Activin receptor antagonists for cancer-related anemia and bone disease

Bibliography

• Risbridger GP, Schmitt JF, Robertson DM. Activins and inhibins in endocrine and other tumors. Endocr Rev 2001;22(6):836-58
   PubMed Web of Science ®Google Scholar
• Chen YG, Wang Q, Lin SL, Activin signaling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis. Exp Biol Med (Maywood) 2006;231(5):534-44
   PubMed Web of Science ®Google Scholar
• Leto G. Activin A and bone metastasis. J Cell Physiol 2010;225(2):302-9
   PubMed Web of Science ®Google Scholar
• Vallet S, Mukherjee S, Vaghela N, Activin A promotes multiple myeloma-induced osteolysis and is a promising target for myeloma bone disease. Proc Natl Acad Sci USA 2010;107(11):5124-9
   PubMed Web of Science ®Google Scholar
• Antsiferova M, Huber M, Meyer M, Activin enhances skin tumourigenesis and malignant progression by inducing a pro-tumourigenic immune cell response. Nat Commun 2011;2:576; doi: 10.1038/ncomms1585
   PubMed Web of Science ®Google Scholar
• Ludwig H, Rai K, Blade J, Management of disease-related anemia in patients with multiple myeloma or chronic lymphocytic leukemia: epoetin treatment recommendations. Hematol J 2002;3(3):121-30
   PubMedGoogle Scholar
• Steensma DP. Hematopoietic growth factors in myelodysplastic syndromes. Semin Oncol 2011;38(5):635-47
   PubMed Web of Science ®Google Scholar
• Groopman JE, Itri LM. Chemotherapy-induced anemia in adults: incidence and treatment. J Natl Cancer Inst 1999;91(19):1616-34
   PubMed Web of Science ®Google Scholar
• Caro JJ, Salas M, Ward A, Goss G. Anemia as an independent prognostic factor for survival in patients with cancer: a systemic, quantitative review. Cancer 2001;91(12):2214-21
   PubMed Web of Science ®Google Scholar
• Rawn J. The silent risks of blood transfusion. Curr Opin Anaesthesiol 2008;21(5):664-8
   PubMed Web of Science ®Google Scholar
• Spivak JL, Gascon P, Ludwig H. Anemia management in oncology and hematology. Oncologist 2009;14(Suppl 1):43-56
   PubMed Web of Science ®Google Scholar
• Rizzo JD, Brouwers M, Hurley P, American Society of Hematology/American Society of Clinical Oncology clinical practice guideline update on the use of epoetin and darbepoetin in adult patients with cancer. Blood 2010;116(20):4045-59
   PubMed Web of Science ®Google Scholar
• Bohlius J, Schmidlin K, Brillant C, Recombinant human erythropoiesis-stimulating agents and mortality in patients with cancer: a meta-analysis of randomised trials. Lancet 2009;373(9674):1532-42
   PubMed Web of Science ®Google Scholar
• Ikushima H, Miyazono K. TGFβ signalling: a complex web in cancer progression. Nat Rev Cancer 2010;10(6):415-24
   PubMed Web of Science ®Google Scholar
• Dodson S, Baracos VE, Jatoi A, Muscle wasting in cancer cachexia: clinical implications, diagnosis, and emerging treatment strategies. Annu Rev Med 2011;62:265-79
   PubMed Web of Science ®Google Scholar
• Wiater E, Vale W. Inhibin is an antagonist of bone morphogenetic protein signaling. J Biol Chem 2003;278(10):7934-41
   PubMed Web of Science ®Google Scholar
• Harrison CA, Al-Musawi SL, Walton KL. Prodomains regulate the synthesis, extracellular localisation and activity of TGF-β superfamily ligands. Growth Factors 2011;29(5):174-86
   PubMed Web of Science ®Google Scholar
• Sengle G, Ono RN, Sasaki T, Sakai LY. Prodomains of transforming growth factor β (TGFβ) superfamily members specify different functions: extracellular matrix interactions and growth factor bioavailability. J Biol Chem 2011;286(7):5087-99
   PubMed Web of Science ®Google Scholar
• Walton KL, Makanji Y, Harrison CA. New insights into the mechanisms of activin action and inhibition. Mol Cell Endocrinol 2012;359(1-2):2-12
   PubMed Web of Science ®Google Scholar
• Cash JN, Rejon CA, McPherron AC, The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding. EMBO J 2009;28(17):2662-76
   PubMed Web of Science ®Google Scholar
• Yamashita H, ten Dijke P, Huylebroeck D, Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects. J Cell Biol 1995;130(1):217-26
   PubMed Web of Science ®Google Scholar
