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Journal articles on the topic 'Lysosomal storage diseases'

Author: Grafiati

Published: 4 June 2021

Last updated: 30 July 2024

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1

Xu, Miao, Ke Liu, Manju Swaroop, Wei Sun, Seameen J. Dehdashti, John C. McKew, and Wei Zheng. "A Phenotypic Compound Screening Assay for Lysosomal Storage Diseases." Journal of Biomolecular Screening 19, no. 1 (August 27, 2013): 168–75. http://dx.doi.org/10.1177/1087057113501197.

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The lysosome is a vital cellular organelle that primarily functions as a recycling center for breaking down unwanted macromolecules through a series of hydrolases. Functional deficiencies in lysosomal proteins due to genetic mutations have been found in more than 50 lysosomal storage diseases that exhibit characteristic lipid/macromolecule accumulation and enlarged lysosomes. Recently, the lysosome has emerged as a new therapeutic target for drug development for the treatment of lysosomal storage diseases. However, a suitable assay for compound screening against the diseased lysosomes is currently unavailable. We have developed a Lysotracker staining assay that measures the enlarged lysosomes in patient-derived cells using both fluorescence intensity readout and fluorescence microscopic measurement. This phenotypic assay has been tested in patient cells obtained from several lysosomal storage diseases and validated using a known compound, methyl-β-cyclodextrin, in primary fibroblast cells derived from Niemann Pick C disease patients. The results demonstrate that the Lysotracker assay can be used in compound screening for the identification of lead compounds that are capable of reducing enlarged lysosomes for drug development.

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2

Schulze, M., S. Groeschel, J. Gburek-Augustat, T. Nägele, and M. Horger. "Lysosomal Storage Diseases – Lysosomale Speichererkrankungen." RöFo - Fortschritte auf dem Gebiet der Röntgenstrahlen und der bildgebenden Verfahren 187, no. 12 (November 26, 2015): 1057–60. http://dx.doi.org/10.1055/s-0035-1552368.

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3

Simonaro, Calogera M. "Lysosomes, Lysosomal Storage Diseases, and Inflammation." Journal of Inborn Errors of Metabolism and Screening 4 (May 14, 2016): 232640981665046. http://dx.doi.org/10.1177/2326409816650465.

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4

Breiden, Bernadette, and Konrad Sandhoff. "Lysosomal Glycosphingolipid Storage Diseases." Annual Review of Biochemistry 88, no. 1 (June 20, 2019): 461–85. http://dx.doi.org/10.1146/annurev-biochem-013118-111518.

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Glycosphingolipids are cell-type-specific components of the outer leaflet of mammalian plasma membranes. Gangliosides, sialic acid–containing glycosphingolipids, are especially enriched on neuronal surfaces. As amphi-philic molecules, they comprise a hydrophilic oligosaccharide chain attached to a hydrophobic membrane anchor, ceramide. Whereas glycosphingolipid formation is catalyzed by membrane-bound enzymes along the secretory pathway, degradation takes place at the surface of intralysosomal vesicles of late endosomes and lysosomes catalyzed in a stepwise fashion by soluble hydrolases and assisted by small lipid-binding glycoproteins. Inherited defects of lysosomal hydrolases or lipid-binding proteins cause the accumulation of undegradable material in lysosomal storage diseases (GM1 and GM2 gangliosidosis; Fabry, Gaucher, and Krabbe diseases; and metachromatic leukodystrophy). The catabolic processes are strongly modified by the lipid composition of the substrate-carrying membranes, and the pathological accumulation of primary storage compounds can trigger an accumulation of secondary storage compounds (e.g., small glycosphingolipids and cholesterol in Niemann-Pick disease).

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5

Gorbunova, Victoria N. "Congenital metabolic diseases. Lysosomal storage diseases." Pediatrician (St. Petersburg) 12, no. 2 (August 11, 2021): 73–83. http://dx.doi.org/10.17816/ped12273-83.

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The classification and epidemiology of hereditary metabolic disorders are presented. That is a large group consisting from more them 800 monogenic diseases, each of which caused by inherited deficiency of certain metabolic fate. Many of these disorders are extremely rare, but their total incidence in the population is close to 1:10005000. Lysosomal storage diseases (LSD) resulting from inherited deficiency in lysosomal functions occupy a special place among hereditary metabolic disorders. The defects of catabolism cause the accumulation of undigested or partially digested macromolecules in lysosomes (that is, storage), which can result in cellular damage. About 60 diseases take part in this group with total incidence of about 1:70008000. LSDs typically present in infancy and childhood, although adult-onset forms also occur. Most of them have a progressive neurodegenerative clinical course, although symptoms in other organ systems are frequent. The etiology and pathogenetic aspects of their main clinical entities: mucopolysaccharidosis, glycolipidosis, mucolipidosis, glycoproteinosis, etc, are presented. Mucopolysaccharidoses caused by malfunctioning of lysosomal enzymes needed to break down glycosaminoglycans are more frequent among LSD. Sphingolipidoses caused by defects of lipid catabolism are second for frequency group of LSD. The state-of-art in field of newborn screening. clinical, biochemical and molecular diagnostics of these grave diseases are discussed. The main directions of modern lysosomal storage diseases therapy are characterized: transplantation of hematopoietic stem cells; enzyme replacement therapy; therapy with limitation of substrate synthesis (substrate-reducing therapy); pharmacological chaperone therapy. Perspective directions for LSD therapy are gene therapy and genome editing which are at advanced preclinical stages.

