Identification of the iduronate-2-sulfatase proteome in wild-type mouse brain

Cardona, Carolina; Benincore, Eliana; Pimentel, Natalia; Reyes, Luis H.; Patarroyo, Camilo; Rodríguez-López, Alexander; Martín-Rufián, Mercedes; Barrera, Luis Alejandro; Alméciga-Díaz, Carlos J.

doi:10.1016/j.heliyon.2019.e01667

Cited by 9 publications

(17 citation statements)

References 80 publications

(88 reference statements)

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“…However, little or no overlap was observed when comparing the protein expression patterns of these two studies. Cardona et al [90] choose a functional approach when investigating the interactive proteome of IDS in mouse brain. Using a combination of affinity purification and mass spectrometry, they were able to identify 187 IDS-binding proteins in brain tissue extracts from C57BL/6 mice.…”

Section: Disease-specific Proteomicsmentioning

confidence: 99%

Differences in MPS I and MPS II Disease Manifestations

Hampe

Yund

Orchard

et al. 2021

IJMS

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Mucopolysaccharidosis (MPS) type I and II are two closely related lysosomal storage diseases associated with disrupted glycosaminoglycan catabolism. In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA). The subsequent accumulation of HS and DS causes lysosomal hypertrophy and an increase in the number of lysosomes in cells, and impacts cellular functions, like cell adhesion, endocytosis, intracellular trafficking of different molecules, intracellular ionic balance, and inflammation. Characteristic phenotypical manifestations of both MPS I and II include skeletal disease, reflected in short stature, inguinal and umbilical hernias, hydrocephalus, hearing loss, coarse facial features, protruded abdomen with hepatosplenomegaly, and neurological involvement with varying functional concerns. However, a few manifestations are disease-specific, including corneal clouding in MPS I, epidermal manifestations in MPS II, and differences in the severity and nature of behavioral concerns. These phenotypic differences appear to be related to different ratios between DS and HS, and their sulfation levels. MPS I is characterized by higher DS/HS levels and lower sulfation levels, while HS levels dominate over DS levels in MPS II and sulfation levels are higher. The high presence of DS in the cornea and its involvement in the arrangement of collagen fibrils potentially causes corneal clouding to be prevalent in MPS I, but not in MPS II. The differences in neurological involvement may be due to the increased HS levels in MPS II, because of the involvement of HS in neuronal development. Current treatment options for patients with MPS II are often restricted to enzyme replacement therapy (ERT). While ERT has beneficial effects on respiratory and cardiopulmonary function and extends the lifespan of the patients, it does not significantly affect CNS manifestations, probably because the enzyme cannot pass the blood–brain barrier at sufficient levels. Many experimental therapies, therefore, aim at delivery of IDS to the CNS in an attempt to prevent neurocognitive decline in the patients.

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Section: Disease-specific Proteomicsmentioning

confidence: 99%

Differences in MPS I and MPS II Disease Manifestations

Hampe

Yund

Orchard

et al. 2021

IJMS

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“…This gives an insight into the potential implications of IDS in cell growth, molecular adhesion, regulation of enzymatic activity, intracellular traffic, biogenesis of myelin, and glycolytic pathway on the CNS. These results may have a significant impact to the further understanding of the molecular and cellular basis of Hunter syndrome [70].…”

Section: Mucopolysaccharidosis Type II (Hunter Syndrome)mentioning

confidence: 89%

“…Cardona et al [70], demonstrated the distribution of IDS and its interactome in the brain of wild-type mice. This gives an insight into the potential implications of IDS in cell growth, molecular adhesion, regulation of enzymatic activity, intracellular traffic, biogenesis of myelin, and glycolytic pathway on the CNS.…”

Section: Mucopolysaccharidosis Type II (Hunter Syndrome)mentioning

confidence: 99%

A perspective on research, diagnosis, and management of lysosomal storage disorders in Colombia

