Impaired autophagy: The collateral damage of lysosomal storage disorders
| Autor: | Rosa Puertollano, Rachel Myerowitz, Nina Raben |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Lysosomal transport Batten disease Cystinosis Mutant lcsh:Medicine Review Gaucher disease engineering.material Biology General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Lysosome medicine Autophagy Animals Humans Danon disease lcsh:R5-920 lcsh:R Disease Management Pompe disease General Medicine medicine.disease Cell biology Lysosomal Storage Diseases 030104 developmental biology Batten medicine.anatomical_structure Organ Specificity 030220 oncology & carcinogenesis engineering Disease Susceptibility Lysosomes lcsh:Medicine (General) Biomarkers |
| Zdroj: | EBioMedicine, Vol 63, Iss, Pp 103166-(2021) EBioMedicine |
| ISSN: | 2352-3964 |
| Popis: | Lysosomal storage disorders (LSDs), which number over fifty, are monogenically inherited and caused by mutations in genes encoding proteins that are involved in lysosomal function. Lack of the functional protein results in storage of a distinctive material within the lysosomes, which for years was thought to determine the pathophysiology of the disorder. However, our current view posits that the primary storage material disrupts the normal role of the lysosome in the autophagic pathway resulting in the secondary storage of autophagic debris. It is this "collateral damage" which is common to the LSDs but nonetheless intricately nuanced in each. We have selected five LSDs resulting from defective proteins that govern widely different lysosomal functions including glycogen degradation (Pompe), lysosomal transport (Cystinosis), lysosomal trafficking (Danon), glycolipid degradation (Gaucher) and an unidentified function (Batten) and argue that despite the disparate functions, these proteins, when mutant, all impair the autophagic process uniquely. |
| Databáze: | OpenAIRE |
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