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6

Ferreira, Carlos R., and William A. Gahl. "Lysosomal storage diseases." Translational Science of Rare Diseases 2, no. 1-2 (May 25, 2017): 1–71. http://dx.doi.org/10.3233/trd-160005.

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7

Rose Georgy, Smitha. "Lysosomal storage diseases." Journal of Veterinary and Animal Sciences 52, no. 1 (January 1, 2021): 1–6. http://dx.doi.org/10.51966/jvas.2021.52.1.1-6.

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8

Neufeld, Elizabeth F. "Lysosomal Storage Diseases." Annual Review of Biochemistry 60, no. 1 (June 1991): 257–80. http://dx.doi.org/10.1146/annurev.bi.60.070191.001353.

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9

Alroy, Joseph, and Jeremiah A. Lyons. "Lysosomal Storage Diseases." Journal of Inborn Errors of Metabolism and Screening 2 (March 7, 2014): 232640981351766. http://dx.doi.org/10.1177/2326409813517663.

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10

Richtsfeld, Martina, and Kumar G. Belani. "Lysosomal Storage Diseases." Anesthesia & Analgesia 125, no. 3 (September 2017): 716–18. http://dx.doi.org/10.1213/ane.0000000000001887.

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11

Gieselmann, Volkmar. "Lysosomal storage diseases." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1270, no. 2-3 (April 1995): 103–36. http://dx.doi.org/10.1016/0925-4439(94)00075-2.

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12

Kaye, Edward M. "Lysosomal storage diseases." Current Treatment Options in Neurology 3, no. 3 (May 2001): 249–56. http://dx.doi.org/10.1007/s11940-001-0006-9.

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13

Onyenwoke, Rob U., and Jay E. Brenman. "Lysosomal Storage Diseases-Regulating Neurodegeneration." Journal of Experimental Neuroscience 9s2 (January 2015): JEN.S25475. http://dx.doi.org/10.4137/jen.s25475.

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Autophagy is a complex pathway regulated by numerous signaling events that recycles macromolecules and can be perturbed in lysosomal storage diseases (LSDs). The concept of LSDs, which are characterized by aberrant, excessive storage of cellular material in lysosomes, developed following the discovery of an enzyme deficiency as the cause of Pompe disease in 1963. Great strides have since been made in better understanding the biology of LSDs. Defective lysosomal storage typically occurs in many cell types, but the nervous system, including the central nervous system and peripheral nervous system, is particularly vulnerable to LSDs, being affected in two-thirds of LSDs. This review provides a summary of some of the better characterized LSDs and the pathways affected in these disorders.

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14

Zeng, Wenping, Canjun Li, Ruikun Wu, Xingguo Yang, Qingyan Wang, Bingqian Lin, Yanan Wei, et al. "Optogenetic manipulation of lysosomal physiology and autophagy-dependent clearance of amyloid beta." PLOS Biology 22, no. 4 (April 23, 2024): e3002591. http://dx.doi.org/10.1371/journal.pbio.3002591.

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Lysosomes are degradation centers of cells and intracellular hubs of signal transduction, nutrient sensing, and autophagy regulation. Dysfunction of lysosomes contributes to a variety of diseases, such as lysosomal storage diseases (LSDs) and neurodegeneration, but the mechanisms are not well understood. Altering lysosomal activity and examining its impact on the occurrence and development of disease is an important strategy for studying lysosome-related diseases. However, methods to dynamically regulate lysosomal function in living cells or animals are still lacking. Here, we constructed lysosome-localized optogenetic actuators, named lyso-NpHR3.0, lyso-ArchT, and lyso-ChR2, to achieve optogenetic manipulation of lysosomes. These new actuators enable light-dependent control of lysosomal membrane potential, pH, hydrolase activity, degradation, and Ca2+ dynamics in living cells. Notably, lyso-ChR2 activation induces autophagy through the mTOR pathway, promotes Aβ clearance in an autophagy-dependent manner in cellular models, and alleviates Aβ-induced paralysis in the Caenorhabditis elegans model of Alzheimer’s disease. Our lysosomal optogenetic actuators supplement the optogenetic toolbox and provide a method to dynamically regulate lysosomal physiology and function in living cells and animals.

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15

Vogler, Carole, and Harvey S. Rosenberg. "Electron Microscopy in the diagnosis of lysosomal storage diseases." Proceedings, annual meeting, Electron Microscopy Society of America 47 (August 6, 1989): 866–67. http://dx.doi.org/10.1017/s0424820100156316.

