Publications by authors named "Arnela Mehmedbasic"
Sorting protein-related receptor containing LDLR class A repeats (SORLA; also known as LR11) exerts intraneuronal trafficking functions in the central nervous system. Recently, involvement of SORLA in retinogenesis was proposed, but no studies have examined yet in detail the expression pattern of this sorting receptor in the retina. Here, we provide a spatio-temporal characterization of SORL1 mRNA and its translational product SORLA in the postnatal mouse retina.
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- - Gaucher Disease (GD) is caused by mutations in the GBA gene, which disrupts the function of the enzyme GCase, and potential therapy involves manipulating heat shock proteins to improve protein homeostasis.
- - The investigational drug arimoclomol, currently in phase II/III trials, enhances the function and activity of mutated GCase in cells from GD patients, showing promise for neurological symptoms due to its ability to cross the blood-brain barrier.
- - Findings indicate that arimoclomol boosts the production of protective proteins (HSPs), improving GCase function across various genetic mutations, supporting its clinical development as a potential treatment for the neuronopathic forms of GD.
The amyloid precursor protein (APP) and its neurotoxic cleavage product Aβ are key players in the development of Alzheimer's disease (AD) and appear to be essential for neuronal development and cell homeostasis. Proteolytic processing of APP and its physiological function depend on its interaction with heparin and are influenced by the binding of metal ions and sorLA. We created various mutations of metal binding site M1 residing within the extracellular E2 domain of APP.
View Article and Find Full Text PDFSorLA is a neuronal sorting receptor that is genetically associated with Alzheimer disease. SorLA interacts directly with the amyloid precursor protein (APP) and affects the processing of the precursor, leading to a decreased generation of the amyloid-β peptide. The SorLA complement-type repeat (CR) domains associate in vitro with APP, but the precise molecular determinants of SorLA·APP complex formation and the mechanisms responsible for the effect of binding on APP processing have not yet been elucidated.
View Article and Find Full Text PDFsorLA is a sorting receptor for amyloid precursor protein (APP) genetically linked to Alzheimer's disease (AD). Retromer, an adaptor complex in the endosome-to-Golgi retrieval pathway, has been implicated in APP transport because retromer deficiency leads to aberrant APP sorting and processing and levels of retromer proteins are altered in AD. Here we report that sorLA and retromer functionally interact in neurons to control trafficking and amyloidogenic processing of APP.
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