αvβ3 Integrin antagonists as inhibitors of bone resorption

Bibliography

• PYTELA R, PIERSCHBACHER MD, ROUSLAHTI E: A125/115-kDa Cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Proc. Natl. Acad. Sci. USA (1985) 82:5766–5770.
   PubMed Web of Science ®Google Scholar
• SUZUKI S, ARGRAVES WS, PYTELA R et al.: cDNA andamino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmem-brane domain and homologies with other adhesion protein receptors. Proc. Natl. Acad. Sci. USA (1986) 83:8614–8618.
   PubMed Web of Science ®Google Scholar
• HYNES RO: Integrins: a family of cell surface receptors. Cell (1987) 48:549–554.
   PubMed Web of Science ®Google Scholar
• •Excellent summary of early work.
   Google Scholar
• FITZGERALD LA, STEINER B, RALL SC, LO SS, PHILLIPS DR: Protein sequence of endothelial glycoprotein Ma derived from a cDNA clone. J. Biol. Chem. (1987) 267:3936–3939.
   Google Scholar
• D'SOUZA SE, HAAS TA, PIOTROWICZ RS eta/.: ligand and cation binding are dual functions of a discrete segment of the beta-3 subunit: cation displacement is implicated in ligand binding. Cell (1994) 79:659–667.
   Google Scholar
• LAW DA, NANNIZZI-ALAIMO L, PHILLIPS DR: outside-in integrin signal transduction. anb133 (GP lib/Ma) tyrosine phosphorylation induced by platelet aggrega-tion. J. Biol. Chem. (1996) 271:10811–10815.
   Google Scholar
• O'TOOLE TE, YLANNE J, GULLEY BM: Regulation of integrin affinity states through an NPXY Motif in the p subunit cytoplasmic domain. J. Biol. Chem. (1995) 270:8553–8558.
   PubMed Web of Science ®Google Scholar
• HORTON MA: The avp3 integrin `vitronectin receptor'. Int. J. Bioch. Cell Biol. (1997) 29:721–725.
   PubMed Web of Science ®Google Scholar
• PIERSCHBACHER MD, RUOSLAHTI E: Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion./ Biol. Chem. (1987) 262:17294–17298.
   PubMed Web of Science ®Google Scholar
• LOFTUS JC, HALLORAN CE, GINSBERG MH et al.: Theamino-terminal one-third of am defines the ligand recognition specificity of Integrin am,133. J. Biol. Chem. (1996) 271:2033–2039.
   PubMed Web of Science ®Google Scholar
• CHERESH DA, BERLINER SA, VICENTE V, RUGGERI ZM Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells. Cell (1989) 58:945–953.
   PubMed Web of Science ®Google Scholar
• LAM SC-T, PLOW EF, SMITH MA et al.: Evidence thatArginyl-Glycyl-Aspartate peptides and fibrinogen gamma chain peptides share a common binding site on platelets. J. Biol. Chem. (1987) 262:947–950.
   PubMed Web of Science ®Google Scholar
• BLYSTONE SD, WILLIAMS MP, SLATER SE, BROWN EJ: Requirement of integrin 133 Tyrosine 747 for 133 tyrosine phosphorylation and regulation of av133 avidity. J. Biol. Chem. (1997) 272:28757–28761.
   PubMed Web of Science ®Google Scholar
• HYNES RO: Cell adhesion: old and new questions. Trends Cell Biol. (1999) 9:M33–M37.
   PubMed Web of Science ®Google Scholar
• BENNETT JS, CHAN C, VILAIRE G, MOUSA SA, DEGRADOWF: Agonist-activated av133 on platelets and lympho-cytes binds to the matrix protein osteopontin. J. Biol. Chem. (1997) 272:8137–8140.
   PubMed Web of Science ®Google Scholar
• BYZOVA TV, PLOW EF: Activation of av133 on vascularcells controls recognition of prothrombin. J. Cell Biol. (1998) 143:2081–2092.
   PubMed Web of Science ®Google Scholar
• PAMPORI N, HATO T, STUPACK DG et al.: Mechanisms and consequences of affinity modulation of integrin av133 detected with a novel patch-engineered monovalent ligand. J. Biol. Chem. (1999) 274:21609–21616.
   PubMed Web of Science ®Google Scholar
• ••Leading paper on affinity/avidity modulation.
   Google Scholar
• Principles Of Bone Biology. Bilezikian JP, Raisz LG, Rodan GA (Eds.) Academic Press, New York, USA (1996).
