Show simple item record

dc.contributor.authorGallagher, John T
dc.date.accessioned2010-04-09T11:26:00Z
dc.date.available2010-04-09T11:26:00Z
dc.date.issued1994-04
dc.identifier.citationHeparan sulphates as membrane receptors for the fibroblast growth factors. 1994, 32 (4):239-47 Eur J Clin Chem Clin Biochemen
dc.identifier.issn0939-4974
dc.identifier.pmid8038264
dc.identifier.urihttp://hdl.handle.net/10541/96127
dc.description.abstractThe complex polymeric structure of heparan sulphate contains intra-chain sequences of sulphated sugar residues that define active sites for the binding and activation of growth factors. The molecular mechanisms of recognition and activation are slowly being revealed at least in the case of the interaction of heparan sulphate with basic fibroblast growth factor. Current data indicate that relatively long but specific binding sequences in heparan sulphate may induce a conformational change in basic fibroblast growth factor exposing a site on the protein that is recognised by signal transducing receptors. Heparan sulphate may also subserve functions of dimerisation of basic fibroblast growth factor and facilitation of receptor transfer by a secondary interaction with the receptor itself. Various models for heparan sulphate mediated induction of mitogenesis by basic fibroblast growth factor have been proposed and there are suggestions that the core protein of plasma membrane heparan sulphate-proteoglycans may participate in the cell signalling process. The vital importance of heparan sulphate in controlling growth factor activities has opened up a new chapter in proteoglycan research and has brought proteoglycans into the mainstream of cell biology. Further investigation of their mode of action is likely to reveal new information on the control of cell growth and development in both embryonic and adult tissues and may suggest novel methods of controlling diseases such as cancer, atherosclerosis or fibrosis that are driven by abnormal expression of growth factors or their receptors.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCarbohydrate Sequence
dc.subject.meshHeparitin Sulfate
dc.subject.meshMolecular Sequence Data
dc.subject.meshReceptors, Fibroblast Growth Factor
dc.titleHeparan sulphates as membrane receptors for the fibroblast growth factors.en
dc.typeArticleen
dc.contributor.departmentMed. Oncology Department, University of Manchester, Christie Hospital, United Kingdom.en
dc.identifier.journalEuropean Journal of Clinical Chemistry and Clinical Biochemistryen
html.description.abstractThe complex polymeric structure of heparan sulphate contains intra-chain sequences of sulphated sugar residues that define active sites for the binding and activation of growth factors. The molecular mechanisms of recognition and activation are slowly being revealed at least in the case of the interaction of heparan sulphate with basic fibroblast growth factor. Current data indicate that relatively long but specific binding sequences in heparan sulphate may induce a conformational change in basic fibroblast growth factor exposing a site on the protein that is recognised by signal transducing receptors. Heparan sulphate may also subserve functions of dimerisation of basic fibroblast growth factor and facilitation of receptor transfer by a secondary interaction with the receptor itself. Various models for heparan sulphate mediated induction of mitogenesis by basic fibroblast growth factor have been proposed and there are suggestions that the core protein of plasma membrane heparan sulphate-proteoglycans may participate in the cell signalling process. The vital importance of heparan sulphate in controlling growth factor activities has opened up a new chapter in proteoglycan research and has brought proteoglycans into the mainstream of cell biology. Further investigation of their mode of action is likely to reveal new information on the control of cell growth and development in both embryonic and adult tissues and may suggest novel methods of controlling diseases such as cancer, atherosclerosis or fibrosis that are driven by abnormal expression of growth factors or their receptors.


This item appears in the following Collection(s)

Show simple item record