Education:

Graduate:

Ph.D. in Biochemistry; University of South Dakota, 1976;
Advisor: Dr. Robert J. Peanasky.
Thesis: Ascaris lumbricoides var suum Proteins (Inhibitors) Which Bind Specifically to Carboxypeptidases A and B: Isolation, Characterizations, Reactions and a Mode of Interaction Based on Studies with Carboxypeptidases A Modified at the Active Site.

Post-Graduate:

• NIH Postdoctoral Fellow, Laboratory of Chemical Biology, National Institute of Arthritis, Metabolic and Digestive Disorders, The National Institutes of Health, Bethesda, MD. 1978-1980
• Postdoctoral Research Associate, Department of Chemistry, Division of Biochemistry, Purdue University, West Lafayette, IN, 1976-1978

Employment History:

• Professor of Biochemistry, Department of Biochemistry, Rush Medical College at Rush-Presbyterian-St Luke's Medical Center, 1995-2002, Associate Professor 1988-1992.
• Director of Educational Programs, Department of Biochemistry, 2000-2002. Assoc Director 1999-2000, Asst Director 1992-1999.
• Dr. Ralph and Marian C. Falk Professor of Biochemistry Endowed Chair at Rush University, 1996-2002.
• Senior Biochemist, Pharmaceutical Products Division, Pharmaceutical Discovery, Abbott Laboratories, Abbott Park, IL, 1986-1988.
• Associate Professor, Department of Medicine, University of Wisconsin- Milwaukee Clinical Campus, Mt. Sinai Medical Center, Milwaukee, WI., 1986-88. Asst Prof 1984-1986.
• Feb 1980-Nov 1981: Staff Cancer Research Scientist (Assistant Professor), Department of Molecular Biology, Roswell Park Memorial Institute, Buffalo, NY, 1980-86.

Teaching Experience:

Past course director for graduate courses in advanced biochemistry topics including protein structure, structure function correlates and study methods, past course director for undergraduate courses in biochemistry with emphasis on metabolic biochemistry, past course director for Biochemistry for Medical Students course and former instructor in problem based medical biochemistry curricula.

Selected Honors:

• Dr. Ralph and Marian C. Falk Professor of Biochemistry Endowed Chair at Rush University, 1996-2002. Recognition for contributions to study of Osteoarthritis and Cartilage Physiology.
• Awarded permanent membership in the "Frontiers in Bioscience Society of Scientists" in 1999.

Research:

Osteoarthritis is caused by a gradual self-destruction of cartilage, the tough yet elastic tissue that covers the ends of long bones and cushions joints. This is a very common disease and can be initiated by traumatic injury and perhaps, in part, by the aging process. At least 50 million adults in the United States alone and close to 15% of the world's adult population suffer from this painful and disabling disease. There are not yet any known treatments or drugs that effectively slow the progression of the disease. Most of the drugs used merely decrease the pain that results when the cartilage wears away and bone rubs against bone.

A major reason for the lack of suitable treatments is that the causes of osteoarthritis are not well understood. While we understand many of the later stage biochemical events that occur during later stages of the disease, we do not know the initial cause(s) of osteoarthritis, nor how to stop the early processes. We have discovered a novel pathway that may be one of the initiating factors in osteoarthritis, if not a system of amplification that contributes to progression of the disease. We have found that proteolysis of the extracellular protein, fibronectin, which is found in the cartilage tissue surrounding the chondrocyte cells, results in small fibronectin fragments, which have the capability of enhancing damage as well as altering repair responses of the cartilage, by interfering with the activities of the parent molecule. The relevance of this pathway is supported by observations of elevated levels of fibronectin fragments in arthritic fluids and cartilage. Interestingly, the fragments can also amplify reparative responses and thus may be key metabolic regulators that the damaged tissue uses to accelerate tissue clearance as well as subsequent attempted tissue repair or remodeling. Mechanistically, the fragments at low concentrations enhance activation of growth factors but at higher concentrations as found in disease, enhance expression of catabolic cytokines and matrix metalloproteinases and alter synthesis of matrix proteins, activities that all contribute to a massive degree of matrix damage.