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Diagnostic procedures for evaluation of patients with lysosomal storage diseases (LSD) seek to identify a deficiency of a responsible lysosomal enzyme or accumulation of a substance that requires the missing enzyme for degradation. Most patients with LSD have progressive neurological degeneration and may have a variety of musculoskeletal and visceral abnormalities. In the LSD, the abnormally diminished lysosomal enzyme results in accumulation of unmetabolized catabolites in distended lysosomes. Because of the subcellular morphology and size of lysosomes, electron microscopy is an ideal tool to study tissue from patients with suspected LSD. In patients with LSD all cells lack the specific lysosomal enzyme but the distribution of storage material is dependent on the extent of catabolism of the substrate in each cell type under normal circumstances. Lysosmal storages diseases affect many cell types and tissues. Storage material though does not accumulate in all tissues and cell types and may be different biochemically and morphologically in different tissues.Conjunctiva, skin, rectal mucosa and peripheral blood leukocytes may show ultrastructural evidence of lysosomal storage even in the absence of clinical findings and thus any of these tissues can be used for ultrastructural examination in the diagnostic evaluation of patients with suspected LSD. Biopsy of skin and conjunctiva are easily obtained and provide multiple cell types including endothelium, epithelium, fibroblasts and nerves for ultrastructural study. Fibroblasts from skin and conjunctiva can also be utilized for the initiation of tissue cultures for chemical assays. Brain biopsy has been largely replaced by biopsy of more readily obtained tissue and by biochemical assays. Such assays though may give equivical or nondiagnostic results and in some lysosomal storage diseases an enzyme defect has not yet been identified and diagnoses can be made only by ultrastructural examination.

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16

Heard, Jean Michel, Julie Bruyère, Elise Roy, Stéphanie Bigou, Jérôme Ausseil, and Sandrine Vitry. "Storage problems in lysosomal diseases." Biochemical Society Transactions 38, no. 6 (November 24, 2010): 1442–47. http://dx.doi.org/10.1042/bst0381442.

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Biochemical disorders in lysosomal storage diseases consist of the interruption of metabolic pathways involved in the recycling of the degradation products of one or several types of macromolecules. The progressive accumulation of these primary storage products is the direct consequence of the genetic defect and represents the initial pathogenic event. Downstream consequences for the affected cells include the accumulation of secondary storage products and the formation of histological storage lesions, which appear as intracellular vacuoles that represent the pathological hallmark of lysosomal storage diseases. Relationships between storage products and storage lesions are not simple and are still largely not understood. Primary storage products induce malfunction of the organelles where they accumulate, these being primarily, but not only, lysosomes. Consequences for cell metabolism and intracellular trafficking combine the effects of primary storage product toxicity and the compensatory mechanisms activated to protect the cell. Induced disorders extend far beyond the primarily interrupted metabolic pathway.

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17

Platt, Frances M., Barry Boland, and Aarnoud C. van der Spoel. "Lysosomal storage disorders: The cellular impact of lysosomal dysfunction." Journal of Cell Biology 199, no. 5 (November 26, 2012): 723–34. http://dx.doi.org/10.1083/jcb.201208152.

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Lysosomal storage diseases (LSDs) are a family of disorders that result from inherited gene mutations that perturb lysosomal homeostasis. LSDs mainly stem from deficiencies in lysosomal enzymes, but also in some non-enzymatic lysosomal proteins, which lead to abnormal storage of macromolecular substrates. Valuable insights into lysosome functions have emerged from research into these diseases. In addition to primary lysosomal dysfunction, cellular pathways associated with other membrane-bound organelles are perturbed in these disorders. Through selective examples, we illustrate why the term “cellular storage disorders” may be a more appropriate description of these diseases and discuss therapies that can alleviate storage and restore normal cellular function.

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18

Schulze, H., and K. Sandhoff. "Lysosomal Lipid Storage Diseases." Cold Spring Harbor Perspectives in Biology 3, no. 6 (April 18, 2011): a004804. http://dx.doi.org/10.1101/cshperspect.a004804.

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19

Schultz, Mark L., Luis Tecedor, Michael Chang, and Beverly L. Davidson. "Clarifying lysosomal storage diseases." Trends in Neurosciences 34, no. 8 (August 2011): 401–10. http://dx.doi.org/10.1016/j.tins.2011.05.006.

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20

Martina, José A., Nina Raben, and Rosa Puertollano. "SnapShot: Lysosomal Storage Diseases." Cell 180, no. 3 (February 2020): 602–602. http://dx.doi.org/10.1016/j.cell.2020.01.017.

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21

Werber, Yaron. "Lysosomal storage diseases market." Nature Reviews Drug Discovery 3, no. 1 (January 2004): 9–10. http://dx.doi.org/10.1038/nrd1286.

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22

Morand, Olivier, and Hélène Peyro-Saint-Paul. "Lysosomal storage diseases market." Nature Reviews Drug Discovery 3, no. 1 (January 2004): 98. http://dx.doi.org/10.1038/nrd1286-c2.

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23

Maegawa, Gustavo H. B. "Lysosomal Leukodystrophies Lysosomal Storage Diseases Associated With White Matter Abnormalities." Journal of Child Neurology 34, no. 6 (February 13, 2019): 339–58. http://dx.doi.org/10.1177/0883073819828587.