• Upton PD, Davies RJ, Trembath RC, Morrell NW. Bone morphogenetic protein (BMP) and activin type II receptors balance BMP9 signals mediated by activin receptor-like kinase-1 in human pulmonary artery endothelial cells. J Biol Chem 2009;284(23):15794-804
   PubMed Web of Science ®Google Scholar
• Xia Y, Yu PB, Sidis Y, Repulsive guidance molecule RGMa alters utilization of bone morphogenetic protein (BMP) type II receptors by BMP2 and BMP4. J Biol Chem 2007;282(25):18129-40
   PubMed Web of Science ®Google Scholar
• de Caestecker M. The transforming growth factor-β superfamily of receptors. Cytokine Growth Factor Rev 2004;15(1):1-11
   PubMed Web of Science ®Google Scholar
• Derynck R, Zhang YE. Smad-dependent and Smad-independent pathways in TGF-β family signalling. Nature 2003;425(6958):577-84
   PubMed Web of Science ®Google Scholar
• Matzuk MM, Lu N, Vogel H, Multiple defects and perinatal death in mice deficient in follistatin. Nature 1995;374(6520):360-3
   PubMed Web of Science ®Google Scholar
• Gazzerro E, Canalis E. Bone morphogenetic proteins and their antagonists. Rev Endocr Metab Disord 2006;7(1-2):51-65
   PubMed Web of Science ®Google Scholar
• Bilandzic M, Stenvers KL. Betaglycan: a multifunctional accessory. Mol Cell Endocrinol 2011;339(1-2):180-9
   PubMed Web of Science ®Google Scholar
• Bartholin L, Maguer-Satta V, Hayette S, Transcription activation of FLRG and follistatin by activin A, through Smad proteins, participates in a negative feedback loop to modulate activin A function. Oncogene 2002;21(14):2227-35
   PubMed Web of Science ®Google Scholar
• Yu PB, Beppu H, Kawai N, Bone morphogenetic protein (BMP) type II receptor deletion reveals BMP ligand-specific gain of signaling in pulmonary artery smooth muscle cells. J Biol Chem 2005;280(26):24443-50
   PubMed Web of Science ®Google Scholar
• Soderberg SS, Karlsson G, Karlsson S. Complex and context dependent regulation of hematopoiesis by TGF-β superfamily signaling. Ann NY Acad Sci 2009;1176:55-69
   PubMed Web of Science ®Google Scholar
• Nicks KM, Perrien DS, Akel NS, Regulation of osteoblastogenesis and osteoclastogenesis by the other reproductive hormones, activin and inhibin. Mol Cell Endocrinol 2009;310(1-2):11-20
   PubMed Web of Science ®Google Scholar
• Goldman DC, Bailey AS, Pfaffle DL, BMP4 regulates the hematopoietic stem cell niche. Blood 2009;114(20):4393-401
   PubMed Web of Science ®Google Scholar
• Paulson RF, Shi L, Wu DC. Stress erythropoiesis: new signals and new stress progenitor cells. Curr Opin Hematol 2011;18(3):139-45
   PubMed Web of Science ®Google Scholar
• Broxmeyer HE, Lu L, Cooper S, Selective and indirect modulation of human multipotential and erythroid hematopoietic progenitor cell proliferation by recombinant human activin and inhibin. Proc Natl Acad Sci USA 1988;85(23):9052-6
   PubMed Web of Science ®Google Scholar
• Shao L, Frigon NL Jr, Sehy DW, Regulation of production of activin A in human marrow stromal cells and monocytes. Exp Hematol 1992;20(10):1235-42
   PubMed Web of Science ®Google Scholar
• Shiozaki M, Kosaka M, Eto Y. Activin A: a commitment factor in erythroid differentiation. Biochem Biophys Res Commun 1998;242(3):631-5
   PubMed Web of Science ®Google Scholar
• Maguer-Satta V, Bartholin L, Jeanpierre S, Regulation of human erythropoiesis by activin A, BMP2, and BMP4, members of the TGFβ family. Exp Cell Res 2003;282(2):110-20
   PubMed Web of Science ®Google Scholar
• Shiozaki M, Sakai R, Tabuchi M, In vivo treatment with erythroid differentiation factor (EDF/activin A) increases erythroid precursors (CFU-E and BFU-E) in mice. Biochem Biophys Res Commun 1989;165(3):1155-61
   PubMed Web of Science ®Google Scholar
• Shav-Tal Y, Zipori D. The role of activin A in regulation of hemopoiesis. Stem Cells 2002;20(6):493-500
   PubMed Web of Science ®Google Scholar
• Zhou L, Nguyen AN, Sohal D, Inhibition of the TGF-β receptor I kinase promotes hematopoiesis in MDS. Blood 2008;112(8):3434-43
   PubMed Web of Science ®Google Scholar
• Gaddy-Kurten D, Coker JK, Abe E, Inhibin suppresses and activin stimulates osteoblastogenesis and osteoclastogenesis in murine bone marrow cultures. Endocrinology 2002;143(1):74-83