Our research focuses on the physiologic and intracellular signaling mechanisms by which these fibronectin fragments regulate cartilage homeostasis.. Specifically, we are investigating how these fragments are generated during disease, the types of cellular receptors they bind, how they initiate altered intracellular signaling, what types of intracellular kinases are activated and the genes that are upregulated. We have also begun to compare our fibronectin fragment pathway to another relevant pathway, that caused by degradation of cartilage collagen into active fragments. Our ultimate objective is to describe a global mechanism by which degradation products of the extracellular matrix are utilized to amplify the catabolic response as well as reparative response and regulate cartilage homeostasis. This knowledge will be useful in determining what types of chondroprotective agents have therapeutic potential using these two systems as in vitro models of osteoarthritic cartilage damage.  These models are also being used to study the innate reparative pathways of damaged cartilage and investigate the mechanisms of selected chondroprotective agents, including nutraceutical compounds

Partial History of Funding:

• Project leader and Core Director in NIH Program Project, "Correlation of Structural and Functional Properties of Fibronectins", 1983 - 1987.
• Project leader in NIH Specialized Center of Research (SCOR) in Osteoarthritis grant, "Osteoarthritis: A Continuum" 1987 - 2002.
• Past recipient of grants from Arthritis Foundation, American Heart Association, Scleroderma Foundation, Hoechst Werk Kalle Albert Co., Abbott Laboratories, Proctor and Gamble Corp. and Glaxo-Smith and Kline.
• Recipient of grants from Seikagaku Corp, 1992-2002, "Investigation of Cartilage Reparative Mechanisms of High Molecular Weight Hyaluronan.

Selected Publications:

1. Homandberg, G.A. and Peanasky, R.J. Characterization of proteins from ascaris lumbricoides which bind specifically to carboxypeptidase. J. Biol. Chem. 251, 2226-2233, 1976.
2. Homandberg, G.A., Mattis, J.A. and Laskowski, M., Jr. Synthesis of peptide bonds by proteinases: the addition of organic cosolvents shift peptide bond equilibria toward synthesis. Biochemistry 17, 5220-5227, 1978.
3. Homandberg, G.A. and Laskowski, M., Jr. Enzymatic re-synthesis of the hydrolyzed peptide bond(s) in ribonuclease S. Biochemistry 18, 586-592, 1979.
4. Homandberg, G.A., Minor, S.T. and Peanasky, R.J. Modification of carboxypeptidase a active site residue glu-270 prevents interaction with a protein inhibitor from Ascaris. Biochim. Biophys. Acta 612, 384-394, 1980.
5. Homandberg, G.A. and Chaiken, I.M. Trypsin-catalyzed conversion of staphylococcal nuclease-t fragment complexes to covalent forms. J. Biol. Chem. 255, 4903-4909, 1980.
6. Komoriya, A., Homandberg, G.A. and Chaiken, I.M. Enzyme-catalyzed formation of semisynthetic staphylococcal nuclease using a new synthetic fragment, [Gly 48] synthetic-(6-49). Int. J. Peptide Protein Res. 16, 433-439, 1980.
7. Juillerat, M. and Homandberg, G.A. Clostripain-catalyzed reformation of a peptide bond in a cytochrome c-fragment complex. Int. J. Peptide Protein Res. 18, 335-342, 1981.
8. Homandberg, G.A., Komoriya, A. and Chaiken, I.M. Enzymatic condensation of non-associated peptide fragments using a molecular trap. Biochemistry 21, 3385-3389, 1982.
9. Homandberg, G.A. Chemical modification of mouse b-glucuronidase implicates lysyl, carboxyl and tyrosyl residues as catalytically essential and causes reversible dissociation of the subunits. Biochem. Biophys. Res. Commun. 105, 1109-1114, 1982.
10. Tooney, N.M., Amrani, D.L., Homandberg, G.A., McDonald, J.A. and Mosesson, M.W. Near ultraviolet circular dichroism spectroscopy of plasma fibronectin and fibronectin fragments. Biochem. Biophys. Res. Commun. 108, 1085-1091, 1982.
11. Kanmera, T., Homandberg, G.A., Komoriya, A. and Chaiken, I.M. Minimum information content and formation of interacting ribonuclease fragment complexes. Int. J. Peptide Protein Res. 21, 74-83, 1983.
12. Tooney, N.M., Amrani, D.L., Homandberg, G.A. and Mosesson, M.W. CD studies of fibronectin structure. Biochem. J. 41, 390, 1983.
13. Amrani, D.L., Homandberg, G.A., Tooney, N.M., Wolfenstein-Todel, C. and Mosesson, M.W. Separation and analysis of the major forms of plasma fibronectin. Biochim. Biophys. Acta 748, 308-320, 1983.
14. Mosesson, M.W., Homandberg, G.A. and Amrani, D.L. Human platelet fibrinogen gamma chain structure. Blood 63, 990-995, 1984.
15. Peanasky, R.J., Bente, Y., Homandberg, G.A., Minor, S.T. and Babin, D.R. The isoinhibitors of chymotrypsin/elastase from ascaris lumbricoides: the reactive site. Arch. Biochem. Biophys. 232, 135-142, 1984.
16. Homandberg, G.A., Amrani, D.L., Evans, D.B., Kane, C.M., Ankel, E. and Mosesson, M.W. Preparation of functionally intact monomers by limited disulfide reduction of plasma fibronectin dimers. Arch. Biochem. Biophys. 238, 652-663, 1985.
17. Homandberg, G.A., Evans, D.B., Kramer, J. and Erickson, J.W. Interaction between fluorescently-labeled fibronectin fragments studied by gel filtration HPLC. J. Chromatogr. 327, 343-349, 1985.
18. Homandberg, G.A., Williams, J.E., Evans, D.B. and Mosesson, M.W. Evidence that rat platelet fibrinogen molecules lack the gamma chain variant found in plasma fibrinogen molecules. Thrombosis Research 38, 203-209, 1985.
19. Homandberg, G.A., Evans, D.B., Kane, C.M. and Mosesson, M.W. Amino acid sequence of the carboxyl-terminal regions of rat plasma fibrinogen ga and g' chains. Thrombosis Research 39, 263-269, 1985.
20. Homandberg, G.A., Williams, J.E., Grant, D., Schumacher, B. and Eisenstein, R. Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth. American Journal of Pathology 120, 327-332, 1985