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The leukodystrophies are a group of genetic metabolic diseases characterized by an abnormal development or progressive degeneration of the myelin sheath. The myelin is a complex sheath composed of several macromolecules covering axons as an insulator. Each of the leukodystrophies is caused by mutations in genes encoding enzymes that are involved in myelin production and maintenance. The lysosomal storage diseases are inborn disorders of compartmentalized cellular organelles with broad clinical manifestations secondary to the progressive accumulation of undegraded macromolecules within lysosomes and related organelles. The more than 60 different lysosomal storage diseases are rare diseases; however, collectively, the incidence of lysosomal storage diseases ranges just over 1 in 2500 live births. The majority of lysosomal storage diseases are associated with neurologic manifestations including developmental delay, seizures, acroparesthesia, motor weakness, and extrapyramidal signs. These inborn organelle disorders show wide clinical variability affecting individuals from all age groups. In addition, several of neurologic, also known as neuronopathic, lysosomal storage diseases are associated with some level of white matter disease, which often triggers the diagnostic investigation. Most lysosomal storage diseases are autosomal recessively inherited and few are X-linked, with females being at risk of presenting with mild, but clinically relevant neurologic manifestations. Biochemical assays are the basis of the diagnosis and are usually confirmed by molecular genetic testing. Novel therapies have emerged. However, most affected patients with lysosomal storage diseases have only supportive management to rely on. A better understanding of the mechanisms resulting in the leukodystrophy will certainly result in innovative and efficacious disease-modifying therapies.

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24

Winchester, B., A. Vellodi, and E. Young. "The molecular basis of lysosomal storage diseases and their treatment." Biochemical Society Transactions 28, no. 2 (February 1, 2000): 150–54. http://dx.doi.org/10.1042/bst0280150.

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The lysosomal system is the main intracellular mechanism for the catabolism of naturally occurring endogenous and exogenous macromolecules and the subsequent recycling of their constituent monomeric components. It also plays an important part in processing essential metabolites. A genetic defect in a protein responsible for maintaining the lysosomal system results in the accumulation within lysosomes of partially degraded molecules, the initial step in the process leading to a lysosomal storage disease. The defective protein can be a luminal lysosomal enzyme or protein cofactor, a lysosomal membrane protein or a protein involved in the post-translational modification or transport of lysosomal proteins. Over 40 lysosomal storage diseases are known and they have a collective incidence of ≈ 1 in 7000–8000 live births. Most of the genes for the lysosomal proteins have been cloned, permitting mutation analysis in individual cases. This information can be used for genotype/phenotype correlation, genetic counselling and the selection of patients for novel forms of therapy, such as substrate deprivation or dispersal, enzyme replacement, bone-marrow transplantation and gene transfer.

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25

De Pasquale, Valeria, Melania Scarcella, and Luigi Michele Pavone. "Molecular Mechanisms in Lysosomal Storage Diseases: From Pathogenesis to Therapeutic Strategies." Biomedicines 10, no. 4 (April 17, 2022): 922. http://dx.doi.org/10.3390/biomedicines10040922.

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26

Seranova, Elena, Kyle J. Connolly, Malgorzata Zatyka, Tatiana R. Rosenstock, Timothy Barrett, Richard I. Tuxworth, and Sovan Sarkar. "Dysregulation of autophagy as a common mechanism in lysosomal storage diseases." Essays in Biochemistry 61, no. 6 (December 12, 2017): 733–49. http://dx.doi.org/10.1042/ebc20170055.

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The lysosome plays a pivotal role between catabolic and anabolic processes as the nexus for signalling pathways responsive to a variety of factors, such as growth, nutrient availability, energetic status and cellular stressors. Lysosomes are also the terminal degradative organelles for autophagy through which macromolecules and damaged cellular components and organelles are degraded. Autophagy acts as a cellular homeostatic pathway that is essential for organismal physiology. Decline in autophagy during ageing or in many diseases, including late-onset forms of neurodegeneration is considered a major contributing factor to the pathology. Multiple lines of evidence indicate that impairment in autophagy is also a central mechanism underlying several lysosomal storage disorders (LSDs). LSDs are a class of rare, inherited disorders whose histopathological hallmark is the accumulation of undegraded materials in the lysosomes due to abnormal lysosomal function. Inefficient degradative capability of the lysosomes has negative impact on the flux through the autophagic pathway, and therefore dysregulated autophagy in LSDs is emerging as a relevant disease mechanism. Pathology in the LSDs is generally early-onset, severe and life-limiting but current therapies are limited or absent; recognizing common autophagy defects in the LSDs raises new possibilities for therapy. In this review, we describe the mechanisms by which LSDs occur, focusing on perturbations in the autophagy pathway and present the latest data supporting the development of novel therapeutic approaches related to the modulation of autophagy.

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27

Tikkanen, Ritva. "A Journey towards Understanding the Molecular Pathology and Developing Therapies for Lysosomal Storage Disorders." Cells 11, no. 1 (December 23, 2021): 36. http://dx.doi.org/10.3390/cells11010036.

