![]() ![]() ![]() In this chapter, we describe current methodologies to quantitatively analyze CMA activity in different experimental models.Ĭhaperones Lysosomes Proteolysis Subcellular fractionation. Chaperone-mediated autophagy (CMA) is a unique proteolytic pathway, in which cytoplasmic proteins recognized by heat shock cognate protein 70 (Hsc70/HSPA8) are transported into lysosomes for. Dysfunctional CMA occurs with age and has now been described in a growing list of human pathologies such as metabolic disorders, neurodegeneration, cancer, immunodeficiency, and diabetes. Lastly, due to the intrinsic protein selectivity of CMA, this type of autophagy exerts regulatory functions by mediating timely degradation of key cellular proteins that participate in processes such as lipid and glucose metabolism, cell cycle, DNA repair, and cellular reprogramming, among others. Here, we report reduced CMA activity in vascular smooth muscle cells and macrophages in murine and human arteries in response to atherosclerotic challenges. CMA also participates in the control of the cellular energetic balance through recycling of amino acids resulting from lysosomal proteolysis of the substrate proteins. Chaperone-mediated autophagy (CMA) contributes to regulation of energy homeostasis by timely degradation of enzymes involved in glucose and lipid metabolism. ![]() CMA plays an important role in maintaining cellular proteostasis by eliminating damaged and altered proteins. Chaperone-Mediated Autophagy of eNOS in Myocardial Ischemia-Reperfusion Injury Circ Res. There, they are translocated into the organelle lumen through a lysosomal membrane receptor/translocation complex. These proteins are identified by a chaperone that targets them to lysosomes. Chaperone-mediated autophagy (CMA) is a selective type of autophagy whereby a specific subset of intracellular proteins is targeted to the lysosome for degradation. Chaperone-mediated autophagy plays an important role in regulating retinal progenitor cell homeostasis. ![]()
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