   Google Scholar
• ERIKSEN EF: Normal and pathological remodeling of human trabecular bone: three dimensional reconstruction of the remodeling sequence in normals and in metabolic bone disease. Endocr. Rev. (1986) 7:379–408.
   PubMed Web of Science ®Google Scholar
• LIAN JB, STEIN GS: Osteoblast biology. In: Osteoporosis. Marcus R, Feldman D, Kelsey J (Eds.) Academic Press, San Diego, USA (1996):23–59.
   Google Scholar
• VAANANEN HK, HORTON M: The osteoclast clear zone is a specialized cell-extracellular matrix adhesion structure. J. Cell Sci. (1995) 108:2729–2732.
   PubMed Web of Science ®Google Scholar
• LEU C-T, WESOLOWSKI G, NAGY RM et al.: Osteoclasts have over 107 high affinity echistatin binding sites (RGD-Integrins). J. Bone Min. (1997) 12:S416.
   Google Scholar
• NAKAMURA IJ, GAILIT J, SASAKI T: Osteoclast integrin av133 is present in the clear zone and contributes to cellular polization. Cell Tiss. Res. (1996) 286:507–515.
   PubMed Web of Science ®Google Scholar
• LAKKAKORPI PT, HELFRICH MH, HORTON MA, VAANANEN HK: Spatial organization of microfilaments and vitronectin receptor, av133, in osteoclasts. a study using confocal laser scanning microscopy. J. Cell Sci. (1993) 104:663–670.
   Google Scholar
• CHAMBERS TJ, FULLER K, DARBY JA, PRINGLE JA, HORTON MA: Monoclonal antibodies against osteoclasts inhibit bone resorption in vitro. Bone Miner. (1986) 1:127–135.
   PubMedGoogle Scholar
• SATO M, SARDANA MK, GRASSER WA et al.: Echistatin is apotent inhibitor of bone resorption in culture. J. Cell Biol. (1990) 111:1713–1723.
   PubMed Web of Science ®Google Scholar
• HORTON MA, DOREY EL, NESBITT SA et al.: Modulationof vitronectin receptor-mediated osteoclast adhesion by arg-gjy-asp-peptide analogs: a structure-function analysis. J. Bone Min. (1993) 8:239–247.
   PubMed Web of Science ®Google Scholar
• Osteoporosis. Marcus R, Feldman D, Kelsey J (Eds.) Academic Press, San Diego, USA (1996):23–59.
   Google Scholar
• RAY NF, CHAN JK, THAMER M, MELTON LJ: Medical expenditures for the treatment of osteoporotic fractures in the United States in 1995: report from the National Osteoporosis Foundation. J. Bone Min. (1997) 12:24–35.
   PubMed Web of Science ®Google Scholar
• GOULD RJ, POLOKOFF MA, FRIEDMAN PA et al.: Disintegrins: a family of integrin inhibitory proteins from viper venoms. Proc. Soc. Exp. Biol. Med. (1990) 195:168–171.
   PubMed Web of Science ®Google Scholar
• GAN Z-R, GOULD RJ, JACOBS JW, FRIEDMAN PA, POLOKOFF MA: Echistatin. A potent platelet aggrega-tion inhibitor from the venom of the viper, Edo& Carinatus. J. Biol. Chem. (1988) 263:19827–19832.
   Google Scholar
• YAMAMOTO M, FISHER JE, GENTILE Metal.: The integrin ligand echistatin prevents bone loss in ovariectomized mice and rats. Endocrinology (1998) 139:1411–1419.
   Google Scholar
• FISHER JE, CAULFIELD MP, SATO M et al.: Inhibition of osteoclastic bone resorption in vivo by echistatin, an Arginyl-Glycyl-Aspartyf (RGD)-containing protein. Endocrinology (1993) 132:1411–1413.
   PubMed Web of Science ®Google Scholar
• PFAFF M, TANGEMANN K, MOLLER B et al.: Selective recognition of cyclic RGD peptides of NMR defined conformation by ath,03, avp3 and a3a1 integrins. J. Biol. Chem. (1994) 269:20233–20238.
   PubMed Web of Science ®Google Scholar
• DECHANTSREITER MA, PLANKER E, MATHA B et al.: N-Methylated cyclic RGD peptides as highly active and selective avP3 integrin antagonists./ Med. Chem. (1999) 42:3033–3040.
   Google Scholar
• MOUSA SA: Anti-integrins as a potential therapeutic target in angiogenesis. Exp. Opin. Ther. Patents (1999) 9:1237–1248.