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28

Gorbunova, Viktoria N., Natalia V. Buchinskaia, Lidia V. Liazina, and Anastasia O. Vechkasova. "Lysosomal storage diseases. Sphingolipidoses — gangliosidoses." Pediatrician (St. Petersburg) 14, no. 4 (November 23, 2023): 93–111. http://dx.doi.org/10.17816/ped14493-111.

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Epidemiology, clinical, biochemical and molecular genetic characteristics of gangliosidoses, genetically heterogeneous group of autosomal recessive diseases caused by hereditary deficiency of lysosomal glycohydrolases involved in the catabolism of GM1-, GM2- and GA2-gangliosides, are presented. Three clinical forms of GM1 gangliosidosis are caused by hereditary deficiency of lysosomal β-galactosidase, one of the activities of which is the release of galactose from carbohydrate complexes. As a result, GM1-ganglioside and, to a lesser extent, keratan sulfate accumulate in the lysosomes of neurons and other cells. Three genetically heterogeneous forms of GM2-gangliosidosis are associated with dysfunction of hexosaminidase activity. Tay–Sachs disease, or GM2 ganglioside variant B, is caused by mutations in the hexosaminidase alpha chain HEXA gene. Sandhoff’s disease is associated with mutations in the HEXB gene for the hexosaminidase beta chain. In this case, there is a deficiency of the A and B components of the enzyme — the null variant of GM2 gangliosidosis. In variant AB, or juvenile GM2 gangliosidosis, all hexosaminidase components are present, but the activating factor is defective due to mutations in the GM2A gene. All types of gangliosidosis are characterized by progressive retardation of psychomotor development and early death of patients, most often under the age of 3 years. The frequency of various types of gangliosidoses in different populations does not exceed 1 : 300,000. An exception is the ethic group of Ashkenazi Jews, in which the incidence of Tay–Sachs disease, reaches 1 : 3000, which makes total screening of heterozygotes and prenatal diagnosis of the disease in high-risk families economically justified. The article highlights the importance of experimental models for studying the molecular basis of pathogenesis and developing various therapeutic approaches, such as bone marrow transplantation, enzyme replacement therapy and substrate reducing therapy, gene therapy, and genome editing. Clinical examples of patients with gangliosidosis are given to improve the efficiency of diagnostics of these rare diseases by clinicians.

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29

Bobillo Lobato, Joaquin, Maria Jiménez Hidalgo, and Luis Jiménez Jiménez. "Biomarkers in Lysosomal Storage Diseases." Diseases 4, no. 4 (December 17, 2016): 40. http://dx.doi.org/10.3390/diseases4040040.

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30

Scarpa, Maurizio, and Yoshikatsu Eto. "Lysosomal storage diseases: new challenges." Acta Paediatrica 97, s457 (April 2008): 5–6. http://dx.doi.org/10.1111/j.1651-2227.2008.00645.x.

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31

Rapola, J. "Lysosomal Storage Diseases in Adults." Pathology - Research and Practice 190, no. 8 (September 1994): 759–66. http://dx.doi.org/10.1016/s0344-0338(11)80422-x.

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32

Rama Rao, K. V., and T. Kielian. "Astrocytes and lysosomal storage diseases." Neuroscience 323 (May 2016): 195–206. http://dx.doi.org/10.1016/j.neuroscience.2015.05.061.

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33

Jolly, Robert D. "Lysosomal Storage Diseases in Livestock." Veterinary Clinics of North America: Food Animal Practice 9, no. 1 (March 1993): 41–53. http://dx.doi.org/10.1016/s0749-0720(15)30670-8.

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34

Gorbunova, Victoria N., Natalia V. Buchinskaia, Anastasia O. Vechkasova, and Varvara S. Kruglova. "Lysosomal storage diseases. Sphingolipidoses – leukodystrophy." Pediatrician (St. Petersburg) 14, no. 6 (May 7, 2024): 89–112. http://dx.doi.org/10.17816/ped626382.

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Epidemiological, clinical, biochemical and molecular-genetic characteristics of lysosomal leukodystrophies are presented, which include metachromatic leukodystrophy, globoid cell leukodystrophy, or Krabbe disease, combined saposin and multiple sulfatase deficiency. The pathogenesis of metachromatic and globoid cell leukodystrophy is based on hereditary deficiency of two lysosomal enzymes — arylsulfatase A and galactocerebrosidase, accompanied by excessive accumulation of galactosphingosulfatides and galactosylceramide, respectively. The consequence of this is demyelination of the central and peripheral nervous system and damage to the white matter of the brain. Experimental models show effectiveness of pathogenetic approaches, such as hematopoietic stem cell transplantation and gene therapy, only if treatment is started before the development of severe neurological anomalies. In this regard, neonatal screening methods for these two forms of leukodystrophy are being developed, which have been particularly successful in the early diagnosis of Krabbe disease. For each of the two leukodystrophies (metachromatic and globoid cell), rare genetic variants have been described due to the absence of activator proteins for arylsulfatase A and galactocerebrosidase (saposins B and C), respectively, due to specific mutations in the gene of the precursor of saposins, prosaposin (PSPA). Mutations in the PSPA gene resulting in the absence of all four saposins (A, D, C and D) are the cause of combined saposin deficiency, characterized by the development of severe neurological disorders soon after birth and death before the age of 1 year. The pathogenesis of multiple sulfatase deficiency is based on the accumulation of sulfatides, sulfated glycosaminoglycans, sphingolipids, and steroid sulfates, caused by inactivating mutations in the SUMF1 gene of the sulfatase-modifying factor 1 involved in the biosynthesis of all sulfatases. The disease is characterized by a combined manifestation of metachromatic leukodystrophy and mucopolysaccharidosis in combination with severe neurological disorders, mental retardation, sensorineural hearing loss and ichthyosis. Clinical guidelines for the diagnosis, management and therapy of combined saposin and multiple sulfatase deficiency have not yet been developed. The article presents a description of a clinical case of Krabbe disease in a child observed in the medical genetic center of St. Petersburg.

