Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 15 to 23 amino acid residues in defined sequence
Reexamination Certificate
1999-09-28
2003-04-15
Romeo, David S. (Department: 1646)
Chemistry: natural resins or derivatives; peptides or proteins;
Peptides of 3 to 100 amino acid residues
15 to 23 amino acid residues in defined sequence
C530S327000, C435S007200, C435S325000
Reexamination Certificate
active
06548634
ABSTRACT:
FIELD OF THE INVENTION
The field of this invention is growth factors, particularly fibroblast growth factors.
BACKGROUND OF THE INVENTION
Basic fibroblast growth factors (bFGF)(also known as FGF2), so named because they contain a high number of basic amino acid residues (lysine, arginine and histidine) and therefore are cations at neutral pH, are potent mitogens for vascular endothelial cells in vitro and stimulate new capillary growth in vivo, i.e. they are angiogenic. Both human and bovine forms of basic FGF have been isolated, and the genes expressing these products have been cloned and sequenced. In addition, bFGF has been found to be expressed in a wide variety of tissue types, including pituitary, brain, adrenal gland, corpus luteum, retina, kidney, placenta, etc.
Patents of interest describing basic fibroblast growth factors include: U.S. Pat. Nos. 5,639,868; 5,604,293; 5,514,652; 5,478,740; 5,464,774; 5,459,015; 5,439,818; 5,352,589; 5,348,863; 5,331,095; 5,155,214; 5,143,829; 5,136,025; 5,130,418; 5,026,839; 4,994,559; 4,956,455.
Other References of interest include: Iwane et al, “
Expression of cDNA Encoding Human Basic Fibroblast Growth Factor
in
E. coli
,” Biochem. Biophys. Res. Comm. (1987)146:470-477; Thompson et al, “
Cloning, Recombinant Expression, and Characterization of Basic Fibroblast Growth Factor
,” Methods Enzymol. (1991)198:96-116; Fox et al, “
Production, Biological Activity, and Structure of Recombinant Basic Fibroblast Growth Factor and an Analog
. . . ,” J. Biol. Chem. (1988) 263:18452-18458; Thompson et al, “
The Disulfide Structure of Bovine Pituitary Basic Fibroblast Growth Factor
,” J. Biol. Chem. (1992) 267:2269-2273; Conn et al, “
The Isolation and Purification of Two Anionic Endothelial Cell Growth Factors from Human Brain
,” Biochem. Biophys. Res. Comm.(1984) 124:262-268; Bohlen et al., “
Acidic Fibroblast Growth Factor
(
FGF
)
from Bovine Brain: Amino
-
Terminal Sequence and Comparison with Basic FGF
,” EMBO J. (1985) 4:1951-1956; Abraham et al., J. Cell. Biochem. (1987) Supplement, vol. 0, No. 11, p. 50, Abst No. 191; Guillermo Gimenez-Gallego et al., Biochem. Biophy. Res. Communications (1986)135: 541-548; Esch et al. Proc. Natl. Acad. Sci. USA, (1985) 82: 6507-6511; Bohlen et al., Proc. Natl. Acad. Sci., USA, (1984) 81: 5364-5368; Gospodarowicz et al., Biochem. Biophy. Res. Communications (1985) 128: 554-562.
SUMMARY OF THE INVENTION
Peptidic compositions capable of binding to the FGF receptor, as well as fusion proteins and oligomers of the same, are provided. The subject peptidic compositions are characterized by having substantially no sequence homology to known naturally occurring FGF receptor ligands and may further exhibit one or more FGF activities. The subject fusion proteins comprise the peptidic composition joined to an oligomerization (e.g. dimerization) domain, either directly or through a linker group and optionally further include a heparin binding domain. The subject compositions find use in a variety of applications, including diagnostic and therapeutic applications.
REFERENCES:
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patent: 5684129 (1997-11-01), Fish
patent: 0 246 753 (1987-11-01), None
patent: 92/13958 (1992-08-01), None
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patent: WO 98/21237 (1998-05-01), None
patent: 00/03245 (2000-01-01), None
Yayon, A. et al. Isolation of peptides that inhibit binding of basic fibroblast growth factor to its receptor from a random phage-epitope library. Proc. Natl. Acad. Sci. USA 1993 90;10643-10647.*
Mikayama T. Molecular cloning and functional expression of a cDNA encoding glycosylation-inhibiting factor. Proc. Natl. Acad. Sci. USA vol. 90, pp. 10056-10060, 1993.*
Voet et al. Biochemistry. 1990. John Wiley & Sons, Inc.. pp. 126-128 and 228-234.*
Schettler, et al. Release of proteinases from stimulated polymorphonuclear leukocytes. Evidence for subclasses of the main granule types and their association with cytoskeletal components. Eur J Biochem. Apr. 10, 1991; 197(1):197-202.*
Ballinger, Marcus D., et al., “Semirational Design of a Potent, Artificial Agonist of Fibroblast Growth Factor Receptors,”Nature Biotechnology(Dec. 1999) vol. 17:1199-1204.
Yayon, Avner, et al., “Isolation of Peptides That Inhibit Binding of Basic Fibroblast Growth Factor to Its Receptor from a Random Phage-Epitope Library,”Proc. Natl. Acad. Sci. USA(Nov. 1993) vol. 90:10643-10647.
Ballinger Marcus
Kavanaugh Michael
Alexander Lisa E.
Blackburn Robert P.
Borden Paula A.
Chiron Corporation
Murphy Joseph F.
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