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proteins. Page last changed on 19 Dec 2016.
SULF2, sulfatase 2, HSulf-2
Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Heparan sulfate 6-O-endosulfatases, such as SULF2, selectively remove 6-O-sulfate groups from heparan sulfate. This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules (Dai et al., 2005 [PubMed 16192265]).[supplied by OMIM, Mar 2008] (from
Gu et al., Shanghai, China. In Oncol Rep, Jan 2016
UNASSIGNED: In previous studies Sulf2 has been evidenced to play an important role in tumor progression through editing sulfate moieties on heparan sulfate proteoglycans (HSPGs) and modulating heparin binding growth factors.
Reynard et al., Newcastle upon Tyne, United Kingdom. In Arthritis Rheumatol, Nov 2015
OBJECTIVE: To functionally characterize the osteoarthritis (OA) susceptibility variants that map to a region of high linkage disequilibrium (LD) on chromosome 20q13 marked by the single-nucleotide polymorphism (SNP) rs6094710 and encompassing NCOA3 and SULF2.
Sakashita et al., Tokushima, Japan. In J Biol Chem, Nov 2015
We also found that cellular interaction and cytotoxicity of apoA-IIowa amyloid were significantly attenuated in CHO cells that stably expressed the human extracellular endoglucosamine 6-sulfatases HSulf-1 and HSulf-2.
Morel et al., Montpellier, France. In Genes Immun, Oct 2015
These factors are implicated in different functions, such as the respiratory chain (ND3), the transport of lipids (OSBP2, PLTP), the regulation of signaling linked to extracellular factors (SULF2, GALNT1, SIAE) or the regulation of gene expression (TET2 and LARP6).
Dierks et al., Bielefeld, Germany. In Plos One, 2014
INTRODUCTION: Sulf1 and Sulf2 are cell surface sulfatases, which remove specific 6-O-sulfate groups from heparan sulfate (HS) proteoglycans, resulting in modulation of various HS-dependent signaling pathways.
Dredge et al., Brisbane, Australia. In Front Oncol, 2013
As substrates for the key enzymes sulfatases and heparanase, the modification of HSPGs is typically characterized by the degradation of heparan sulfate (HS) chains/sulfation patterns via the endo-6-O-sulfatases (Sulf1 and Sulf2) or by heparanase, an endo-glycosidase that cleaves the HS polymers releasing smaller fragments from HSPG complexes.
Belinsky et al., Albuquerque, United States. In Oncogene, 2012
genes and pathways modulated by epigenetic inactivation of SULF2 and the effects on sensitivity to chemotherapy were characterized in lung cancer in vitro and in vivo; silencing SULF2 primarily increased expression of interferon-inducible genes including ISG15
Dhoot et al., London, United Kingdom. In Biochem Biophys Res Commun, 2011
This study demonstrates that unlike normal adult lung with little or no SULF2 expression, this enzyme is expressed at high levels in most lung tumours showing differential cellular distribution of full length and shorter SULF2 variants in such tumours.
Dierks et al., Bielefeld, Germany. In J Biotechnol, 2007
The recent discovery of two sulfatases, Sulf1 and Sulf2, with the unique ability to edit sulfation patterns at the cell surface, has opened up a new dimension as to how we understand the regulation of HS sulfation patterning and pattern-dependent cell signaling events.