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35

Fernández-Pereira, Carlos, Beatriz San Millán-Tejado, María Gallardo-Gómez, Tania Pérez-Márquez, Marta Alves-Villar, Cristina Melcón-Crespo, Julián Fernández-Martín, and Saida Ortolano. "Therapeutic Approaches in Lysosomal Storage Diseases." Biomolecules 11, no. 12 (November 26, 2021): 1775. http://dx.doi.org/10.3390/biom11121775.

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Lysosomal Storage Diseases are multisystemic disorders determined by genetic variants, which affect the proteins involved in lysosomal function and cellular metabolism. Different therapeutic approaches, which are based on the physiologic mechanisms that regulate lysosomal function, have been proposed for these diseases. Currently, enzyme replacement therapy, gene therapy, or small molecules have been approved or are under clinical development to treat lysosomal storage disorders. The present article reviews the main therapeutic strategies that have been proposed so far, highlighting possible limitations and future perspectives.

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36

Gorbunova, V. N., and N. V. Buchinskaya. "Lysosomal storage diseases. Mucopolysaccharidosis type III, sanfilippo syndrome." Pediatrician (St. Petersburg) 12, no. 4 (December 13, 2021): 69–81. http://dx.doi.org/10.17816/ped12469-81.

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The review describes the clinical, biochemical and molecular genetic characteristics of autosomal recessive mucopolysaccharidosis type III, or Sanfilippo syndrome. This is a genetically heterogeneous group of rare, but similar in nature, diseases caused by a deficiency of one of the four lysosomal enzymes involved in the degradation of heparan sulfate. All types of mucopolysaccharidosis III are characterized by severe degeneration of the central nervous system in combination with mild somatic manifestations, which is explained by the accumulation of high concentrations of heparan sulfate in the lysosomes of various cells, including the central nervous system. The primary biochemical defect in the most common type of mucopolysaccharidosis IIIA, occurring with a frequency of 1 : 105 and presented in 60% of all cases of the disease, is heparan-N-sulfatase, or sulfamidase deficiency. Mucopolysaccharidosis IIIB type occurs twice less often and accounts for about 30% of all cases of Sanfilippo syndrome. It is caused by the presence of inactivating mutations in the lysosomal -N-acetylglucosaminidase gene. Mucopolysaccharidosis IIIC and IIID are 4% and 6%, and occur at frequencies of 0.7 and 1.0 : 106. Mucopolysaccharidosis IIIC is caused by inactivating mutations in the gene of membrane-bound lysosomal acetyl-CoA:-glucosaminid-N-acetyltransferase, or N-acetyltransferase. Mucopolysaccharidosis IIID is based on the deficiency of lysosomal N-acetylglucosamine-6-sulfatase. The role of experimental models in the study of the biochemical basis of the pathogenesis of Sanfilippo syndrome and the development of various therapeutic approaches are discussed. The possibility of neonatal screening, early diagnosis, prevention and pathogenetic therapy of these severe lysosomal diseases are considered. As an example, a clinical case of diagnosis and treatment of a child with type IIIB mucopolysaccharidosis is presented.

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37

van Eijk, Marco, Maria J. Ferraz, Rolf G. Boot, and Johannes M. F. G. Aerts. "Lyso-glycosphingolipids: presence and consequences." Essays in Biochemistry 64, no. 3 (August 18, 2020): 565–78. http://dx.doi.org/10.1042/ebc20190090.

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Abstract Lyso-glycosphingolipids are generated in excess in glycosphingolipid storage disorders. In the course of these pathologies glycosylated sphingolipid species accumulate within lysosomes due to flaws in the respective lipid degrading machinery. Deacylation of accumulating glycosphingolipids drives the formation of lyso-glycosphingolipids. In lysosomal storage diseases such as Gaucher Disease, Fabry Disease, Krabbe disease, GM1 -and GM2 gangliosidosis, Niemann Pick type C and Metachromatic leukodystrophy massive intra-lysosomal glycosphingolipid accumulation occurs. The lysosomal enzyme acid ceramidase generates the deacylated lyso-glycosphingolipid species. This review discusses how the various lyso-glycosphingolipids are synthesized, how they may contribute to abnormal immunity in glycosphingolipid storing lysosomal diseases and what therapeutic opportunities exist.

