Hepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells.

2.50
Hdl Handle:
http://hdl.handle.net/10541/92754
Title:
Hepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells.
Authors:
Rahmoune, H; Rudland, P S; Gallagher, John T; Fernig, D G
Abstract:
Hepatocyte growth factor/scatter factor (HGF/SF) is a heparan sulfate (HS)-binding growth factor and morphogen for mammary epithelial cells that is produced by mammary stromal fibroblasts. HS chains, purified as peptidoglycans from a panel of cell lines representative of the ductal epithelial cell (Huma 123), the myoepithelial cell (Huma 109), the stromal fibroblast (Rama 27), and malignant mammary epithelial cells (MCF-7 and ZR-75), were used in a biosensor-based assay to identify the classes of HGF/SF-binding sites in the polysaccharide chains. At least three distinct binding sites were identified. One site exhibits fast association and fast dissociation kinetics [kass (1.4-7.7) x 10(6) M-1 s-1; kdiss 0. 0032-0.0096 s-1] and is present on the HS from benign Huma 123 epithelial cells, Huma 109 myoepithelial-like cells, and ZR-75 malignant cells. The second binding site, found on HS from the malignant MCF-7 cells, has slower HGF/SF-binding kinetics (kass 0.20 x 10(6) M-1 s-1; kdiss 0.00055 s-1). The third binding site possesses fast association and slow dissociation kinetics (kass 1.1 x 10(6) M-1 s-1; kdiss 0.00020 s-1) and was found on the HS isolated from the culture medium of the Huma 123 benign epithelial cells. The first and second binding sites have a similar Kd, 1-3 nM, while the third binding site has a considerably higher affinity for HGF/SF (Kd 200 pM). The three binding sites seem to be mutually exclusive, since each sample of HS possessed just one of the sites.
Affiliation:
School of Biological Sciences, Life Sciences Building, University of Liverpool, U.K.
Citation:
Hepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells. 1998, 37 (17):6003-8 Biochemistry
Journal:
Biochemistry
Issue Date:
28-Apr-1998
URI:
http://hdl.handle.net/10541/92754
DOI:
10.1021/bi972468t
PubMed ID:
9558337
Type:
Article
Language:
en
ISSN:
0006-2960
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorRahmoune, Hen
dc.contributor.authorRudland, P Sen
dc.contributor.authorGallagher, John Ten
dc.contributor.authorFernig, D Gen
dc.date.accessioned2010-02-23T13:04:40Z-
dc.date.available2010-02-23T13:04:40Z-
dc.date.issued1998-04-28-
dc.identifier.citationHepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells. 1998, 37 (17):6003-8 Biochemistryen
dc.identifier.issn0006-2960-
dc.identifier.pmid9558337-
dc.identifier.doi10.1021/bi972468t-
dc.identifier.urihttp://hdl.handle.net/10541/92754-
dc.description.abstractHepatocyte growth factor/scatter factor (HGF/SF) is a heparan sulfate (HS)-binding growth factor and morphogen for mammary epithelial cells that is produced by mammary stromal fibroblasts. HS chains, purified as peptidoglycans from a panel of cell lines representative of the ductal epithelial cell (Huma 123), the myoepithelial cell (Huma 109), the stromal fibroblast (Rama 27), and malignant mammary epithelial cells (MCF-7 and ZR-75), were used in a biosensor-based assay to identify the classes of HGF/SF-binding sites in the polysaccharide chains. At least three distinct binding sites were identified. One site exhibits fast association and fast dissociation kinetics [kass (1.4-7.7) x 10(6) M-1 s-1; kdiss 0. 0032-0.0096 s-1] and is present on the HS from benign Huma 123 epithelial cells, Huma 109 myoepithelial-like cells, and ZR-75 malignant cells. The second binding site, found on HS from the malignant MCF-7 cells, has slower HGF/SF-binding kinetics (kass 0.20 x 10(6) M-1 s-1; kdiss 0.00055 s-1). The third binding site possesses fast association and slow dissociation kinetics (kass 1.1 x 10(6) M-1 s-1; kdiss 0.00020 s-1) and was found on the HS isolated from the culture medium of the Huma 123 benign epithelial cells. The first and second binding sites have a similar Kd, 1-3 nM, while the third binding site has a considerably higher affinity for HGF/SF (Kd 200 pM). The three binding sites seem to be mutually exclusive, since each sample of HS possessed just one of the sites.en
dc.language.isoenen
dc.subjectBreast Canceren
dc.subjectCultured Tumour Cellsen
dc.subject.meshAnimals-
dc.subject.meshBinding Sites-
dc.subject.meshBiosensing Techniques-
dc.subject.meshBreast Neoplasms-
dc.subject.meshCell Line-
dc.subject.meshEpithelial Cells-
dc.subject.meshFibroblasts-
dc.subject.meshHeparan Sulfate Proteoglycans-
dc.subject.meshHepatocyte Growth Factor-
dc.subject.meshHumans-
dc.subject.meshKinetics-
dc.subject.meshMammary Glands, Animal-
dc.subject.meshRats-
dc.subject.meshReceptors, Cell Surface-
dc.subject.meshTumor Cells, Cultured-
dc.titleHepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells.en
dc.typeArticleen
dc.contributor.departmentSchool of Biological Sciences, Life Sciences Building, University of Liverpool, U.K.en
dc.identifier.journalBiochemistryen
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