Growth factor modified protein matrices for tissue engineering

Details Growth factor modified protein matrices for tissue engineering Growth factor modified protein matrices for tissue engineering

2007-07-24

2007-07-24

Lankford, Jr., Leon B (Department: 1651)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C514S017400, C530S333000, C530S399000, C530S300000

Reexamination Certificate

active

10325021

ABSTRACT:
Proteins are incorporated into protein or polysaccharide matrices for use in tissue repair, regeneration and/or remodeling and/or drug delivery. The proteins can be incorporated so that they are released by degradation of the matrix, by enzymatic action and/or diffusion. As demonstrated by the examples, one method is to bind heparin to the matrix by either covalent or non-covalent methods, to form a heparin-matrix. The heparin then non-covalently binds heparin-binding growth factors to the protein matrix. Alternatively, a fusion protein can be constructed which contains a crosslinking region such as a factor XIIIa substrate and the native protein sequence. Incorporation of degradable linkages between the matrix and the bioactive factors can be particularly useful when long-term drug delivery is desired, for example in the case of nerve regeneration, where it is desirable to vary the rate of drug release spatially as a function of regeneration, e.g. rapidly near the living tissue interface and more slowly farther into the injury zone. Additional benefits include the lower total drug dose within the delivery system, and spatial regulation of release which permits a greater percentage of the drug to be released at the time of greatest cellular activity.