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Jolly, R. D., and S. U. Walkley. "Lysosomal Storage Diseases of Animals: An Essay in Comparative Pathology." Veterinary Pathology 34, no. 6 (November 1997): 527–48. http://dx.doi.org/10.1177/030098589703400601.

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A wide variety of inherited lysosomal hydrolase deficiencies have been reported in animals and are characterized by accumulation of sphingolipids, glycolipids, oligosaccharides, or mucopolysaccharides within lysosomes. Inhibitors of a lysosomal hydrolase, e.g., swainsonine, may also induce storage disease. Another group of lysosomal storage diseases, the ceroid-lipofuscinoses, involve the accumulation of hydrophobic proteins, but their pathogenesis is unclear. Some of these diseases are of veterinary importance, and those caused by a hydrolase deficiency can be controlled by detection of heterozygotes through the gene dosage phenomenon or by molecular genetic techniques. Other of these diseases are important to biomedical research either as models of the analogous human disease and/or through their ability to help elucidate specific aspects of cell biology. Some of these models have been used to explore possible therapeutic strategies and to define their limitations and expectations.

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Ivanova, Margarita. "Altered Sphingolipids Metabolism Damaged Mitochondrial Functions: Lessons Learned From Gaucher and Fabry Diseases." Journal of Clinical Medicine 9, no. 4 (April 14, 2020): 1116. http://dx.doi.org/10.3390/jcm9041116.

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Sphingolipids represent a class of bioactive lipids that modulate the biophysical properties of biological membranes and play a critical role in cell signal transduction. Multiple studies have demonstrated that sphingolipids control crucial cellular functions such as the cell cycle, senescence, autophagy, apoptosis, cell migration, and inflammation. Sphingolipid metabolism is highly compartmentalized within the subcellular locations. However, the majority of steps of sphingolipids metabolism occur in lysosomes. Altered sphingolipid metabolism with an accumulation of undigested substrates in lysosomes due to lysosomal enzyme deficiency is linked to lysosomal storage disorders (LSD). Trapping of sphingolipids and their metabolites in the lysosomes inhibits lipid recycling, which has a direct effect on the lipid composition of cellular membranes, including the inner mitochondrial membrane. Additionally, lysosomes are not only the house of digestive enzymes, but are also responsible for trafficking organelles, sensing nutrients, and repairing mitochondria. However, lysosomal abnormalities lead to alteration of autophagy and disturb the energy balance and mitochondrial function. In this review, an overview of mitochondrial function in cells with altered sphingolipid metabolism will be discussed focusing on the two most common sphingolipid disorders, Gaucher and Fabry diseases. The review highlights the status of mitochondrial energy metabolism and the regulation of mitochondria–autophagy–lysosome crosstalk.

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Blumenreich, Shani, Or B. Barav, Bethan J. Jenkins, and Anthony H. Futerman. "Lysosomal Storage Disorders Shed Light on Lysosomal Dysfunction in Parkinson’s Disease." International Journal of Molecular Sciences 21, no. 14 (July 14, 2020): 4966. http://dx.doi.org/10.3390/ijms21144966.

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The lysosome is a central player in the cell, acting as a clearing house for macromolecular degradation, but also plays a critical role in a variety of additional metabolic and regulatory processes. The lysosome has recently attracted the attention of neurobiologists and neurologists since a number of neurological diseases involve a lysosomal component. Among these is Parkinson’s disease (PD). While heterozygous and homozygous mutations in GBA1 are the highest genetic risk factor for PD, studies performed over the past decade have suggested that lysosomal loss of function is likely involved in PD pathology, since a significant percent of PD patients have a mutation in one or more genes that cause a lysosomal storage disease (LSD). Although the mechanistic connection between the lysosome and PD remains somewhat enigmatic, significant evidence is accumulating that lysosomal dysfunction plays a central role in PD pathophysiology. Thus, lysosomal dysfunction, resulting from mutations in lysosomal genes, may enhance the accumulation of α-synuclein in the brain, which may result in the earlier development of PD.

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Gieselmann, Volkmar, Ulrich Matzner, Diana Klein, Jan Eric Mansson, Rudi D'Hooge, Peter D. DeDeyn, Renate Lüllmann Rauch, Dieter Hartmann, and Klaus Harzer. "Gene therapy: prospects for glycolipid storage diseases." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 358, no. 1433 (May 29, 2003): 921–25. http://dx.doi.org/10.1098/rstb.2003.1277.

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Lysosomal storage diseases comprise a group of about 40 disorders, which in most cases are due to the deficiency of a lysosomal enzyme. Since lysosomal enzymes are involved in the degradation of various compounds, the diseases can be further subdivided according to which pathway is affected. Thus, enzyme deficiencies in the degradation pathway of glycosaminoglycans cause mucopolysaccharidosis, and deficiencies affecting glycopeptides cause glycoproteinosis. In glycolipid storage diseases enzymes are deficient that are involved in the degradation of sphingolipids. Mouse models are available for most of these diseases, and some of these mouse models have been used to study the applicability of in vivo gene therapy. We review the rationale for gene therapy in lysosomal disorders and present data, in particular, about trials in an animal model of metachromatic leukodystrophy. The data of these trials are compared with those obtained with animal models of other lysosomal diseases.

