Multiple domains of the large fibroblast proteoglycan, versican - PubMed (original) (raw)

Multiple domains of the large fibroblast proteoglycan, versican

D R Zimmermann et al. EMBO J. 1989 Oct.

Abstract

The primary structure of a large chondroitin sulfate proteoglycan expressed by human fibroblasts has been determined. Overlapping cDNA clones code for the entire 2389 amino acid long core protein and the 20-residue signal peptide. The sequence predicts a potential hyaluronic acid-binding domain in the amino-terminal portion. This domain contains sequences virtually identical to partial peptide sequences from a glial hyaluronate-binding protein. Putative glycosaminoglycan attachment sites are located in the middle of the protein. The carboxy-terminal portion includes two epidermal growth factor (EGF)-like repeats, a lectin-like sequence and a complement regulatory protein-like domain. The same set of binding elements has also been identified in a new class of cell adhesion molecules. Amino- and carboxy-terminal portions of the fibroblast core protein are closely related to the core protein of a large chondroitin sulfate proteoglycan of chondrosarcoma cells. However, the glycosaminoglycan attachment regions in the middle of the core proteins are different and only the fibroblast core protein contains EGF-like repeats. Based on the similarities of its domains with various binding elements of other proteins, we suggest that the large fibroblast proteoglycan, herein referred to as versican, may function in cell recognition, possibly by connecting extracellular matrix components and cell surface glycoproteins.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Biochemistry. 1978 Oct 31;17(22):4756-70 - PubMed
    1. Cell. 1989 Mar 24;56(6):1033-44 - PubMed
    1. Nucleic Acids Res. 1984 Jan 25;12(2):857-72 - PubMed
    1. J Biol Chem. 1984 Mar 25;259(6):3407-12 - PubMed
    1. Biochem J. 1985 Aug 15;230(1):133-41 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources