2.50
Hdl Handle:
http://hdl.handle.net/10541/84313
Title:
Heparan sulfate 2-O-sulfotransferase (Hs2st) and mouse development
Authors:
Wilson, Valerie A; Gallagher, John T; Merry, Catherine L R
Abstract:
Heparan sulphate 2-O-sulphotransferase (Hs2st) acts at an intermediate stage in the pathway of biosynthesis of heparan sulphate (HS), catalysing the transfer of sulphate from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to the C2-position of selected hexuronic acid residues within the maturing HS chain. It is well established that 2-O-sulphation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions. HS plays a central role in embryonic development and cellular function, modulating the activities of an extensive range of growth factors. Interestingly, in contrast to the early failure of embryos entirely lacking HS, Hs2st(-/-) mice survive until birth, but die perinatally due to a complete failure of kidney formation. The phenotype of Hs2st(-/-) mutant kidneys suggests that signalling between two tissues, ureteric bud and metanephric mesenchyme, is disrupted. We discuss candidate signalling molecules that may mediate this interaction. The HS generated by these mice lacks 2-O-sulphate groups but is extensively modified above wild type levels by O-sulphation at C-6 of glucosamine-N-sulfate (GlcNS) residues. We will discuss the potentially altered role of this atypical HS in growth factor signalling.
Affiliation:
Cancer Research UK Department of Medical Oncology, Christie Hospital NHS Trust, Manchester M20 4BX.
Citation:
Heparin sequencing. 2002, 19(4-5):347-354 Gly J.
Journal:
Glycoconjugate Journal
Issue Date:
2002
URI:
http://hdl.handle.net/10541/84313
DOI:
http://dx.doi.org/10.1023/A:1025325222530
Type:
Article
Language:
en
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorWilson, Valerie Aen
dc.contributor.authorGallagher, John Ten
dc.contributor.authorMerry, Catherine L Ren
dc.date.accessioned2009-10-16T10:42:45Z-
dc.date.available2009-10-16T10:42:45Z-
dc.date.issued2002-
dc.identifier.citationHeparin sequencing. 2002, 19(4-5):347-354 Gly J.en
dc.identifier.doihttp://dx.doi.org/10.1023/A:1025325222530-
dc.identifier.urihttp://hdl.handle.net/10541/84313-
dc.description.abstractHeparan sulphate 2-O-sulphotransferase (Hs2st) acts at an intermediate stage in the pathway of biosynthesis of heparan sulphate (HS), catalysing the transfer of sulphate from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to the C2-position of selected hexuronic acid residues within the maturing HS chain. It is well established that 2-O-sulphation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions. HS plays a central role in embryonic development and cellular function, modulating the activities of an extensive range of growth factors. Interestingly, in contrast to the early failure of embryos entirely lacking HS, Hs2st(-/-) mice survive until birth, but die perinatally due to a complete failure of kidney formation. The phenotype of Hs2st(-/-) mutant kidneys suggests that signalling between two tissues, ureteric bud and metanephric mesenchyme, is disrupted. We discuss candidate signalling molecules that may mediate this interaction. The HS generated by these mice lacks 2-O-sulphate groups but is extensively modified above wild type levels by O-sulphation at C-6 of glucosamine-N-sulfate (GlcNS) residues. We will discuss the potentially altered role of this atypical HS in growth factor signalling.en
dc.language.isoenen
dc.subjectHeparan Sulphateen
dc.subjectHeparan Sulphate 2-0-Sulphotransferaseen
dc.subjectHs2sten
dc.subjectMiceen
dc.subjectEmbryoen
dc.titleHeparan sulfate 2-O-sulfotransferase (Hs2st) and mouse developmenten
dc.typeArticleen
dc.contributor.departmentCancer Research UK Department of Medical Oncology, Christie Hospital NHS Trust, Manchester M20 4BX.en
dc.identifier.journalGlycoconjugate Journalen
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