21. Ankel, E.G., Homandberg, G.A., Tooney, N.M. and Lai, C-S. Heparin modulates conformational states of plasma fibronectin: an ESR spin label approach. Arch Biochem Biophys, 238, 652-663, 1985.
22. Homandberg, G.A. and Erickson, J.W. A model of fibronectin tertiary structure based on studies of interactions between fragments. Biochemistry 25, 6917-6925.
23. Homandberg, G.A., Bjerke, J., Grant, D., Christianson, G. and Eisenstein, R. Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth: structure-function correlates. Biochim Biophys Acta 874, 61-71, 1986.
24. Mosesson, M.W., DiOrio, J., Muller, M.F., Shainoff, J.R., Siebenlist, K.R., Amrani, D.L., Homandberg, G.A., Soria, J., Soria, C. and Samama, M. Studies on the ultrastructure of fibrins lacking fibrinopeptide b (b-fibrin) Blood 69, 1073-1081, 1987.
25. Lai, C-S., Homandberg, G.A., Miziorko, H. and Wolff, C. Tryptophan fluorescence studies of plasma fibronectin. effects of environmental factors. Biopolymers 26, 1381-1389, 1987.
26. Homandberg, G.A. Characterization of the interactions of an amino-terminal fibronectin fragment with the native molecule: implications for polymerization of fibronectin. Biopolymers 26, 2087-2098, 1987.
27. Homandberg, G.A. Inaccessibility to ligands of the amino-terminal region of plasma fibronectin. Thrombosis Research 48, 321-327, 1987.
28. Homandberg, G.A. and Bjerke-Kramer, J. Thrombospondin binds to amino-terminal fragments of plasma fibronectin. Thrombosis Research 48, 329-335, 1987.
29. Lohr, K.M., Homandberg, G.A. and Kurth, C.A. Amino-terminal fragments of fibronectin mediate selective monocyte recruitment. Clin Res 35, 855A, 1987.
30. Denninger, M.H., Jandrot-Perrus, M., Elion, J., Bertrand, O., Homandberg, G.A., Mosesson, M.W. and Guillin, M.C. ADP-induced platelet aggregation depends on the conformation or availability of the terminal gamma chain sequence of fibrinogen. study of the reactivity of fibrinogen Paris 1. Blood 70, 558-563, 1987.
31. Homandberg, G.A., Litwiller, R.D. and Peanasky, R.J. Carboxypeptidase inhibitors from ascaris suum: the primary structure. Arch. Biochem. Biophys. 270, 153-161, 1989.
32. Homandberg, G.A. and Wai, T. Comparison of affinities of urokinase and tissue plasminogen activator for fibrin clots. Thrombosis Research 55, 493-501, 1989.
33. Homandberg, G.A., Dunn, B., Grant, D., Bartley, D. and Eisenstein, R. Synthetic peptides of the amino-terminus of fibronectin inhibit endothelial cell growth. Cell Biology International Reports 13, 891-900, 1989.
34. Homandberg, G.A. and Wai, T. Reduction of disulfides in urokinase and insertion of a synthetic peptide. Biochim. Biophys. Acta 1038, 209-215, 1990.
35. Homandberg, G.A. and Wai, T. Insertion of fibrin peptides into urokinase enhances fibrin affinity. Thrombosis Research 58, 403-412, 1990.
36. Lohr, K.M., Kurth, C.A., Xie, D.L., Seyer, J.M. and Homandberg, G.A. The amino-terminal 29 - and 72 kd fragments of fibronectin mediate selective monocyte recruitment. Blood 76, 2117-2124, 1990.
37. Kang, K., Schwarz, D., Aresenis, H, Sky-Peck, H., Kuettner, K.E. and Homandberg, G.A. Human PMN elastase: a novel method of purification using adsorption to an HPLC gel filtration column and investigation of its metalloenzyme properties. J. Chromatography 567, 57-63, 1991.
38. Homandberg, G.A., Meyers, R. and Williams, J. Fibronectin fragment mediated damage to joint tissue. Anat Rec 229, 39-40, 1991.
39. Homandberg, G.A., Meyers, R., Tripier, D. and Kuettner, K.E. Isolation and characterization of an abundant elastase inhibitor from nacl extracts of bovine nasal and articular cartilage. Conn Tiss Res 28, 289-305, 1992.
40. Homandberg, G.A., Meyers, R. and Xie, D.L. Fibronectin fragments cause chondrolysis of bovine articular cartilage slices in culture. J. Biol. Chem. 267, 3597-3604, 1992.
