LAMP2 as a marker of EBV-mediated B lymphocyte transformation in the study of lysosomal storage diseases

Following the degradative pathway, vesicles loaded with extracellular material, eventually, dock and fuse with lysosomes, acquiring specific membrane markers of these organelles and acid hydrolases responsible for digest their content. The lysosomal-associated membrane protein 2 (LAMP-2), the best c...

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Bibliographic Details
Published in:	Molecular and cellular biochemistry Vol. 385; no. 1-2; pp. 1 - 6
Main Authors:	Mello, A. S., Goldim, M. P., Mezzalira, J., Garcia, C. S., Daitz, V. V., Castilhos, C. D., Viegas, M. S., Vieira, O. V., Coelho, J. C.
Format:	Journal Article
Language:	English
Published:	New York Springer US 2014 Springer Springer Nature B.V
Subjects:	alpha-Galactosidase - metabolism B cells B-Lymphocytes - metabolism B-Lymphocytes - pathology B-Lymphocytes - virology beta-Galactosidase - metabolism Biochemistry Biomarkers - metabolism Biomedical and Life Sciences Cardiology Cell Line, Transformed Enzymatic activity Enzymes Genetic markers Herpesvirus 4, Human - physiology Humans Hydrolases Hydrolases - metabolism Life Sciences Lymphocyte receptors Lymphocytes Lysosomal Storage Diseases - metabolism Lysosomal Storage Diseases - pathology Lysosomal Storage Diseases - virology Lysosomal-Associated Membrane Protein 2 - metabolism Lysosomes - enzymology Medical Biochemistry Medical research Medicine, Experimental Membranes Metabolic disorders Metabolism, Inborn errors of Microscopy, Confocal Neurosciences Oncology Physiological aspects Studies Brazil Pompe disease Inborn errors of metabolism Gaucher disease Lysosomal storage disorders Fabry disease Lymphocyte transformation Epstein–Barr virus
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Summary:	Following the degradative pathway, vesicles loaded with extracellular material, eventually, dock and fuse with lysosomes, acquiring specific membrane markers of these organelles and acid hydrolases responsible for digest their content. The lysosomal-associated membrane protein 2 (LAMP-2), the best characterized lysosomal membrane protein, is found in late stages of endosome maturation and may be used as a marker of lysosome-associated membranes. Lysosomal storage disorders (LSDs) are described by the absence or deficiency in hydrolase activity leading to substrate accumulation within lysosomal components and to the onset of several diseases. It is known that lymphocytes infected by Epstein–Barr virus (EBV) are able to form cytoplasmic vacuoles, which work as a storage compartment for lysosomal acidic hydrolases. At the present study, we validate the EBV as a transforming agent of B lymphocytes in stability studies of long-term stored samples, since the methods used to keep samples in liquid nitrogen and thaw them have all proven to be efficient in samples frozen for up to 2 years. To confirm and investigate some of the most prevalent LSDs in the South of Brazil—Pompe, Fabry and Gaucher diseases—we first measured the enzymatic activity of α-glicosidase, α-galactosidase, and β-glicosidase in those cytoplasmic-formed vacuoles and then looked to LAMP-2 immunoreactivity by employing confocal microscopy techniques.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0300-8177 1573-4919
DOI:	10.1007/s11010-013-1806-4