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Pandey, Manoj Kumar. "Exploring Pro-Inflammatory Immunological Mediators: Unraveling the Mechanisms of Neuroinflammation in Lysosomal Storage Diseases." Biomedicines 11, no. 4 (April 1, 2023): 1067. http://dx.doi.org/10.3390/biomedicines11041067.

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Lysosomal storage diseases are a group of rare and ultra-rare genetic disorders caused by defects in specific genes that result in the accumulation of toxic substances in the lysosome. This excess accumulation of such cellular materials stimulates the activation of immune and neurological cells, leading to neuroinflammation and neurodegeneration in the central and peripheral nervous systems. Examples of lysosomal storage diseases include Gaucher, Fabry, Tay–Sachs, Sandhoff, and Wolman diseases. These diseases are characterized by the accumulation of various substrates, such as glucosylceramide, globotriaosylceramide, ganglioside GM2, sphingomyelin, ceramide, and triglycerides, in the affected cells. The resulting pro-inflammatory environment leads to the generation of pro-inflammatory cytokines, chemokines, growth factors, and several components of complement cascades, which contribute to the progressive neurodegeneration seen in these diseases. In this study, we provide an overview of the genetic defects associated with lysosomal storage diseases and their impact on the induction of neuro-immune inflammation. By understanding the underlying mechanisms behind these diseases, we aim to provide new insights into potential biomarkers and therapeutic targets for monitoring and managing the severity of these diseases. In conclusion, lysosomal storage diseases present a complex challenge for patients and clinicians, but this study offers a comprehensive overview of the impact of these diseases on the central and peripheral nervous systems and provides a foundation for further research into potential treatments.

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Gabig-Cimińska, M., J. Jakóbkiewicz-Banecka, M. Malinowska, A. Kloska, E. Piotrowska, I. Chmielarz, M. Moskot, A. Węgrzyn, and G. Węgrzyn. "Combined Therapies for Lysosomal Storage Diseases." Current Molecular Medicine 15, no. 8 (October 6, 2015): 746–71. http://dx.doi.org/10.2174/1566524015666150921105658.

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Dawson, Glyn, Karl Johnson, Norah R. McCabe, and Larry W. Hancock. "Molecular heterogeneity in lysosomal storage diseases." Neurochemical Pathology 8, no. 3 (June 1988): 203–17. http://dx.doi.org/10.1007/bf03160147.

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Mononen, I. "Laboratory Diagnostics of Lysosomal Storage Diseases." Scandinavian Journal of Clinical and Laboratory Investigation 48 (1988): 81–82. http://dx.doi.org/10.3109/00365518809168517.

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Boudes, Pol F. "Clinical studies in lysosomal storage diseases." Rare Diseases 1, no. 1 (January 2013): e26690. http://dx.doi.org/10.4161/rdis.26690.

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Gelb, Michael H., C. Ronald Scott, and Frantisek Turecek. "Newborn Screening for Lysosomal Storage Diseases." Clinical Chemistry 61, no. 2 (February 1, 2015): 335–46. http://dx.doi.org/10.1373/clinchem.2014.225771.

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Abstract BACKGROUND There is worldwide interest in newborn screening for lysosomal storage diseases because of the development of treatment options that give better results when carried out early in life. Screens with high differentiation between affected and nonaffected individuals are critical because of the large number of potential false positives. CONTENT This review summarizes 3 screening methods: (a) direct assay of enzymatic activities using tandem mass spectrometry or fluorometry, (b) immunocapture-based measurement of lysosomal enzyme abundance, and (c) measurement of biomarkers. Assay performance is compared on the basis of small-scale studies as well as on large-scale pilot studies of mass spectrometric and fluorometric screens. SUMMARY Tandem mass spectrometry and fluorometry techniques for direct assay of lysosomal enzymatic activity in dried blood spots have emerged as the most studied approaches. Comparative mass spectrometry vs fluorometry studies show that the former better differentiates between nonaffected vs affected individuals. This in turn leads to a manageable number of screen positives that can be further evaluated with second-tier methods.

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Alroy, J. "Secondary changes in lysosomal storage diseases." Acta Paediatrica 91 (January 2, 2007): 149. http://dx.doi.org/10.1111/j.1651-2227.2002.tb03181.x.

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KOLODNY, EDWIN H. "Early Detection of Lysosomal Storage Diseases." Annals of the New York Academy of Sciences 477, no. 1 Mental Retard (December 1986): 312–20. http://dx.doi.org/10.1111/j.1749-6632.1986.tb40350.x.

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Mononen, I. "Laboratory Diagnostics of Lysosomal Storage Diseases." Scandinavian Journal of Clinical and Laboratory Investigation 48, sup190 (January 1988): 81–82. http://dx.doi.org/10.1080/00365518809168517.

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