REFERENCES:
patent: 4613665 (1986-09-01), Larm
patent: 4810784 (1989-03-01), Larm
patent: 5100668 (1992-03-01), Edelman et al.
patent: 5171670 (1992-12-01), Kronenberg et al.
patent: 5202247 (1993-04-01), Kilburn et al.
patent: 5428014 (1995-06-01), Labroo et al.
patent: 5504001 (1996-04-01), Foster
patent: 5561982 (1996-10-01), Tunkel et al.
patent: 5582862 (1996-12-01), Reed et al.
patent: 5641670 (1997-06-01), Treco et al.
patent: 5693341 (1997-12-01), Schroeder et al.
patent: 5773577 (1998-06-01), Cappello
patent: 5814603 (1998-09-01), Oldenburg et al.
patent: 5840837 (1998-11-01), Krstenansky et al.
patent: 5877153 (1999-03-01), Harris et al.
patent: 5958874 (1999-09-01), Clark et al.
patent: 6054122 (2000-04-01), MacPhee et al.
patent: 6117425 (2000-09-01), MacPhee et al.
patent: 6136564 (2000-10-01), Kopetzki et al.
patent: 6197325 (2001-03-01), MacPhee et al.
patent: 6331422 (2001-12-01), Hubbell et al.
patent: 6559119 (2003-05-01), Burgess et al.
patent: 200 10 297 (2000-08-01), None
patent: WO 89/00051 (1989-01-01), None
patent: WO 90/05177 (1990-05-01), None
patent: WO 92/02620 (1992-02-01), None
patent: WO 92/09301 (1992-06-01), None
patent: WO 92/22312 (1992-12-01), None
patent: WO 94/20133 (1994-09-01), None
patent: WO 95/05396 (1995-02-01), None
patent: WO 95/23611 (1995-09-01), None
patent: WO 96/17633 (1996-06-01), None
patent: WO 00/64481 (2000-11-01), None
patent: WO 03/040235 (2003-05-01), None
Adams, et al., “Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis,”Genes&Development13:295-306 (1999).
Baumgartner, et al., “Constitutive expression of phVEGF165 after intramuscular gene transfer promotes collateral vessel development in patients with critical limb ischemia,”Circulation97:1114-1123 (1998).
Blaess, et al., “Structural analysis of the sixth immunoglobulin-l ike domain of mouse neural cell adhesion molecule L1 and its interactions with αvβ3, αllbβ3, and α5 β1 integrins,”J Neurochem, 71:2615-2625 (1998).
Brooks, et al., “Requirement of vascular integrin αvβ3 for angiogenesis,”Science264:569-571 (1994).
Bruckner, “EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains,”Neuron22:511-524 (1999).
Calderwood, et al., “Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling,”J Biol Chem275:22607-22610 (2000).
Camarata, et al., “Sustained Release of Nerve Growth Factor from Biodegradable Polymer Microspheres,”Neurosurgery30(3) 313-319 (1992).
Cardin, et al., “Molecular Modeling of Protein-Glycosaminoglycan Interactions,”Arteriosclerosis9:21-32 (1989).
Conover, et al., “Disruption of Eph/ephrin signaling affects migration and proliferation in the adult subventricular zone,”Nature Neuroscience3(11):1091-3324 (2000).
Dalva, et al., “EphB receptors interact with NMDA receptors and regulate excitatory synapse formulation,”Cell103:945-956 (2000).
Dedhar & Hannigan, “Integrin cytoplasmic interactions and bidirectional transmembrane signaling,”Current Opinion in Cell Biology8:657-669 (1996).
Downs, et al., “Calcium Alginate Beads as a Slow-Release System for Delivering Angiogenic Molecules in Vivo and In Vitro,”Journal of Cellular Physiology152:422-429 (1992).
Eliceiri & Cheresh, “The role of αv integrins during angiogenesis: insights into potential mechanisms of action and clinical development,”Journal of Clinical Investigation103:1227-1230 (1999).
Fasol, et al., “Experimental use of a modified fibrin glue to induce site-directed angiogenesis from the aorta to the heart,” Journal of Thoracic and Cardiovascular Surgery 107:1432-9 (1994).
Felding-Habermann, et al., “A single immunoglobulin-like domain of the human neural cell adhesion molecule L1 supports adhesion by multiple and platelet integrins,”J Cell Biol139:1567-1581 (1997).
Feng, et al., “Roles for ephrins in positionally selective synaptogenesis between motor neurons and muscle fibers,”Neuron25:295-306 (2000).
Ferrara & Alitalo, “Clinical applications of angiogenic growth factors and their inhibitorsl”Nature Medicine5:1359-1364 (1999).
Ferrara, “Molecular and biological properties of vascular endothelial growth factor,” J Mol Med 77:527-543 (1999).
Folkman, “Angiogenesis in cancer, vascular , rheumatoid and other disease,”Nature Medicine1:27-31 (1995).
Gale, et al., “Ephrin-B2 selectivity marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells,”Developmental Biology230:151-160 (2001).
Griesler, et al., “Enhanced endothelial of expanded polyethrafluoroethylene grafts by fibroblast growth factor type 1 Pretreatment,”Surgery112:244-255 (1992).
Hall, “Molecular properties of fibrin-based matrices for promotion of angiogenesis in vitro,”Microvascular Research62:315-326 (2001).
Hall, et al., “Trimerization of cell adhesion molecule L1 mimics clustered L1 expression on the cell surface: Influence on L1-Ligand interactions and on promotion of neurite outgrowth,”J of Neurochemistry75:336-346 (2000).
Hammond, et al., “Management of coronary artery disease: Therapeutic options in patients with diabetes,”JACC36:355-65 (2000).
Houle & Johnson, “Nerve growth factor (NGF)-treated nitrocellulose enhances and directs the regeneration of adult rat dorsal root axons through intraspinal neural tissue transplants,”Neuroscience Letters103:17-23 (1989).
Hubbell, “Bioactive biomaterials”Curr. Opinion Biotechnol. 10(2): 123-129 (1999).
Humphries, “Integrin activation: the link between ligand binding and signal transduction,”Curr Opin Cell Biol8:632-640 (1996).
Ilan, et al., “Distinct signal transduction pathways are utilized during the tube formation and survival phases of in vitro angiogenesis,”J of Cell Science111:3621-3631 (1998).
Ingber & Folkman, “How does extracellular matrix control capillary morphogenesis?” Cell 58:803-805 (1989).
Kang, et al., “Selective stimulation of endothelial cell proliferation with inhibition of smooth muscle cell proliferation by fibroblast growth factor-1 plus heparin delivered from glue suspensions,”Surgery118:280-287 (1995).
Lee, et al., “Analysis of affinity and structural selectivity in the binding of proteins to glycosaminoglycans: Development of a sensitive electrophoretic approach,”Biochemistry88:

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