Polypeptide

Details Polypeptide Polypeptide

1982-08-04

1985-05-21

Apley, Richard J.

Chemistry of carbon compounds

Miscellaneous organic carbon compounds

C-metal

3 14, 2601125R, 514 12, A61F 100, A61K 3700, C07C10352, C07G 700

Patent

active

045176868

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.

REFERENCES:
Grinnell, F. et al., Distribution of Fibronectin During Wound Healing in Vivo, J. Invest. Dermatol. 76:181-189, 3/1981.
Seitz, T. L. et al., Effect of Fibronectin on the Adhesion of an Established Cell Line to a Surface Reactive Biomaterial, J. Biomed. Res. 16,3:195-207, 5/1982.
Clark, R. A. F. et al., Fibronectin is Produced by Blood Vessels in Response to Injury, J. Exp. Med. 156:646-651, 8/1982.
Engvall, et al., Affinity Chromatography of Collagen on Collagen-Binding Fragments of Fibronectin, Collagen Rel. Res., vol. 1/1981, pp. 505-516.
McDonagh, R. P., et al., Amino Acid Sequence of the Factor XIII.sub.a Acceptor Site in Bovine Plasma Fibronectin, Febs Letters, 127:174-178, 1981.
Vibe-Pedersen, Karen, et al., Amino Acid Sequence of a Peptide from Bovine Plasma Fibronectin Containing a Free Sulfydrayl Group (Cysteine), Febs Letters 142:26-30, 1982.
Ruoslahti, et al., Fibronectin: Current Concept of Its Structure and Functions, Coll. Res., vol. 1/1981, pp. 95-128.
Engvall, et al., Binding of Soluble Form of Fibroblast Surface Protein, Fibronectin, to Collagen, Int. J. Cancer: 20,1-5, (1977).
Ruoslahti et al., Interaction of Fibronectin with Antibodies and Collagen in Radioimmunoassay, Biochimica et Biophysica Acta, 534, (1978), 210-218.
Engvall, et al., Nonhelical, Fibronectin-Binding Basement-Membrane Collagen from Endodermal Cell Culture, Cell, vol. 29, 475-482, Jun. 1982.
Ehrismann, et al., Arrangement of Attachment-Promoting, Self-Association, and Heparin-Binding Sites in Horse Serum Fibronectin, J. of Biol. Checm., vol. 257, No. 13, Jul. 10, pp. 7381-7387, 1982.
Ruoslahti, Erkki, et al., Alignment of Biologically Active Domains in the Fibronectin Molecule, J. Biol. Chem., 256:7277-7281, 1981.
Pande, Hema and John E. Shively, NH.sub.2 -Terminal Sequences of DNA-Heparin-, and Gelatin-Binding Tryptic Fragments from Human Plasma Fibronectin, Arch. Bioch. Biophy. 213:258-265, 1982.
Pierschbacher, Michael D., et al., The Cell Attachment Domain of Fibronectin, J. Bio. Chem. 257:9593-9597, 1982.

Affiliated with

Also associated with

Rating

Polypeptide does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Polypeptide, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Polypeptide will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-1530694