41. Xie, D.L., Meyers, R. and Homandberg, G.A. Fibronectin fragments in osteoarthritic synovial fluid. J. Rheumatol. 19, 1448-1452, 1992.
42. Xie, D.L., Meyers, R. and Homandberg, G.A. Fibronectin fragments cause elastase release from attached monocytes. Blood 81, 186-192, 1993.
43. Homandberg, G.A., Meyers, R. and Williams, J. Intra-articular injection of fibronectin fragments causes severe depletion of cartilage proteoglycan in vivo. J. Rheumatol 20, 1378-1382, 1993.
44. Xie, D.l. and Homandberg, G.A. Fibronectin fragments bind and penetrate cartilage tissue resulting in protease expression and cartilage damage. Biochim Biophys Acta 1182, 189-196, 1993.
45. Xie, D.L., Hui, F. and Homandberg, G.A. Fibronectin fragments alter matrix protein synthesis in cartilage in vitro. Arch Biochem Biophys 307, 110-118, 1993.
46. Homandberg, G.A. and Hui, F. Arg-Gly-Asp-Ser peptide analogs suppress cartilage chondrolysis activities of integrin-binding and non-binding fibronectin fragments. Arch Biochem Biophys 310, 40-48, 1994.
47. Xie, D.L., Hui, F., Meyers, R. and Homandberg, G.A. Cartilage chondrolysis by fibronectin fragments is associated with release of several proteinases; stromelysin plays a major role in chondrolysis. Arch Biochem Biophys 311, 205-212, 1994.
48. Homandberg, G.A. and Hui, F. High concentrations of fibronectin fragments cause short term catabolic effects in cartilage tissue while lower concentrations cause continuous anabolic effects. Arch Biochem Biophys 311, 213-218, 1994.
49. Chow, G., Knudson, C.B., Homandberg, G.A. and Knudson, W. Increased expression of CD44 in bovine articular chondrocytes by catabolic cellular mediators. J. Biol. Chem. 270, 27734-27741, 1995.
50. Bewsey, K., Wen, C., Purple, C. and Homandberg, G.A. Fibronectin fragments induce the expression of stromelysin-1 mRNA and protein in bovine chondrocytes in monolayer culture Biochim Biophys Acta 1317, 55-64, 1996.
51. Homandberg, G.A., Hui, F. and Wen, C. Association of proteoglycan degradation with catabolic cytokine and stromelysin release from cartilage cultured with fibronectin fragments. Arch. Biochem. Biophys 334, 325-331, 1996.
52. Homandberg, G.A., Hui, F. and Wen, C. Fibronectin fragment mediated cartilage chondrolysis: (I) suppression by anti-oxidants. Biochim Biophys Acta 1317, 134-142, 1996.
53. Homandberg, G.A. Hui, F. and Wen, C. Fibronectin fragment mediated cartilage chondrolysis: (II) reparative effects of anti-oxidants. Biochim Biophys Acta. 1317, 143-148, 1996.
54. Homandberg, G.A., Hui, F., Wen, C., Purple, C., Bewsey, K., Koepp, H., Huch, K. and Harris, A. Fibronectin fragment induced cartilage chondrolysis is associated with release of catabolic cytokines. Biochemistry Journal 321, 751-757, 1997.
55. Homandberg, G.A., Hui, F., Williams, J.M. and Kuettner, K.E. Hyaluronic acid suppresses fibronectin fragment mediated cartilage chondrolysis in vitro. Osteoarthritis Cart 5, 309-319, 1997.
56. Williams, J.M., Plaza, V., Wen, C. and Homandberg, G.A. Hyaluronic acid suppresses fibronectin fragment mediated cartilage chondrolysis II in vivo. Osteoarthritis Cart 5, 235-240, 1997.
57. Homandberg, G.A., Hui, F., Manigalis, C. and Shrikhande, A. Cartilage chondrolysis caused by fibronectin fragments causes cleavage of aggrecan at the same sites as in osteoarthritis Osteoarthritis Cart 5, 450-453, 1997.
58. Homandberg, G.A., Wen, C. and Hui, F. Agents that block fibronectin fragment mediated cartilage damage also promote repair. Inflammation Research 46, 467-471, 1997.
59. Homandberg, G.A., Wen, C. Exposure of cartilage to a fibronectin fragment amplifies catabolic processes while also enhancing anabolic processes to limit damage. J Orthop Res 16, 237-246, 1998.
