Tinkering with heparan sulfate sulfation to steer development

Bushra Gorsi; Sally E. Stringer

doi:10.1016/j.tcb.2007.02.006

Tinkering with heparan sulfate sulfation to steer development

Bushra Gorsi, Sally E. Stringer

Research output: Contribution to journal › Article › peer-review

Abstract

Heparan sulfate (HS) proteoglycans, at the cell surface and extracellular matrix, facilitate ligand-receptor interactions crucial to many physiological processes. The distinct sulfation patterns of HS sugar chains presented by their protein core are key to HS proteoglycan activity. Tight regulation of several Golgi complex enzyme families is crucial to produce complex tissue-specific HS sequences. Several in vivo models deficient in HS biosynthesis enzymes demonstrate that developmental abnormalities result from modified HS structure. This review will discuss the plasticity of sulfation requirements on HS for activating protein ligands, which might reflect a flexible HS biosynthetic mechanism. In addition, the latest discovery of HS acting enzymes, the Sulfs, responsible for extracellular tweaking of HS sulfation levels subsequent to biosynthesis will be considered. © 2007 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	173-177
Number of pages	4
Journal	Trends in cell biology
Volume	17
Issue number	4
DOIs	https://doi.org/10.1016/j.tcb.2007.02.006
Publication status	Published - Apr 2007

Access to Document

10.1016/j.tcb.2007.02.006

Cite this

@article{eb282652139c4de09d5b6a6ece98433d,

title = "Tinkering with heparan sulfate sulfation to steer development",

abstract = "Heparan sulfate (HS) proteoglycans, at the cell surface and extracellular matrix, facilitate ligand-receptor interactions crucial to many physiological processes. The distinct sulfation patterns of HS sugar chains presented by their protein core are key to HS proteoglycan activity. Tight regulation of several Golgi complex enzyme families is crucial to produce complex tissue-specific HS sequences. Several in vivo models deficient in HS biosynthesis enzymes demonstrate that developmental abnormalities result from modified HS structure. This review will discuss the plasticity of sulfation requirements on HS for activating protein ligands, which might reflect a flexible HS biosynthetic mechanism. In addition, the latest discovery of HS acting enzymes, the Sulfs, responsible for extracellular tweaking of HS sulfation levels subsequent to biosynthesis will be considered. {\textcopyright} 2007 Elsevier Ltd. All rights reserved.",

author = "Bushra Gorsi and Stringer, {Sally E.}",

year = "2007",

month = apr,

doi = "10.1016/j.tcb.2007.02.006",

language = "English",

volume = "17",

pages = "173--177",

journal = "Trends in cell biology",

issn = "1879-3088",

publisher = "Elsevier BV",

number = "4",

}

TY - JOUR

T1 - Tinkering with heparan sulfate sulfation to steer development

AU - Gorsi, Bushra

AU - Stringer, Sally E.

PY - 2007/4

Y1 - 2007/4

N2 - Heparan sulfate (HS) proteoglycans, at the cell surface and extracellular matrix, facilitate ligand-receptor interactions crucial to many physiological processes. The distinct sulfation patterns of HS sugar chains presented by their protein core are key to HS proteoglycan activity. Tight regulation of several Golgi complex enzyme families is crucial to produce complex tissue-specific HS sequences. Several in vivo models deficient in HS biosynthesis enzymes demonstrate that developmental abnormalities result from modified HS structure. This review will discuss the plasticity of sulfation requirements on HS for activating protein ligands, which might reflect a flexible HS biosynthetic mechanism. In addition, the latest discovery of HS acting enzymes, the Sulfs, responsible for extracellular tweaking of HS sulfation levels subsequent to biosynthesis will be considered. © 2007 Elsevier Ltd. All rights reserved.

AB - Heparan sulfate (HS) proteoglycans, at the cell surface and extracellular matrix, facilitate ligand-receptor interactions crucial to many physiological processes. The distinct sulfation patterns of HS sugar chains presented by their protein core are key to HS proteoglycan activity. Tight regulation of several Golgi complex enzyme families is crucial to produce complex tissue-specific HS sequences. Several in vivo models deficient in HS biosynthesis enzymes demonstrate that developmental abnormalities result from modified HS structure. This review will discuss the plasticity of sulfation requirements on HS for activating protein ligands, which might reflect a flexible HS biosynthetic mechanism. In addition, the latest discovery of HS acting enzymes, the Sulfs, responsible for extracellular tweaking of HS sulfation levels subsequent to biosynthesis will be considered. © 2007 Elsevier Ltd. All rights reserved.

U2 - 10.1016/j.tcb.2007.02.006

DO - 10.1016/j.tcb.2007.02.006

M3 - Article

SN - 1879-3088

VL - 17

SP - 173

EP - 177

JO - Trends in cell biology

JF - Trends in cell biology

IS - 4

ER -

Tinkering with heparan sulfate sulfation to steer development

Abstract

Access to Document

Fingerprint

Cite this