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dc.contributor.authorPonting, Julie M
dc.contributor.authorKumar, Shant
dc.date.accessioned2010-05-17T16:00:33Z
dc.date.available2010-05-17T16:00:33Z
dc.date.issued1995-10
dc.identifier.citationLocalisation and cellular origin of hyaluronectin. 1995, 187 ( Pt 2):331-46 J. Anat.en
dc.identifier.issn0021-8782
dc.identifier.pmid7591996
dc.identifier.urihttp://hdl.handle.net/10541/99021
dc.description.abstractHyaluronectin is an extracellular matrix glycoprotein which specifically binds to hyaluronan. Isoforms of hyaluronectin are present in nervous and mesenchymal tissues but, while the nervous tissue isoform has been characterised in some detail, less is known about the mesenchymal isoform. Although its tissue localisation suggests a role in tumour development, neither its cellular origin nor its exact function are known. In this study we demonstrate hyaluronectin synthesis in fibroblasts and smooth muscle cells in vitro. The pattern of immunolocalisation of hyaluronectin in fibroblasts depended on the cell type, length of time spent by the cells in culture and cell density. Immunoreactivity in sparsely plated migratory cells was seen mainly in a patchy distribution at the attached cell surface and in the migration tracks left by the cells on the subtratum. In stationary cells a more uniform distribution associated with the attached cell surface was observed, while in confluent cultures hyaluronectin immunoreactivity was mainly seen as a network of fibrillar material above the cell. The pattern of staining was distinct from that of other hyaluronan-binding proteins. Immunoprecipitation, using antihyaluronectin antibodies, of the substratum-attached material deposited by human fetal fibroblasts revealed a family of proteins ranging from 22 to 90 kDa, the major protein being of approximately 60 kDa. These results lead us to propose that hyaluronectin plays an important role in cell migration, probably by regulation of hyaluronan distribution and binding.
dc.language.isoenen
dc.subjectCultured Tumour Cellsen
dc.subject.meshAdult
dc.subject.meshAnimals
dc.subject.meshAntigens, CD44
dc.subject.meshCattle
dc.subject.meshCells, Cultured
dc.subject.meshChick Embryo
dc.subject.meshExtracellular Matrix Proteins
dc.subject.meshFemale
dc.subject.meshFibroblasts
dc.subject.meshFibronectins
dc.subject.meshFluorescent Antibody Technique
dc.subject.meshHumans
dc.subject.meshMesoderm
dc.subject.meshMuscle, Smooth
dc.subject.meshSkin
dc.subject.meshTalin
dc.subject.meshTumor Cells, Cultured
dc.titleLocalisation and cellular origin of hyaluronectin.en
dc.typeArticleen
dc.contributor.departmentDepartment of Clinical Research, Christie Hospital, Manchester, UK.en
dc.identifier.journalJournal of Anatomyen
html.description.abstractHyaluronectin is an extracellular matrix glycoprotein which specifically binds to hyaluronan. Isoforms of hyaluronectin are present in nervous and mesenchymal tissues but, while the nervous tissue isoform has been characterised in some detail, less is known about the mesenchymal isoform. Although its tissue localisation suggests a role in tumour development, neither its cellular origin nor its exact function are known. In this study we demonstrate hyaluronectin synthesis in fibroblasts and smooth muscle cells in vitro. The pattern of immunolocalisation of hyaluronectin in fibroblasts depended on the cell type, length of time spent by the cells in culture and cell density. Immunoreactivity in sparsely plated migratory cells was seen mainly in a patchy distribution at the attached cell surface and in the migration tracks left by the cells on the subtratum. In stationary cells a more uniform distribution associated with the attached cell surface was observed, while in confluent cultures hyaluronectin immunoreactivity was mainly seen as a network of fibrillar material above the cell. The pattern of staining was distinct from that of other hyaluronan-binding proteins. Immunoprecipitation, using antihyaluronectin antibodies, of the substratum-attached material deposited by human fetal fibroblasts revealed a family of proteins ranging from 22 to 90 kDa, the major protein being of approximately 60 kDa. These results lead us to propose that hyaluronectin plays an important role in cell migration, probably by regulation of hyaluronan distribution and binding.


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