   Web of Science ®Google Scholar
• WONG A, HWANG SM, MCDEVITT P et al.: Studies on av133/ligand interactions using a [311]SK&F-107260 binding assay. Molec. Pharm. (1996) 50:529–537.
   PubMed Web of Science ®Google Scholar
• BACH II AC, ESPINA JR, JACKSON SA et al.: Type II to type I b-turn swap changes specificity for integrins. J. Am. Chem. Soc. (1996) 118:293–294.
   Web of Science ®Google Scholar
• SAMANEN J: GPIlb/BIa antagonists. In: Annual Reports In Medicinal Chemistry. Bristol JA (Ed.) Academic Press, New York, USA (1996):91–100.
   Google Scholar
• KEENAN RM, MILLER WH, KWON C et al.: Discovery of potent nonpeptide vitronectin receptor (av133) antago-nists. J. Med. Chem. (1997) 40:2289–2292.
   PubMed Web of Science ®Google Scholar
• MILLER WH, ALBERTS DP, BHATNAGAR PK et al.: Discovery of orally active nonpeptide vitronectin receptor antagonists based on a 2-benzazepine gjy-asp mimetic. J. Med. Chem. (2000) 43:22–26.
   PubMed Web of Science ®Google Scholar
• WARD KW, AZZARANO LM, BONDINELL WE et al Preclinical pharmacokinetics and interspecies scalingof a novel vitronectin receptor antagonist. Drug Meta. D. (1999) 27:1232–1241.
   PubMed Web of Science ®Google Scholar
• LARK MW, STROUP GB, HWANG SM et al.: Design and characterization of orally active Arg-Gly-Asp peptidomimetic vitronectin receptor antagonist SB 265123 for prevention of bone loss in osteoporosis. J. Pharm. Exp. (1999) 291:612–617.
   PubMed Web of Science ®Google Scholar
• LARK MW, STROUP G, COUSINS RD et al.: An orally active vitronectin receptor avb3 antagonist prevents bone resorption in vitro and in vivo in the ovariectomized rat. J. Bone Min. (1998) 23:S219.
   Google Scholar
• EGBERTSON MS, NAYLOR AM, HARTMAN GD et al.: Non-peptide fibrinogen receptor antagonists. 3. design of a centrally constrained inhibitor. Bioorg. Med. Chem. Lett. (1994) 4:1835–1840.
   Google Scholar
• DUGGAN ME. Design and evaluation of potent non-peptide ligands of av13 as inhibitors of bone resorption. 211th National ACS Meeting. New Orleans, LA, USA (1996).
   Google Scholar
• DUGGAN ME, DUONG LT, FISHER JE et al.: Non-peptide av13 antagonists. i. transformation of a potent, integrin selective anbp3 antagonist into the potent avP3 antagonist L-767,635. J. Med. Chem. (2000) (Submitted).
   Google Scholar
• ADANG AEP, LUCAS H, DE MAN APA, ENGH RA, GROOTENHUIS PDJ: Novel acylguanidine containing thrombin inhibitors with reduced basicity at the Pi moiety. Bioorg. Med. Chem. Lett. (1998) 8:3603–3608.
   PubMed Web of Science ®Google Scholar
• ISHIKAWA M, YAMAMOTO M, KUBOTA D et al. Synthesis of potent, non-peptide integrin avp3 antagonists. 218th American Chemical Society Annual Meeting. New Orleans, LA, USA (1999).
   Google Scholar
• BATT DG, PETRAITIS JJ, HOUGHTON GC et al.: Disubsti-tuted indazoles as potent antagonists of the integrin avP3. J. Med. Chem. (2000) 43:41–58.
   PubMed Web of Science ®Google Scholar
• PITTS WJ, WITYAK J, SMALLHEER JM et al.: Isoxazolines as potent antagonists of the integrin avP3.J. Med. Chem. (2000) 43:27–40.
   Google Scholar
• ENGLEMAN VW, NICKOLS GA, ROSS FP et al.: A peptidomimetic antagonist of the avp3 integrin inhibits bone resorption in vitro and prevents osteoporosis in vivo .J. Clin. Invest. (1997) 99:2284–2292.
   Google Scholar
• MEDI 144, SEARLE: avP3 antagonists. 217th ACS National Meeting. Anaheim, CA, USA (1999).
   Google Scholar
• PEYMAN A, WEHNER V, KNOLLE J et al.: RGD mimetics containing a central hydantoin scaffold: avp3 vs. a nbI3 3 selectivity requirements. Bioorg. Med. Chem. Lea. (2000) 10:179–182.
   Google Scholar