Results 51 to 60 of about 2,842 (215)

A rare case of severe Hunter's Syndrome

CHRISMED Journal of Health and Research, 2018
Hunter's Syndrome or mucopolysaccharidosis Type II is a rare metabolic disorder caused by the deficiency of lysosomal enzyme iduronate-2-sulfatase. It results in progressive accumulation of deramatan and heparan sulfates in tissues leading to a wide ...
Sharon Vincent, Joe Mathew Cherian, Abi M Thomas, Rajesh Kumar   +3 more
doaj   +1 more source

Clinical Characteristics and Healthcare Resource Utilization for Patients with Mucopolysaccharidosis II (MPS II) in the United States: A Retrospective Chart Review

Journal of Health Economics and Outcomes Research, 2022
**Background:** Mucopolysaccharidosis II (MPS II; Hunter syndrome) is a rare, X-linked, life-limiting lysosomal storage disease characterized by a deficiency in the activity of the enzyme iduronate-2-sulfatase.
Olulade Ayodele, Kersten Müller, Solmaz Setayeshgar, David Alexanderian, Karen S. Yee   +4 more
doaj   +2 more sources

Mucopolysaccharidosis type II (Hunter syndrome) in a boy from the Republic of Serbia: A case report [PDF]

Kragujevac Journal of Science, 2023
Mucopolysaccharidosis type II or Hunter syndrome is a hereditary, progressive disease that occurs due to the deposition of acidic glucosaminoglycans in lysosomes, due to hereditary deficits of specific degradation enzymes.
Tubić-Vukajlović Jovana M., Bojović Lana P., Jevremović Nevena G., Simić Ivan B.   +3 more
doaj  

Management of Difficult Airway in a Patient with Mucopolysaccharidosis Type II

Journal of Pediatric Emergency and Intensive Care Medicine, 2019
Mucopolysaccharidosis type II (MPS II) is a rare, X-linked recessive disease characterized by deficiency of lysosomal iduronate-2-sulfatase. Progressive upper airway obstruction is common in patients with MPS II.
Damla Hanalioğlu, Batuhan Yeke, Ahmet Ziya Birbilen, Serap Sivri, Özlem Tekşam   +4 more
doaj   +1 more source

Multiplex tandem mass spectrometry enzymatic activity assay for the screening and diagnosis of Mucolipidosis type II and III

Molecular Genetics and Metabolism Reports, 2023
Mucolipidosis type II and III (MLII/III) is caused by defects in the mannose-6-phosphate system, which is essential to target most of the lysosomal hydrolases to the lysosome.
Xinying Hong, Laura Pollard, Miao He, Michael H. Gelb, Timothy C. Wood   +4 more
doaj   +1 more source

In vitro recapitulation of the site-specific editing (to wild-type) of mutant IDS mRNA transcripts, and the characterization of IDS protein translated from the edited mRNAs [PDF]

, 2017
The transfer of genomic information into the primary RNA sequence can be altered by RNA editing. We have previously shown that genomic variants can be RNA-edited to wild-type. The presence of distinct “edited” iduronate 2-sulfatase (IDS) mRNA transcripts
Amico, Giulia, Bruschi, Maurizio, Candiano, Giovanni, Cooper, David Neil, Corsolini, Fabio, Dardis, Andrea, Del Zotto, Genny, Filocamo, Mirella, Lualdi, Susanna, Pedemonte, Nicoletta, Tomati, Valeria, Zegarra-Moran, Olga   +11 more
core   +2 more sources

Changes in Glycogen and Glycosaminoglycan Levels in Hepatocytes of Iduronate-2-Sulfatase Knockout Mice before and after Recombinant Iduronate-2-Sulfatase Supplementation

Yonsei Medical Journal, 2011
Mucopolysaccharidosis II (MPS II) is a lysosomal storage disorder caused by a deficiency of iduronate-2 sulfatase (IdS), which is involved in the degradation of glycosaminoglycan (GAG). In this study, the frequency of fasting hypoglycemia in patients with MPS II was investigated and changes in accumulation of glycogen and GAG in the hepatocytes of IdS ...
Lee, Jee Hyun, Choe, Yon Ho, Kim, Su Jin, Paik, Kyung Hoon, Jin, Dong-Kyu   +4 more
openaire   +2 more sources

Generation of an induced pluripotent stem cell line (TRNDi008-A) from a Hunter syndrome patient carrying a hemizygous 208insC mutation in the IDS gene

Stem Cell Research, 2019
Mucopolysaccharidosis Type II (MPS II), also known as Hunter syndrome, is a rare X-linked genetic disease caused by mutations in the IDS gene encoding iduronate 2-sulfatase (I2S).
Junjie Hong, Miao Xu, Rong Li, Yu-Shan Cheng, Jennifer Kouznetsova, Jeanette Beers, Chengyu Liu, Jizhong Zou, Wei Zheng   +8 more
doaj   +1 more source

Heparan sulfate and heparin interactions with proteins. [PDF]

, 2015
Heparan sulfate (HS) polysaccharides are ubiquitous components of the cell surface and extracellular matrix of all multicellular animals, whereas heparin is present within mast cells and can be viewed as a more sulfated, tissuespecific, HS variant.
Alessandri G, Andrew K. Powell, Ashley J. Hughes, Casu B, Dietrich CP, Edwin A. Yates, Guimond S, Helena B. Nader, Kato M, Landt M, Lyon M, Maccarana M, Marcelo A. Lima, Maria C. Z. Meneghetti, Porcionatto MA, Timothy R. Rudd, Toth L, Turnbull JE, Walker A   +18 more
core   +1 more source

RNF13 is a previously undescribed interactor of iduronate 2‐sulfatase that modifies its glycosylation and maturation

The FEBS Journal, EarlyView.
Iduronate 2‐sulfatase (IDS; purple) is expressed as a precursor protein that goes through multiple steps of maturation, modification, and trafficking to become an active lysosomal enzyme that degrades glycosaminoglycans. Our study shows that the transmembrane ubiquitin ligases RNF13 (orange) and RNF167 (pink) heterodimerize, affecting IDS intracellular
Valérie C. Cabana, Antoine Y. Bouchard, Audrey M. Sénécal, Laurent Cappadocia, Marc P. Lussier   +4 more
wiley   +1 more source