60. Homandberg, G.A., Hui, F, and Wen, C. Cartilage damaging activities of fibronectin fragments derived from cartilage and synovial Fluids. Osteoarthritis Cart 6, 231-244, 1998.
61. Kang, Y., Koepp, H., Cole, A.A., Kuettner, K.E. and Homandberg, G.A. Cultured human ankle and knee cartilage differ in susceptibility to damage mediated by fibronectin fragments. J Orthopaedic Research 16, 551-556, 1998.
62. Koepp, H.E., Sampath, K.T., Kuettner, K.E. and Homandberg, G.A. Osteogenic protein-1 (OP-1) blocks cartilage damage caused by fibronectin fragments and promotes repair by enhancing proteoglycan synthesis. Inflammation Research 48, 199-204, 1999.
63. Kang, Y., Williams, J., Koepp, H., Kuettner, K.E. and Homandberg, G.A. Hyaluronan suppresses fibronectin fragment mediated damage to human cartilage explant cultures by enhancing proteoglycan synthesis. J. Orthop Res 17, 858-869, 2000.
64. Homandberg, G.A. Cartilage damage by matrix degradation products: fibronectin fragments. Clin Orthop Rel Res 391S, S100-S107, 2001.
65. Homandberg, G.A., Kang, Y., Zhang, J., Cole, A.A. and Williams, J.M. A single injection of fibronectin fragments into rabbit knee joints enhances catabolism in the articular cartilage followed by reparative responses but also induces systemic effects in the non-injected joints. Osteoarthritis Cart 9, 673-683, 2001.
66. Homandberg, G.A., Costa, V. and Wen, C. Anti-Sense oligonucleotides to the alpha5 integrin subunit suppress cartilage chondrolytic activities of amino-terminal fibronectin fragments. Osteoarthritis Cart 10, 381-393, 2002.
67. Purple, C.R., Untermann, T.G., Pichika, R.and Homandberg, G.A. Fibronectin Fragments Upregulate Insulin-like Growth Factor Binding Proteins in Chondrocytes. Osteoarthritis Cart 10, 734-46, 2002.
68. Homandberg, G.A., Costa, V. and Wen, C. Fibronectin fragments active in chondrocytic chondrolysis can be chemically crosslinked to the alpha5 integrin receptor subunit. Osteoarthritis Cart 10, 938-949, 2002
69. Williams, J.M., Zhang, J., Kang, Y. and Homandberg, G.A. Effect of intra-articular injection of high molecular weight hyaluronic acid in joints of skeletally mature rabbits on protection against cartilage chondrolysis induced by fibronectin fragments. Osteoarthritis Cart 11, 44-49, 2002.
70. Homandberg, G.A., Ummadi, V. and Kang, H. High Molecular Weight Hyaluronan Promotes Repair Of IL-1b Damaged Cartilage Explants From Both Young And Old Bovines. Osteoarthritis Cart 11, 177-186, 2003.
71. Dang, Y.W., Cole, A.A. and Homandberg, G.A. Comparison of the Catabolic Effects Of Fibronectin Fragments (Fn-F) In Human Knee And Ankle Cartilages. Osteoarthritis Cart 11, 538-547, 2003.
72. Homandberg, G.A., Ummadi, V.J., Kang, H. The Role of Insulin-like Growth Factor-I in Hyaluronan Mediated Repair of Cultured Cartilage Explants.  Inflammation Research 53, 396-404, 2004.
73. Pichika, R. and Homandberg, G.A. Fibronectin Fragments Elevate Nitric Oxide (NO) And Inducible No Synthetase (iNOS) Levels In Bovine Cartilage And INOS Inhibitors Block Fibronectin Fragment Mediated Damage And Promote Repair.  Inflammation Research 53, 405-412, 2004.
74. Homandberg, G.A., Ummadi, V..J and Kang, H. Hyaluronan Enhances Cartilage Repair Through Low Grade Tissue Remodeling Involving Cytokines and Matrix Metalloproteinases. Inflammation Research 53, 534-543, 2004.
75. Aota, Y., An, H.S., Homandberg, G.A., Thonar, E.J., Andersson, G.B., Pichika, R., Masuda, K. Differential effects of fibronectin fragments on the proteoglycan metabolism of intervertebral disc cells. A comparison with articular chondrocytes.  Spine 30:722-728, 2005.
76. Homandberg, GA, Guo, D., Ray, L. and Ding, L.  Mixtures Of Glucosamine And Chondroitin Sulfate Reverse Fibronectin Fragment Mediated Damage To Cartilage More Effectively Than Either Agent Alone. Osteoarthritis and Cartilage (in press).

