. This accumulation leads to inhibition of lysosomal enzymes that require an acidic pH, and prevents fusion of endosomes and lysosomes. Moreover, Chloroquine inhibits autophagy as it raises the lysosomal pH, which leads to inhibition of both fusion of autophagosome with lysosome and lysosomal protein degradation 4.

     
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