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Article ; Online: Tinkering with heparan sulfate sulfation to steer development.

Gorsi, Bushra / Stringer, Sally E

2007 Volume 17, Issue 4, Page(s) 173–177

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 ... ...

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.
MeSH term(s)	Animals ; Carbohydrate Epimerases/metabolism ; Heparitin Sulfate/biosynthesis ; Heparitin Sulfate/metabolism ; Humans ; Morphogenesis/physiology ; N-Acetylglucosaminyltransferases/genetics ; Sulfatases/metabolism ; Sulfotransferases/genetics
Chemical Substances	Heparitin Sulfate (9050-30-0) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; exostosin-1 (EC 2.4.1.224) ; Sulfotransferases (EC 2.8.2.-) ; heparan sulfate 6-O-sulfotransferase (EC 2.8.2.-) ; heparan-sulfate 2-sulfotransferase (EC 2.8.2.-) ; heparitin sulfotransferase (EC 2.8.2.8) ; Sulfatases (EC 3.1.6.-) ; Carbohydrate Epimerases (EC 5.1.3.-) ; heparin-heparan sulfate-glucuronic acid C5-epimerase (EC 5.1.3.-)
Language	English
Publishing date	2007-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2007.02.006
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Article ; Online: Dynamic expression patterns of 6-O endosulfatases during zebrafish development suggest a subfunctionalisation event for sulf2.

Gorsi, Bushra / Whelan, Simon / Stringer, Sally E

Developmental dynamics : an official publication of the American Association of Anatomists

2010 Volume 239, Issue 12, Page(s) 3312–3323

Abstract: The 6-O-endosulfatase enzymes (Sulfs) edit the final sulfation pattern and function of heparan sulfate (HS) by removal of 6-O-sulfate groups from the chain. To date, two mammalian sulf genes have been identified that regulate many signalling pathways ... ...

Abstract	The 6-O-endosulfatase enzymes (Sulfs) edit the final sulfation pattern and function of heparan sulfate (HS) by removal of 6-O-sulfate groups from the chain. To date, two mammalian sulf genes have been identified that regulate many signalling pathways during embryonic development. In zebrafish a sulf1 ortholog and duplicate copies of the mammalian sulf2 gene, sulf2a and sulf2, have been identified, which contain conserved motifs characteristic of vertebrate sulf genes. Zebrafish sulf1 and sulf2a are broadly expressed in the central nervous system (CNS) and non-neuronal tissue including heart, somite boundaries, olfactory system, and otic vesicle, whereas sulf2 expression is almost entirely restricted to the CNS. The duplicate copies of sulf2 have distinct expression patterns, which together mirror that of mouse sulf2, suggesting duplication in the teleost lineage has been followed by subfunctionalisation, whereby both genes need to be preserved by selection to ensure the ancestral gene's expression profile and function is maintained.
MeSH term(s)	Animals ; Central Nervous System/embryology ; Computational Biology ; Embryo, Nonmammalian/metabolism ; Heart/embryology ; Heparitin Sulfate/metabolism ; In Situ Hybridization ; Olfactory Pathways/embryology ; Proteoglycans/metabolism ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism
Chemical Substances	Proteoglycans ; Zebrafish Proteins ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2010-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1102541-4
ISSN	1097-0177 ; 1058-8388
ISSN (online)	1097-0177
ISSN	1058-8388
DOI	10.1002/dvdy.22456
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Article: Interaction of platelet factor 4 with fibroblast growth factor 2 is stabilised by heparan sulphate.

Chadderton, Naomi S / Stringer, Sally E

The international journal of biochemistry & cell biology

2003 Volume 35, Issue 7, Page(s) 1052–1055

Abstract: The CXC chemokine platelet factor 4 (PF4) appears to inhibit tumour growth through its modulation of the activity of angiogenic growth factors. We investigated the heparan sulphate-dependent mechanism of PF4 inhibition of fibroblast growth factor 2 (FGF- ... ...

