2.50
Hdl Handle:
http://hdl.handle.net/10541/85497
Title:
Role of heparan sulfate-2-O-sulfotransferase in the mouse.
Authors:
Merry, Catherine L R; Wilson, Valerie A
Abstract:
Heparan sulfate (HS) is a long unbranched polysaccharide found covalently attached to various proteins at the cell surface and in the extracellular matrix. It plays a central role in embryonic development and cellular function by modulating the activities of an extensive range of growth factors and morphogens. HS 2-O-sulfotransferase (Hs2st) occupies a critical position in the succession of enzymes responsible for the biosynthesis of HS, catalysing the transfer of sulfate to the C2-position of selected hexuronic acid residues within the nascent HS chain. Previous studies have concluded that 2-O-sulfation of HS is essential for it to cooperate in many growth factor/receptor interactions. Surprisingly therefore, embryos lacking functional Hs2st survive until birth, but die perinatally, suffering complete failure to form kidneys. However, this rather late lethality belies a more intricate involvement of 2-O-sulfated HS during development. The purpose of this review is to summarise the requirements for 2-O-sulfated HS during mouse development, at the morphological and molecular level. The implications that altered HS structure may have on growth factor/receptor signalling in vivo will be discussed.
Affiliation:
Cancer Research Campaign, Department of Medical Oncology, Christie Hospital NHS Trust, Manchester, United Kingdom.
Citation:
Role of heparan sulfate-2-O-sulfotransferase in the mouse. 2002, 1573 (3):319-27 Biochim. Biophys. Acta
Journal:
Biochimica et Biophysica Acta
Issue Date:
19-Dec-2002
URI:
http://hdl.handle.net/10541/85497
PubMed ID:
12417414
Type:
Article
Language:
en
ISSN:
0006-3002
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorMerry, Catherine L Ren
dc.contributor.authorWilson, Valerie Aen
dc.date.accessioned2009-11-06T09:15:26Z-
dc.date.available2009-11-06T09:15:26Z-
dc.date.issued2002-12-19-
dc.identifier.citationRole of heparan sulfate-2-O-sulfotransferase in the mouse. 2002, 1573 (3):319-27 Biochim. Biophys. Actaen
dc.identifier.issn0006-3002-
dc.identifier.pmid12417414-
dc.identifier.urihttp://hdl.handle.net/10541/85497-
dc.description.abstractHeparan sulfate (HS) is a long unbranched polysaccharide found covalently attached to various proteins at the cell surface and in the extracellular matrix. It plays a central role in embryonic development and cellular function by modulating the activities of an extensive range of growth factors and morphogens. HS 2-O-sulfotransferase (Hs2st) occupies a critical position in the succession of enzymes responsible for the biosynthesis of HS, catalysing the transfer of sulfate to the C2-position of selected hexuronic acid residues within the nascent HS chain. Previous studies have concluded that 2-O-sulfation of HS is essential for it to cooperate in many growth factor/receptor interactions. Surprisingly therefore, embryos lacking functional Hs2st survive until birth, but die perinatally, suffering complete failure to form kidneys. However, this rather late lethality belies a more intricate involvement of 2-O-sulfated HS during development. The purpose of this review is to summarise the requirements for 2-O-sulfated HS during mouse development, at the morphological and molecular level. The implications that altered HS structure may have on growth factor/receptor signalling in vivo will be discussed.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshGrowth Substances-
dc.subject.meshHeparitin Sulfate-
dc.subject.meshMice-
dc.subject.meshPhenotype-
dc.subject.meshReceptors, Growth Factor-
dc.subject.meshSignal Transduction-
dc.subject.meshSulfotransferases-
dc.titleRole of heparan sulfate-2-O-sulfotransferase in the mouse.en
dc.typeArticleen
dc.contributor.departmentCancer Research Campaign, Department of Medical Oncology, Christie Hospital NHS Trust, Manchester, United Kingdom.en
dc.identifier.journalBiochimica et Biophysica Actaen

Related articles on PubMed

All Items in Christie are protected by copyright, with all rights reserved, unless otherwise indicated.