Tetrapeptide

Prosthesis (i.e. – artificial body members) – parts thereof – or ai – Implantable prosthesis

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623 1, 623 66, 2601125R, 128 1R, 128334R, 424177, A61F 100, A61K 3700, C07C10352, C07G 700

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active

045780790

ABSTRACT:
The peptide X-Arg-Gly-Asp-R-Y wherein X is H or at least one amino acid and Y is OH or at least one amino acid, and R is an amino acid selected from Thr or Cys, or other amino acid, having the same cell-attachment activity as fibronectin and the peptide X-Arg-Gly-Asp-Ser-Y, wherein X and Y, having said activity are disclosed.

REFERENCES:
Seitz et al., "Effect of Fibronectin . . . "; J. of Biomed. Mat. Res.; vol. 16 #3; pp. 195-207; 5/1982.
Hynes, et al., Cell Surface Fibronectin and Oncogenic Transformation, J. Supramolecular Structure 11:95-104 (1979).
Hahn, Lian-Hsien E. and Kenneth M. Yamada, Isolation and Biological Characterization of Active Fragments of the Adhesive Glycoprotein Fibronectin, Cell18:1043-1051, 1979.
Sekiguchi, Kiyotoshi and Sen-Itiroh Hakomori, Functional Domain Structure of Fibronectin, Proc. Natl. Acad. Sci. 77:2661-2665, 1980.
Grinnell, Frederick, et al., Distribution of Fibronectin During Wound Healing in Vivo. J. Invest. Dermatol. 76:181-189, 1981.
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.
Ruoslahti, Erkki, et al., Alignment of Biologically Active Domains in the Fibronectin Molecule, J. Biol. Chem. 256:7277-2781, 1981.
Pande, Hema, et al., Comparative Structural Studies of Human Plasma and Amniotic Fluid Fibronectins, Bioch. Biophy. Res. Comm. 101:265-272, 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. Biol. Chem. 257:9593-9597, 1982.
Vibe-Pedersen, Karen, et al., Amino Acid Sequence of a Peptide from Bovine Plasma Fibronectin Containing a Free Sulfhydryl Group (Cysteine) Febs. Letters 142:26-30, 1982.
Sekiguchi, Kiyotoshi, et al., Monoclonal Antibodies Directed to Two Different Domains of Human Plasma Fibronectin: Their Specificities, Fed. Eur. Bich. Soc. 142:243-246, 1982.
Ehrismann, Ruth, et al., Arrangement of Attachment-Promoting, Self-Association, and Heparin-Binding Sites in Horse Serum Fibronectin, J. Biol. Chem. 257:7381-7387, 1982.
Clark, Richard A. F., et al., Fibronectin is Produced by Blood Vessels in Response to Injury, J. Exp. Med. 156:646-651, 1982.
Hynes, Richard O. and Kenneth M. Yamada, Fibronectins: Multifunctional Modular Glycoproteins, J. Cell. Biol. 95:369-377, 1982.
Petersen, Torbene, et al., Partial Primary Structure of Bovine Plasma Fibronectin: Three Types of Internal Homology, Proc. Natl. Acad. Sci. 80:137-141, 1983.
Grinnell, Frederick, Cell Attachment and Spreading Factors in Growth and Maturation Factors (Dr. Gordon Guroff, Ed.) John Wiley & Sons, Inc., 1983.
Hayashi, Masao and Kenneth M. Yamada, Domain Structure of the Carboxyl-Terminal Half of Human Plasma Fibronectin, J. Biol. Chem. 258:3332-3340, 1983.
Kornblihtt, Alberto R., et al., Isolation and Characterization of cDNA Clones for Human and Bovine Fibronectins, Proc. Natl. Acad. Sci. 80:3218-3222, 1983.
Pierschbacher, Michael, et al., Synthetic Peptide With Cell Attachment Activity of Fibronectin, Proc. Natl. Acad. Sci. 80:1224-1227, 1983.

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