Abstract	The CXC chemokine platelet factor 4 (PF4) appears to inhibit tumour growth through its modulation of the activity of angiogenic growth factors. We investigated the heparan sulphate-dependent mechanism of PF4 inhibition of fibroblast growth factor 2 (FGF-2). The ability of PF4 to bind simultaneously to both FGF-2 and HS was assessed using affinity gel chromatography. Thirty-three to forty-two percent more HS bound to the FGF-2 affinity gel in the presence of PF4 than with HS alone. Protection assays showed that PF4 and FGF-2 bound to adjacent or overlapping sites together covering a 12 kDa stretch of HS. This study suggests that the three components may form a ternary complex. PF4 released at sites of angiogenesis may bind to angiogenic growth factors attached to endothelial cell surface HS to disrupt or prevent them from interacting with their signalling receptors. Manipulation of this mechanism may prove useful for clinical intervention of angiogenesis.
MeSH term(s)	3T3 Cells ; Animals ; Binding Sites ; Fibroblast Growth Factor 2/antagonists & inhibitors ; Fibroblast Growth Factor 2/metabolism ; Heparitin Sulfate/metabolism ; In Vitro Techniques ; Mice ; Platelet Factor 4/metabolism
Chemical Substances	Fibroblast Growth Factor 2 (103107-01-3) ; Platelet Factor 4 (37270-94-3) ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2003-01-22
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/s1357-2725(02)00299-6
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Article: Identification of an MIP-1alpha -binding heparan sulfate oligosaccharide that supports long-term in vitro maintenance of human LTC-ICs.

Stringer, Sally E / Nelson, Matthew S / Gupta, Pankaj

Blood

2002 Volume 101, Issue 6, Page(s) 2243–2245

Abstract: We previously showed that heparan sulfate (HS) is required for in vitro cytokine + chemokine-mediated maintenance of primitive human hematopoietic progenitors. However, HS preparations are mixtures of polysaccharide chains of varying size, structure, and ...

Abstract	We previously showed that heparan sulfate (HS) is required for in vitro cytokine + chemokine-mediated maintenance of primitive human hematopoietic progenitors. However, HS preparations are mixtures of polysaccharide chains of varying size, structure, and protein-binding abilities. Therefore, we examined whether the long-term culture-initiating cells (LTC-IC) supportive capability of HS is attributable to an oligosaccharide of defined length and protein-binding ability. Oligosaccharides of a wide range of sizes were prepared, and their capability to support human marrow LTC-IC maintenance in the presence of low-dose cytokines and a single chemokine, macrophage inflammatory protein-1alpha (MIP-1alpha), was examined. LTC-IC supportive capability of HS oligosaccharides correlated directly with size and MIP-1alpha binding ability. A specific MIP-1alpha-binding HS oligosaccharide preparation of M(r) 10 kDa that optimally supported LTC-IC maintenance was identified. This oligosaccharide had the structure required for MIP-1alpha binding, which we have recently described. The present study defines the minimum size and structural features of LTC-IC supportive HS.
MeSH term(s)	Antigens, CD34/analysis ; Bone Marrow Cells/cytology ; Bone Marrow Cells/immunology ; Cells, Cultured ; Chemokine CCL3 ; Chemokine CCL4 ; HLA-DR Antigens/analysis ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/immunology ; Heparitin Sulfate/chemistry ; Heparitin Sulfate/metabolism ; Humans ; Macrophage Inflammatory Proteins/metabolism ; Oligosaccharides/chemistry ; Oligosaccharides/metabolism ; Oligosaccharides/pharmacology ; Protein Binding
Chemical Substances	Antigens, CD34 ; Chemokine CCL3 ; Chemokine CCL4 ; HLA-DR Antigens ; Macrophage Inflammatory Proteins ; Oligosaccharides ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2002-10-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2002-08-2588
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Article ; Online: Age-related impairment of endothelial progenitor cell migration correlates with structural alterations of heparan sulfate proteoglycans.

Williamson, Kate A / Hamilton, Andrew / Reynolds, John A / Sipos, Peter / Crocker, Ian / Stringer, Sally E / Alexander, Yvonne M

Aging cell

2012 Volume 12, Issue 1, Page(s) 139–147

Abstract: Aging poses one of the largest risk factors for the development of cardiovascular disease. The increased propensity toward vascular pathology with advancing age maybe explained, in part, by a reduction in the ability of circulating endothelial progenitor ...