Puentes-Tellez

Lerma-Barbosa

Garzón-Jaramillo

et al. 2020

Heliyon

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Lysosomal storage diseases (LSDs) are a group of about 50 inborn errors of metabolism characterized by the lysosomal accumulation of partially or non-degraded molecules due to mutations in proteins involved in the degradation of macromolecules, transport, lysosomal biogenesis or modulators of lysosomal environment. Significant advances have been achieved in the diagnosis, management, and treatment of LSDs patients. In terms of approved therapies, these include enzyme replacement therapy (ERT), substrate reduction therapy, hematopoietic stem cell transplantation, and pharmacological chaperone therapy. In this review, we summarize the Colombian experience in LSDs thorough the evidence published. We identified 113 articles published between 1995 and 2019 that included Colombian researchers or physicians, and which were mainly focused in Mucopolysaccharidoses, Pompe disease, Gaucher disease, Fabry disease, and Tay-Sachs and Sandhoff diseases. Most of these articles focused on basic research, clinical cases, and mutation reports. Noteworthy, implementation of the enzyme assay in dried blood samples, led to a 5-fold increase in the identification of LSD patients, suggesting that these disorders still remain undiagnosed in the country. We consider that the information presented in this review will contribute to the knowledge of a broad spectrum of LSDs in Colombia and will also contribute to the development of public policies and the identification of research opportunities.

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“…Various studies have suggested that pathogenetic IDS mutants are misfolded in the ER [13,36,37]. A previous study on an X-ray crystal structure of IDS revealed that several mutations, namely, L41P, L67P, L72P, L73F, L221P, L314P/H, L403R, and L410P, would introduce main-chain geometry distortion or buried steric clashes, disrupting the local secondary structure in the core of SD1 [13].…”

Section: Misfolding Of Ids Caused By Its Mutationmentioning

confidence: 99%

“…Meanwhile, biochemical and biological studies have also suggested the possibility of the unfolding of IDS mutants. Proteomic analysis of a mouse brain showed that IDS interacts with the ER-resident chaperone heat shock protein 90 [36]. Chaperone proteins bind tightly to unfolded proteins.…”

Section: Misfolding Of Ids Caused By Its Mutationmentioning

confidence: 99%

Loss of Function of Mutant IDS Due to Endoplasmic Reticulum-Associated Degradation: New Therapeutic Opportunities for Mucopolysaccharidosis Type II

Matsuhisa

Imaizumi

2021

IJMS

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Mucopolysaccharidosis type II (MPS II) results from the dysfunction of a lysosomal enzyme, iduronate-2-sulfatase (IDS). Dysfunction of IDS triggers the lysosomal accumulation of its substrates, glycosaminoglycans, leading to mental retardation and systemic symptoms including skeletal deformities and valvular heart disease. Most patients with severe types of MPS II die before the age of 20. The administration of recombinant IDS and transplantation of hematopoietic stem cells are performed as therapies for MPS II. However, these therapies either cannot improve functions of the central nervous system or cause severe side effects, respectively. To date, 729 pathogenetic variants in the IDS gene have been reported. Most of these potentially cause misfolding of the encoded IDS protein. The misfolded IDS mutants accumulate in the endoplasmic reticulum (ER), followed by degradation via ER-associated degradation (ERAD). Inhibition of the ERAD pathway or refolding of IDS mutants by a molecular chaperone enables recovery of the lysosomal localization and enzyme activity of IDS mutants. In this review, we explain the IDS structure and mechanism of activation, and current findings about the mechanism of degradation-dependent loss of function caused by pathogenetic IDS mutation. We also provide a potential therapeutic approach for MPS II based on this loss-of-function mechanism.

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Identification of the iduronate-2-sulfatase proteome in wild-type mouse brain

Cited by 9 publications

References 80 publications

Differences in MPS I and MPS II Disease Manifestations

Differences in MPS I and MPS II Disease Manifestations

A perspective on research, diagnosis, and management of lysosomal storage disorders in Colombia

Loss of Function of Mutant IDS Due to Endoplasmic Reticulum-Associated Degradation: New Therapeutic Opportunities for Mucopolysaccharidosis Type II

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