Decreasing Activity and Altered Protein Processing of Human Iduronate-2-sulfatase Mutations Demonstrated by Expression in COS7 Cells

Autor:	Phannee Sawangareetrakul, Suthipong Pangkanon, Siriporn Keeratichamroen, Ratana Charoenwattanasatien, Pranoot Tanpaiboon, Duangrurdee Wattanasirichaigoon, Voraratt Champattanachai, James R. Ketudat Cairns, Jisnuson Svasti
Rok vydání:	2012
Předmět:	Protein Folding Glycosylation Protein Conformation Biology Transfection Severity of Illness Index Biochemistry Gene Expression Regulation Enzymologic Dermatan sulfate chemistry.chemical_compound Catalytic Domain Lysosome Chlorocebus aethiops Leukocytes Genetics medicine Animals Humans Mucopolysaccharidosis type II Molecular Biology Gene Ecology Evolution Behavior and Systematics Glycoproteins Mucopolysaccharidosis II chemistry.chemical_classification Iduronate-2-sulfatase Hunter syndrome General Medicine Heparan sulfate medicine.disease Molecular biology Enzyme Activation medicine.anatomical_structure Enzyme chemistry COS Cells Mutation Plasmids
Zdroj:	Biochemical Genetics. 50:990-997
ISSN:	1573-4927 0006-2928
Popis:	Hunter syndrome, or mucopolysaccharidosis type II (MPS II; MIM:309900), is a rare X-linked recessive lysosomal storage disorder caused by defects of the gene coding for iduronate-2-sulfatase (IDS; EC 3.1.6.13) (Bach et al. 1973). IDS catabolizes dermatan sulfate and heparan sulfate in the lysosome. Lack of this enzyme leads to the systemic accumulation of these substances, eventually causing characteristic clinical
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99334e92a4fe0fc91ecdb8760e9309d7 https://doi.org/10.1007/s10528-012-9538-9 Zobrazit plný text záznamu Full text from SpringerLink