Abstract	Aging poses one of the largest risk factors for the development of cardiovascular disease. The increased propensity toward vascular pathology with advancing age maybe explained, in part, by a reduction in the ability of circulating endothelial progenitor cells to contribute to vascular repair and regeneration. Although there is evidence to suggest that colony forming unit-Hill cells and circulating angiogenic cells are subject to age-associated changes that impair their function, the impact of aging on human outgrowth endothelial cell (OEC) function has been less studied. We demonstrate that OECs isolated from cord blood or peripheral blood samples from young and old individuals exhibit different characteristics in terms of their migratory capacity. In addition, age-related structural changes were discovered in OEC heparan sulfate (HS), a glycocalyx component that is essential in many signalling pathways. An age-associated decline in the migratory response of OECs toward a gradient of VEGF significantly correlated with a reduction in the relative percentage of the trisulfated disaccharide, 2-O-sulfated-uronic acid, N, 6-O-sulfated-glucosamine (UA[2S]-GlcNS[6S]), within OEC cell surface HS polysaccharide chains. Furthermore, disruption of cell surface HS reduced the migratory response of peripheral blood-derived OECs isolated from young subjects to levels similar to that observed for OECs from older individuals. Together these findings suggest that aging is associated with alterations in the fine structure of HS on the cell surface of OECs. Such changes may modulate the migration, homing, and engraftment capacity of these repair cells, thereby contributing to the progression of endothelial dysfunction and age-related vascular pathologies.
MeSH term(s)	Age Factors ; Apoptosis/physiology ; Blood Cells/cytology ; Cell Growth Processes/physiology ; Cell Movement/physiology ; Cell Survival/physiology ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Fetal Blood/cytology ; Heparan Sulfate Proteoglycans/metabolism ; Humans ; Longevity ; Stem Cells/cytology ; Stem Cells/metabolism
Chemical Substances	Heparan Sulfate Proteoglycans
Language	English
Publishing date	2012-11-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.12031
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Article ; Online: Cartilage tumour progression is characterized by an increased expression of heparan sulphate 6O-sulphation-modifying enzymes.

Waaijer, Cathelijn J F / de Andrea, Carlos E / Hamilton, Andrew / van Oosterwijk, Jolieke G / Stringer, Sally E / Bovée, Judith V M G

Virchows Archiv : an international journal of pathology

2012 Volume 461, Issue 4, Page(s) 475–481

Abstract: Chondrosarcomas are malignant cartilage-forming tumours that can arise centrally (in the medulla) or peripherally (at the surface) of the bone. They are classified into three histological grades which correspond to the clinical severity. Previous studies ...

