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@ARTICLE{Verma:163373,
author = {Verma, Shalja and Pantoom, Supansa and Petters, Janine and
Pandey, Anand Kumar and Hermann, Andreas and Lukas, Jan},
title = {{A} molecular genetics view on {M}ucopolysaccharidosis
{T}ype {II}.},
journal = {Mutation research / Reviews in mutation research},
volume = {788},
issn = {1383-5742},
address = {Amsterdam [u.a.]},
publisher = {Elsevier Science},
reportid = {DZNE-2022-00136},
pages = {108392},
year = {2021},
abstract = {Mucopolysaccharidosis Type II (MPS II) is an X-linked
recessive genetic disorder that primarily affects male
patients. With an incidence of 1 in 100,000 male live
births, the disease is one of the orphan diseases. MPS II
symptoms are caused by mutations in the lysosomal
iduronate-2-sulfatase (IDS) gene. The mutations cause a loss
of enzymatic performance and result in the accumulation of
glycosaminoglycans (GAGs), heparan sulfate and dermatan
sulfate, which are no longer degradable. This inadvertent
accumulation causes damage in multiple organs and leads
either to a severe neurological course or to an attenuated
course of the disease, although the exact relationship
between mutation, extent of GAG accumulation and disease
progression is not yet fully understood. This review is
intended to present current diagnostic procedures and
therapeutic interventions. In times when the genetic profile
of patients plays an increasingly important role in the
assessment of therapeutic success and future drug design, we
chose to further elucidate the impact of genetic diversity
within the IDS gene on disease phenotype and potential
implications in current diagnosis, prognosis and therapy. We
report recent advances in the structural biological
elucidation of I2S enzyme that that promises to improve our
future understanding of the molecular damage of the hundreds
of IDS gene variants and will aid damage prediction of novel
mutations in the future.},
subtyp = {Review Article},
keywords = {Animals / Glycoproteins: chemistry / Glycoproteins:
genetics / Glycoproteins: metabolism / Humans /
Mucopolysaccharidosis II: drug therapy /
Mucopolysaccharidosis II: genetics / Mucopolysaccharidosis
II: metabolism / Mutation / Phenotype / Genotype-phenotype
correlation (Other) / Hunter syndrome (Other) /
Iduronate-2-sulfatase (Other) / Individualized medicine
(Other) / Lysosomal storage disease (Other) / Missense
mutations (Other) / Glycoproteins (NLM Chemicals) / IDS
protein, human (NLM Chemicals)},
cin = {AG Teipel},
ddc = {570},
cid = {I:(DE-2719)1510100},
pnm = {353 - Clinical and Health Care Research (POF4-353)},
pid = {G:(DE-HGF)POF4-353},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:34893157},
doi = {10.1016/j.mrrev.2021.108392},
url = {https://pub.dzne.de/record/163373},
}