Abstract: In accordance with the present invention, there is provided a novel synthetic polypeptide derived from the first type III repeat of fibronectin. The synthetic polypeptide of the invention encompasses a fibronectin-fibronectin binding site, and is capable of inhibiting fibronectin matrix assembly. In contrast to previously identified fibronectin fragments that block fibronectin matrix assembly by blocking an initial event in matrix assembly (i.e., fibronectin binding to cells), the invention polypeptide appears to inhibit an intermediate step in matrix assembly, i.e., fibronectin self-association prior to the disulfide cross-linking that stabilizes the fibronectin matrix.

Abstract: A method of isolating cell surface receptors utilizing a short peptide sequence bound to an affinity column. Cell surface receptors which bind selectively to the short peptide and which are specific to various adhesion proteins may be isolated therewith from various cell preparations. These receptors, whose functional integrity has been maintained by the presence of the peptide ligand, are incorporated into liposomes and used to deliver specific compounds inside the liposomes to select tissues containing the specific adhesion proteins.

Abstract: An adhesion receptor for laminin is provided. The receptor is isolated from cell or tissue extracts and fractionated on an affinity column composed of cell attachment-promoting fragments of laminin coupled to Sepharose.TM. in the presence of divalent cations. This receptor can be used to prepare specific antibodies for the analysis of the amount of laminin receptor expressed by cells and has other applications in cellular and tumor biology.

Abstract: The invention relates to the fibroblast proteoglycan, versican. The versican core protein has the amino acid sequence, and is encoded by the nucleotide sequence, as shown in FIG. 1. The nucleotide sequence and method of hyaluronic acid binding domain is provided and methods of preparing recombinant proteins having hyaluronic acid binding activity are provided. Such protein can be used to determine the presence of hyaluronic acid and as a vehicle to bring other molecules in contact with hyaluronic acid. The complete versican sequence will allow the production of the entire versican molecule to be used, for example, in tissue reconstruction. Nucleic acid probes are provided which are useful for detecting nucleic acid sequences encoding versican. The invention also provides antibodies reactive with versican.

Abstract: The present invention provides a substantially pure integrin-type receptor characterized in that it consists of an .alpha..sub.v and a .beta..sub.1 subunit. The .alpha..sub.v .beta..sub.1 integrin binds to fibronectin and GRGDSPK but does not bind to vitronectin. The .alpha..sub.v .beta..sub.1 integrin can be used to determine the presence of a .alpha..sub.v .beta..sub.1 ligand and to develop adhesion peptides specific for the various integrins. The presence of the .alpha..sub.v .beta..sub.1 integrin can be used to assess ability of cells to adhere to fibronectin.

Abstract: A method of using synthetic cell attachment-promoting peptides from fibronectin to detach cultured cells from the substratum is described.

Abstract: A polypeptide having the cell-attaching activity of fibronectin. The polypeptide has 108 amino acid residues and the formula: H-Ile-Gly-Gln-Gln-Ser-Thr-Val-Ser-Asp-Val-Pro-Arg-Asp-Leu-Glu-Val-Val-Ala- Ala-Thr-Pro-Thr-Ser-Leu-Leu-Ile-Ser-Trp-Asp-Ala-Pro-Ala-Val-Thr-Val-Arg-Tyr -Tyr-Arg-Ile-Thr-Tyr-Gly-Glu-Thr-Gly-Gly-Asn-Ser-Pro-Val-Gln-Glu-Phe-Thr-Va l-Pro-Gly-Ser-Lys-Ser-Thr-Ala-Thr-Ile-Ser-Gly-Leu-Lys-Pro-Gly-Val-Asp-Tyr-T hr-Ile-Thr-Val-Tyr-Ala-Val-Thr-Gly-Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro- Ile-Ser-Ile-Asn-Tyr-Arg-Thr-Glu-Ile-Asp-Lys-Pro-Ser-Gln-Met-OH. The polypeptide or a biologically active fragment thereof can be employed in the preparation of substrate designed for the attachment of cells thereto. It can be linked to the surface of a prosthetic device to particularly attract endothelial cells and fibroblastic cells.

Abstract: A polypeptide having the cell-attaching activity of fibronectin. The polypeptide has 108 amino acid residues and the formula: H-Ile-Gly-Gln-Gln-Ser-Thr-Val-Ser-Asp-Val-Pro-Arg-Asp-Leu-Glu-Val-Val-Ala- Ala-Thr-Pro-Thr-Ser-Leu-Leu-Ile-Ser-Trp-Asp-Ala-Pro-Ala-Val-Thr-Val-Arg-Tyr -Tyr-Arg-Ile-Thr-Tyr-Gly-Glu-Thr-Gly-Gly-Asn-Ser-Pro-Val-Gln-Glu-Phe-Thr-Va l-Pro-Gly-Ser-Lys-Ser-Thr-Ala-T r-Ile-Ser-Gly-Leu-Lys-Pro-Gly-Val-Asp-Tyr-Thr-Ile-Thr-Val-Tyr-Ala-Val-Thr- Gly-Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro-Ile-Ser-Ile-Asn-Tyr-Arg-Thr-Glu -Ile-Asp-Lys-Pro-Ser-Gln-Met-OH. The polypeptide or a biologically active fragment thereof, such as H-Tyr-Ala-Val-Thr-Gly-Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro-Ile-Ser-Ile- Asn-Tyr-Arg-Thr-Glu-Ile-Asp-Lys-Pro-Ser-Gln-Met-OH can be employed in the preparation of substrata designed for the attachment of cells thereto. A Cys-residue may optionally be attached at the C-terminus.

Abstract: A polypeptide having the cell-attaching activity of fibronectin. The polypeptide has 108 amino acid residues and the formula: H-Ile-Gly-Gln-Gln-Ser-Thr-Val-Ser-Asp-Val-Pro-Arg-Asp-Leu-Glu-Val-Val-Ala- Ala-Thr-Pro-Thr-Ser-Leu-Leu-Ile-Ser-Trp-Asp-Ala-Pro-Ala-Val-Thr-Val-Arg-Tyr -Tyr-Arg-Ile-Thr-Tyr-Gly-Glu-Thr-Gly-Gly-Asn-Ser-Pro-Val-Gln-Glu-Phe-Thr-Va l-Pro-Gly-Ser-Lys-Ser-Thr- la-Thr-Ile-Ser-Gly-Leu-Lys-Pro-Gly-Val-Asp-Tyr-Thr-Ile-Thr-Val-Tyr-Ala-Val -Thr-Gly-Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro-Ile-Ser-Ile-Asn-Tyr-Arg-Th r-Glu-Ile-Asp-Lys-Pro-Ser-Gln-Met-OH. The polypeptide or a biologically active fragment thereof can be employed in the preparation of substrata designed for the attachment of cells thereto. It can be linked to the surface of a prosthetic device to particularly attract endothelial cells and fibroblastic cells.

Abstract: Collagen affinity matrices are prepared, useful for separating collagenous substances from other high molecular weight proteinaceous substances. Fibronectin is fragmentated chemically or by enzymatic digestion, etc. Fragments of fibronectin, which retain the collagen-binding site but are severed from other binding sites of intact fibronectin, are selected and coupled to solid support material.