Abstract	Chondrosarcomas are malignant cartilage-forming tumours that can arise centrally (in the medulla) or peripherally (at the surface) of the bone. They are classified into three histological grades which correspond to the clinical severity. Previous studies by our group have shown altered signal transduction of the fibroblast growth factor and Wnt signalling pathways during peripheral chondrosarcoma progression. Heparan sulphate (HS) is a glycosaminoglycan that facilitates receptor binding of multiple growth factors, in which the sulphation of 6O position plays a pivotal role. 6O-Sulphation occurs through three HS 6O-sulphotransferases (HS6ST1-3) and is fine-tuned by two endosulphatases (SULF1-2) that remove 6O-sulphate groups. We have investigated whether the expression of HS6STs and SULFs changes during chondrosarcoma progression and have determined 6O-sulphation levels in two chondrosarcoma cell lines. Immunohistochemistry on tissue microarrays of chondrosarcomas showed that HS6ST3 and SULF1 were highly expressed in most chondrosarcomas, whereas SULF2 expression was absent in most cases. HS6ST1 and HS6ST2 expression are significantly increased during chondrosarcoma progression, which suggest that 6O-sulphation is increased during progression. This was confirmed in one grade III chondrosarcoma cell line, which showed a dramatically increased 6O-sulphation compared to an articular chondrocyte cell line by HPLC; another cell line showed an increased expression of one 6O-sulphated HS disaccharide. In conclusion, our results show increased HS6ST1 and HS6ST2 expression during chondrosarcoma progression and increased HS 6O-sulphation in vitro. As 6O-sulphation plays an important role in signal transduction, altered HS6ST expression might be associated with changes in signal transduction pathways in chondrosarcoma progression.
MeSH term(s)	Biomarkers, Tumor/metabolism ; Biopsy ; Bone Neoplasms/metabolism ; Bone Neoplasms/pathology ; Cell Line, Tumor ; Cells, Cultured ; Chondrocytes/metabolism ; Chondrocytes/pathology ; Chondrosarcoma/metabolism ; Chondrosarcoma/pathology ; Disease Progression ; Fibroblast Growth Factors/metabolism ; Follow-Up Studies ; Humans ; In Vitro Techniques ; Microarray Analysis ; Signal Transduction/physiology ; Sulfotransferases/metabolism ; Wnt Proteins/metabolism
Chemical Substances	Biomarkers, Tumor ; Wnt Proteins ; Fibroblast Growth Factors (62031-54-3) ; HS6ST2 protein, human (EC 2.8.2.-) ; Sulfotransferases (EC 2.8.2.-) ; heparan sulfate 6-O-sulfotransferase (EC 2.8.2.-)
Language	English
Publishing date	2012-08-18
Publishing country	Germany
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1184867-4
ISSN	1432-2307 ; 0945-6317
ISSN (online)	1432-2307
ISSN	0945-6317
DOI	10.1007/s00428-012-1300-5
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Article: VEGF165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase.

Robinson, Christopher J / Mulloy, Barbara / Gallagher, John T / Stringer, Sally E

The Journal of biological chemistry

2005 Volume 281, Issue 3, Page(s) 1731–1740

Abstract: The vascular endothelial growth factor (VEGF) family of proteins controls the formation and growth of blood vessels. The most potent and widely expressed isoform, VEGF165, is secreted as a disulfide-linked homodimer with two identical heparin-binding ... ...

Abstract	The vascular endothelial growth factor (VEGF) family of proteins controls the formation and growth of blood vessels. The most potent and widely expressed isoform, VEGF165, is secreted as a disulfide-linked homodimer with two identical heparin-binding sites. Interactions with heparan sulfate (HS) regulate the diffusion, half-life, and affinity of VEGF165 for its signaling receptors. We have determined a number of key HS structural features that mediate the specific binding of the VEGF165 dimer. Carboxylate groups and 2-O-, 6-O-, and N-sulfation of HS contributed to the strength of the VEGF165 interaction; however, 6-O-sulfates appeared to be particularly important. Cleavage of HS by heparinase, heparitinase, or heparanase severely reduced VEGF165 binding. In contrast, K5 lyase-cleaved HS retained significant VEGF165 affinity, suggesting that binding sites for the growth factor are present within extended stretches of sulfation. Binding studies and molecular modeling demonstrated that an oligosaccharide 6 or 7 residues long was sufficient to fully occupy the heparin-binding site of a VEGF165 monomer. The data presented are consistent with a model whereby the two heparin-binding sites of the VEGF165 dimer interact simultaneously with highly sulfated S-domain regions of the HS chain that can be linked through a stretch of transition sequence.
MeSH term(s)	3T3 Cells ; Animals ; Carbohydrate Conformation ; Cattle ; Chromatography, High Pressure Liquid ; Dimerization ; Disaccharides/chemistry ; Glycosaminoglycans/metabolism ; Heparitin Sulfate/chemistry ; Heparitin Sulfate/isolation & purification ; Heparitin Sulfate/metabolism ; Mice ; Models, Molecular ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Sharks ; Vascular Endothelial Growth Factor A/chemistry ; Vascular Endothelial Growth Factor A/metabolism
Chemical Substances	Disaccharides ; Glycosaminoglycans ; Recombinant Proteins ; VEGFA protein, human ; Vascular Endothelial Growth Factor A ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2005-10-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M510760200
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Article ; Online: Decorin GAG synthesis and TGF-β signaling mediate Ox-LDL-induced mineralization of human vascular smooth muscle cells.

