Nature 295, 614 - 615 (18 February 1982); doi:10.1038/295614a0

A non-collagenous glycoprotein from elastic tissue acts as substratum for growth of cells in vitro

P. Knox^*, P. Wells^† & A. Serafini-Fracassini^‡

^*Department of Biochemistry, St. George's Hospital Medical School, Cranmer Terrace, London SW17 0RE, UK
^†Department of Dental Biochemistry, Royal Dental Hospital of London School of Dental Surgery, St. George's Hospital Medical School, Cranmer Terrace, London SW17 0RE, UK
^‡Department of Microbiology and Biochemistry, University of St Andrews, St Andrews, Fife, UK

In vivo, cells are in intimate contact with an extracellular matrix, one of the components of which is collagen; the adhesion of cells to collagen in vitro has been extensively studied (for review, see ref. 1). In several connective tissue matrices, collagen fibres are replaced to a variable extent by elastin fibres which, under the electron microscope, appear to be composed of an elastin core surrounded by a network of fibrils 11 nm in diameter, usually referred to as the microfibrillin component. These fibrils have been implicated, on morphological grounds, in the biosynthesis of elastin fibres. A glycoprotein referred to as structural glycoprotein (SGP)², which has a molecular weight (M _r) of 34,000 and aggregates to form cylindrical tactoids having a uniform diameter of 11 nm, has been isolated from bovine ligamentum nuchae³. SGP was found to have amine oxidase activity, thus it seems to be functionally related to other peptidylysine oxidases involved in the biosynthesis of the elastin cross-links^4–6. Here we show that SGP acts as a substratum for fibroblasts and other cell types with fibronectin mediating the attachment and spreading of the cells. These results suggest that SGP may have a role in wound healing, morphogenetic movement and development of elastic tissues.

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