Invited Book Chapters:

1. Peanasky, R.J., Abu-Erreish, G.M., Gaush, C.R., Homandberg, G.A., O'Heeron, D., Linkenheil, R.K., Kucich, U. and Babin, D.R. (1974), Proteinase inhibitors from ascaris lumbricoides: properties and their physiological role in Bayer Symposium V, Proteinase Inhibitors (Fritz, H., Tschesche, H., Greene, L.J. and Truscheit, E., eds.), Springer-Verlag, Berlin, Heidelberg, New York, pp 649-666.
2. Homandberg, G.A. and Peanasky, R.J. (1976) Interaction of exopeptidases with specific proteins from ascaris lumbricoides in Protides of the Biological Fluids, XXIII (Peeters, H., ed) Pergamon Press, Oxford, New York, pp 279-284.
3. Homandberg, G.A., Komoriya, A., Juillerat, M. and Chaiken, I.M. (1979) Enzymatic conversion of selected noncovalent complexes of native or synthetic fragments to covalent forms in Peptides: Structure and Biological Function---Proceedings of the Sixth American Peptide Symposium (Gross, E. and Meienhofer, J., eds) Pierce Chemical Company, Rockford, Illinois, pp 587-600.
4. Chaiken, I.M., Komoriya, A. and Homandberg, G.A. (1979) Protein semi-synthesis and the chemical basis of folding and function in Peptides: Structure and Biological Function---Proceedings of the Sixth American Peptide Symposium (Gross, E. and Meienhofer, J., eds) Pierce Chemical Company, Rockford, Illinois, pp 597-600.
5. Komoriya, A., Homandberg, G.A. and Chaiken, I.M. (1981) Enzymatic fragment condensation using kinetic traps in Peptides: 1980 (Brunfelt, K., ed) Scriptor Press, Copenhagen, p 378.
6. Mosesson, M.W., Homandberg, G.A. and Amrani, D.L. (1985) Evidence that the gamma chain population of human platelet fibrinogen lacks the gamma variant that is present in plasma fibrinogen in Fibrinogen, Structural Variants and Interactions, Vol 3. (Henschen, A., Hessel, B., McDonagh, J., and Saldeen, T., eds) W. de Gruyter Publishing Company, New York, pp 133-145.
7. Peanasky, R.J., Martzen, M.R., Homandberg, G.A., Cash, J.M., Babin, D.R. and Litweiler, B. Proteinase inhibitors from intestinal parasitic helminths: structure and indications of some possible functions in molecular paradigms for eradicating helminthic parasites, UCLA symposium on molecular and cellular biology, New Series, Vol 59, Editor, Austin MacInnis, Alan R. Liss, Inc., New York, NY (1987), pp 349-366.
8. Homandberg, GA. Potential Regulation of Cartilage Metabolism in Osteoarthritis by Fibronectin Fragments. In Special Issue "Fundamental Pathways in Osteoarthritis" in journal, Frontiers in Bioscience 4, d713-730, October, 15, 1999 (ed. Charles J. Malemud). Also, published on Web in full text and available indefinitely at Frontier in Biosciences website: (http://www.bioscience.org/current/special/osteoart.htm. PubMed#: 10525477.
9. Koepp, H.E., Fletchenmacher, J., Huch, K., Thonar, J-M.A., Homandberg, G.A. and Kuettner, K.E. Osteogenic Protein -1 (OP-1) Promotes Proteoglycan Synthesis and Inhibits Cartilage Degeneration Mediated by Fibronectin-Fragments (Fn-f). "The Many Faces of Osteoarthritis", (eds. K.E. Kuettner, V. Hascall). Elsevier Publishing.
10. Homandberg, G.A. Cartilage Damage by Matrix Degradation Products: Fibronectin Fragments. In Clinical Orthopaedics and Related Research 391S, pp S100-S107, 2001 (eds. Lippincott Williams and Wilkins, Inc).
11. Homandberg, G.A. Mechanisms of Beneficial Effects of High Molecular Weight Hyaluronan on Cultured Cartilage Tissue.  Clinical Reviews in Rheumatology (in press).