S Suzuki

TL;DR: The results indicate that the preponderance of glycosaminoglycans in the proteoglycan molecule is a main reason for both polydispersity and hydrophilicity of the proteglycan preparation, and suggest that the enzymic procedures could prove useful as a method to obtain new information about the structure and properties of proteogly can core molecules.

TL;DR: Investigation of chick embryo limb buds extracted after metabolically labeled with [35S]sulfate suggested that PG-M plays an important role in the cell condensation process by means of its interaction with fibronectin and type I collagen.

TL;DR: The results suggest the presence in the bound heparan sulphate of a specific structure involved in binding, likely that the binding of basic fibroblast growth factor (bFGF) may require the domain structure of the hepara sulphate to be composed of clustering IdoA(2SO4)-GlcNSO3 units.

TL;DR: It is suggested that most, if not all, of the hyaluronate-binding activity in preparations of chick cellular fibronectin is due to a proteoglycan identical to PG-M, thereby participating in formation of the pericellular matrix of fibroblasts.

TL;DR: Investigation of cartilage tissues shows that this proteoglycan exists in both the cartilage matrix and perichondrial noncartilagenous region, and antibody stains strands found on the cell surfaces and in the intercellular space of substrate-attached cell layers suggest that PG-Lt mediates cell- to-cell and cell-to-substrate contacts.