Yan, Jianyun / Stringer, Sally E / Hamilton, Andrew / Charlton-Menys, Valentine / Götting, Christian / Müller, Benjamin / Aeschlimann, Daniel / Alexander, M Yvonne

Arteriosclerosis, thrombosis, and vascular biology

2011 Volume 31, Issue 3, Page(s) 608–615

Abstract: Objective: Decorin and oxidized low-density lipoprotein (Ox-LDL) independently induce osteogenic differentiation of vascular smooth muscle cells (VSMCs). We aimed to determine whether decorin glycosaminoglycan (GAG) chain synthesis contributes to Ox-LDL- ...

Abstract	Objective: Decorin and oxidized low-density lipoprotein (Ox-LDL) independently induce osteogenic differentiation of vascular smooth muscle cells (VSMCs). We aimed to determine whether decorin glycosaminoglycan (GAG) chain synthesis contributes to Ox-LDL-induced differentiation and calcification of human VSMCs in vitro. Methods and results: Human VSMCs treated with Ox-LDL to induce oxidative stress showed increased alkaline phosphatase (ALP) activity, accelerated mineralization, and a difference in both decorin GAG chain biosynthesis and CS/DS structure compared with untreated controls. Ox-LDL increased mRNA abundance of both xylosyltransferase (XT)-I, the key enzyme responsible for GAG chain biosynthesis and Msx2, a marker of osteogenic differentiation. Furthermore, downregulation of XT-I expression using small interfering RNA blocked Ox-LDL-induced VSMC mineralization. Adenoviral-mediated overexpression of decorin, but not a mutated unglycanated form, accelerated mineralization of VSMCs, suggesting GAG chain addition on decorin is crucial for the process of differentiation. The decorin-induced VSMC osteogenic differentiation involved activation of the transforming growth factor (TGF)-β pathway, because it was attenuated by blocking of TGF-β receptor signaling and because decorin overexpression potentiated phosphorylation of the downstream signaling molecule smad2. Conclusions: These studies provide direct evidence that oxidative stress-mediated decorin GAG chain synthesis triggers TGF-β signaling and mineralization of VSMCs in vitro.
MeSH term(s)	Alkaline Phosphatase/metabolism ; Calcinosis/metabolism ; Cells, Cultured ; Decorin/biosynthesis ; Decorin/genetics ; Gene Expression Regulation ; Homeodomain Proteins/metabolism ; Humans ; Lipoproteins, LDL/metabolism ; Muscle, Smooth, Vascular/metabolism ; Myocytes, Smooth Muscle/metabolism ; Osteogenesis ; Oxidative Stress ; Pentosyltransferases/genetics ; Pentosyltransferases/metabolism ; Phosphorylation ; RNA Interference ; Signal Transduction ; Smad2 Protein/metabolism ; Time Factors ; Transforming Growth Factor beta1/metabolism ; UDP Xylose-Protein Xylosyltransferase
Chemical Substances	DCN protein, human ; Decorin ; Homeodomain Proteins ; Lipoproteins, LDL ; MSX2 protein ; SMAD2 protein, human ; Smad2 Protein ; TGFB1 protein, human ; Transforming Growth Factor beta1 ; oxidized low density lipoprotein ; Pentosyltransferases (EC 2.4.2.-) ; Alkaline Phosphatase (EC 3.1.3.1)
Language	English
Publishing date	2011-01-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1221433-4
ISSN	1524-4636 ; 1079-5642
ISSN (online)	1524-4636
ISSN	1079-5642
DOI	10.1161/ATVBAHA.110.220749
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Article: Heparin sequencing.

Stringer, Sally E / Kandola, Balbant S / Pye, David A / Gallagher, John T

Glycobiology

2003 Volume 13, Issue 2, Page(s) 97–107

Abstract: Heparin is a highly sulfated glycosaminoglycan widely used as an anticoagulant. Modifications in its relatively uniform structure appear to be key to its recognition and modulation of serine proteases, growth factors, chemokines, and extracellular ... ...

Abstract	Heparin is a highly sulfated glycosaminoglycan widely used as an anticoagulant. Modifications in its relatively uniform structure appear to be key to its recognition and modulation of serine proteases, growth factors, chemokines, and extracellular proteins, as has been most clearly demonstrated in the antithrombin binding site. We sequenced the major oligosaccharides released from mastocytoma heparin by partial nitrous acid using a highly sensitive technique tailored for sequencing of metabolically radiolabeled heparin. It utilizes partial nitrous acid cleavage to allow simultaneous sequencing of the internal components of the oligosaccharide under investigation by specific lysosomal exoenzymes. Sequencing revealed that although the majority of the heparin disaccharides are N-, 2-O-, and 6-O-sulfated, the less sulfated disaccharides (lacking 2-O- or 6-O-sulfates) seem to be spaced out along the chain. The technique may be particularly useful for characterizing heparin from novel sources, such as the glial progenitor cells and Ascidia, as well as for sequencing protein binding sites.
MeSH term(s)	Animals ; Carbohydrate Sequence ; Chromatography, High Pressure Liquid/methods ; Electrophoresis, Polyacrylamide Gel/methods ; Heparin/analysis ; Iduronidase/metabolism ; Molecular Sequence Data ; Nitrous Acid/metabolism ; Oligosaccharides/isolation & purification ; Oligosaccharides/metabolism ; Particle Size ; Sequence Analysis/methods ; Sulfatases/metabolism ; Tumor Cells, Cultured
Chemical Substances	Oligosaccharides ; Heparin (9005-49-6) ; Sulfatases (EC 3.1.6.-) ; disulfoglucosamine-6-sulfatase (EC 3.1.6.11) ; Iduronidase (EC 3.2.1.76) ; Nitrous Acid (T2I5UM75DN)
Language	English
Publishing date	2003-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwg006
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Article: Not all perlecans are created equal: interactions with fibroblast growth factor (FGF) 2 and FGF receptors.

Knox, Sarah / Merry, Catherine / Stringer, Sally / Melrose, James / Whitelock, John

The Journal of biological chemistry

2002 Volume 277, Issue 17, Page(s) 14657–14665

Abstract: Human basement membrane heparan sulfate proteoglycan (HSPG) perlecan binds and activates fibroblast growth factor (FGF)-2 through its heparan sulfate (HS) chains. Here we show that perlecans immunopurified from three cellular sources possess different HS ...

Abstract	Human basement membrane heparan sulfate proteoglycan (HSPG) perlecan binds and activates fibroblast growth factor (FGF)-2 through its heparan sulfate (HS) chains. Here we show that perlecans immunopurified from three cellular sources possess different HS structures and subsequently different FGF-2 binding and activating capabilities. Perlecan isolated from human umbilical arterial endothelial cells (HUAEC) and a continuous endothelial cell line (C11 STH) bound similar amounts of FGF-2 either alone or complexed with FGFRalpha1-IIIc or FGFR3alpha-IIIc. Both perlecans stimulated the growth of BaF3 cell lines expressing FGFR1b/c; however, only HUAEC perlecan stimulated those cells expressing FGFR3c, suggesting that the source of perlecan confers FGF and FGFR binding specificity. Despite these differences in FGF-2 activation, the level of 2-O- and 6-O-sulfation was similar for both perlecans. Interestingly, perlecan isolated from a colon carcinoma cell line that was capable of binding FGF-2 was incapable of activating any BaF3 cell line unless the HS was removed from the protein core. The HS chains also exhibited greater bioactivity after digestion with heparinase III. Collectively, these data clearly demonstrate that the bioactivity of HS decorating a single PG is dependent on its cell source and that subtle changes in structure including secondary interactions have a profound effect on biological activity.
MeSH term(s)	Cell Line ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Fibroblast Growth Factor 2/metabolism ; Heparan Sulfate Proteoglycans/isolation & purification ; Heparan Sulfate Proteoglycans/metabolism ; Humans ; Protein Binding ; Receptors, Fibroblast Growth Factor/metabolism
Chemical Substances	Heparan Sulfate Proteoglycans ; Receptors, Fibroblast Growth Factor ; Fibroblast Growth Factor 2 (103107-01-3) ; perlecan (143972-95-6)
Language	English
Publishing date	2002-02-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111826200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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