Lysozyme amyloidosis is an exceedingly rare hereditary autosomal dominant amyloidosis, which is characterized by the precipitation of lysozyme protein within the body, leading to multi-organ dysfunction. Herein, we present the case of a U.S. family affected by lysozyme amyloidosis. In particular, we report pericardial disease involvement leading to recurrent pericardial effusion, which to our knowledge has not been described yet. To our knowledge, we have also for the first time identified the amyloidogenic component of lysozyme amyloidosis via laser microdissection and mass spectrometry from a bone marrow biopsy. The diagnosis of this disease remains challenging as it can be easily mistaken for primary amyloidosis, which also presents with similar symptoms. Immunohistochemical staining of tissue for specific amyloidogenic proteins allows for an accurate diagnosis and should be performed in all amyloidosis patients in order to spare patients from potentially futile or harmful therapy. The widespread systemic involvement of lysozyme amyloidosis currently provides limited options for treatment, although kidney and/or liver transplantation appear to be promising palliative treatments. Practicing clinicians and researchers need to collect more information about this rare entity to further characterize the behavior of this disease and develop new potential treatment strategies.
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http://dx.doi.org/10.5414/CNCS108538 | DOI Listing |
Langmuir
January 2025
Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.
It is crucial to comprehend protein misfolding and aggregation in the domains of biomedicine, pharmaceuticals, and proteins. Amyloid fibrils are formed when proteins misfold and assemble, resulting in the debilitating illness known as "amyloidosis". This work investigates lysozyme fibrillation with pluronics (F68 and F127).
View Article and Find Full Text PDFSpectrochim Acta A Mol Biomol Spectrosc
February 2025
Department of Chemical Engineering and Biotechnology, Tatung University, Taipei 104, Taiwan. Electronic address:
There are currently over forty degenerative diseases that are correlated with abnormal accumulation of peptide/protein aggregates in the human body, such as Alzheimer's disease. Due to their unique physiochemical properties (e.g.
View Article and Find Full Text PDFNat Commun
November 2024
Institute of Protein Biochemistry, Ulm University, Ulm, Germany.
Systemic ALys amyloidosis is a debilitating protein misfolding disease that arises from the formation of amyloid fibrils from C-type lysozyme. We here present a 2.8 Å cryo-electron microscopy structure of an amyloid fibril, which was isolated from the abdominal fat tissue of a patient who expressed the D87G variant of human lysozyme.
View Article and Find Full Text PDFInt J Biol Macromol
November 2024
Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Sciences, 4 Tikhoretsky ave., 194064 St. Petersburg, Russia. Electronic address:
Biosensors (Basel)
August 2024
Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, Republic of Korea.
Quantifying the formation and decomposition of amyloid is a crucial issue in the development of new drugs and therapies for treating amyloidosis. The current technologies for grasping amyloid formation and decomposition include fluorescence analysis using thioflavin-T, secondary structure analysis using circular dichroism, and image analysis using atomic force microscopy or transmission electron microscopy. These technologies typically require spectroscopic devices or expensive nanoscale imaging equipment and involve lengthy analysis, which limits the rapid screening of amyloid-degrading drugs.
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