   PubMed Web of Science ®Google Scholar
• Perrien DS, Akel NS, Edwards PK, Inhibin A is an endocrine stimulator of bone mass and strength. Endocrinology 2007;148(4):1654-65
   PubMed Web of Science ®Google Scholar
• Allan CM, Kalak R, Dunstan CR, Follicle-stimulating hormone increases bone mass in female mice. Proc Natl Acad Sci USA 2010;107(52):22629-34
   PubMed Web of Science ®Google Scholar
• Gajos-Michniewicz A, Piastowska AW, Russell JA, Ochedalski T. Follistatin as a potent regulator of bone metabolism. Biomarkers 2010;15(7):563-74
   PubMed Web of Science ®Google Scholar
• Gajos-Michniewicz A, Pawlowska E, Ochedalski T, Piastowska-Ciesielska A. The influence of follistatin on mechanical properties of bone tissue in growing mice with overexpression of follistatin. J Bone Miner Metab 2012;30(4):426-33
   PubMed Web of Science ®Google Scholar
• Ye L, Mason MD, Jiang WG. Bone morphogenetic protein and bone metastasis, implication and therapeutic potential. Front Biosci 2011;16:865-97
   Web of Science ®Google Scholar
• Leto G, Incorvaia L, Badalamenti G, Activin A circulating levels in patients with bone metastasis from breast or prostate cancer. Clin Exp Metastasis 2006;23(2):117-22
   PubMed Web of Science ®Google Scholar
• Terpos E, Kastritis E, Christoulas D, Circulating activin-A is elevated in patients with advanced multiple myeloma and correlates with extensive bone involvement and inferior survival; no alterations post-lenalidomide and dexamethasone therapy. Ann Oncol 2012;23(10):2681-6
   PubMed Web of Science ®Google Scholar
• Matzuk MM, Finegold MJ, Su JG, Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in mice. Nature 1992;360(6402):313-19
   PubMed Web of Science ®Google Scholar
• Matzuk MM, Finegold MJ, Mather JP, Development of cancer cachexia-like syndrome and adrenal tumors in inhibin-deficient mice. Proc Natl Acad Sci USA 1994;91(19):8817-21
   PubMed Web of Science ®Google Scholar
• Cipriano SC, Chen L, Kumar TR, Matzuk MM. Follistatin is a modulator of gonadal tumor progression and the activin-induced wasting syndrome in inhibin-deficient mice. Endocrinology 2000;141(7):2319-27
   PubMed Web of Science ®Google Scholar
• Takabe K, Wang L, Leal AM, Adenovirus-mediated overexpression of follistatin enlarges intact liver of adult rats. Hepatology 2003;38(5):1107-15
   PubMed Web of Science ®Google Scholar
• Schwall RH, Robbins K, Jardieu P, Activin induces cell death in hepatocytes in vivo and in vitro. Hepatology 1993;18(2):347-56
   PubMed Web of Science ®Google Scholar
• Yasuda H, Mine T, Shibata H, Activin A: an autocrine inhibitor of initiation of DNA synthesis in rat hepatocytes. J Clin Invest 1993;92(3):1491-6
   PubMed Web of Science ®Google Scholar
• Ogino H, Yano S, Kakiuchi S, Follistatin suppresses the production of experimental multiple-organ metastasis by small cell lung cancer cells in natural killer cell-depleted SCID mice. Clin Cancer Res 2008;14(3):660-7
   PubMed Web of Science ®Google Scholar
• Matzuk MM, Kumar TR, Vassalli A, Functional analysis of activins during mammalian development. Nature 1995;374(6520):354-6
   PubMed Web of Science ®Google Scholar
• Lau AL, Kumar TR, Nishimori K, Activin betaC and betaE genes are not essential for mouse liver growth, differentiation, and regeneration. Mol Cell Biol 2000;20(16):6127-37
   PubMed Web of Science ®Google Scholar
• Gold E, Jetly N, O'Bryan MK, Activin C antagonizes activin A in vitro and overexpression leads to pathologies in vivo. Am J Pathol 2009;174(1):184-95
   PubMed Web of Science ®Google Scholar
• Rodgarkia-Dara C, Vejda S, Erlach N, The activin axis in liver biology and disease. Mutat Res 2006;613(2-3):123-37
   PubMed Web of Science ®Google Scholar
• Jeruss JS, Sturgis CD, Rademaker AW, Woodruff TK. Down-regulation of activin, activin receptors, and Smads in high-grade breast cancer. Cancer Res 2003;63(13):3783-90
   PubMed Web of Science ®Google Scholar
• Zhou Y, Sun H, Danila DC, Truncated activin type I receptor Alk4 isoforms are dominant negative receptors inhibiting activin signaling. Mol Endocrinol 2000;14(12):2066-75
   PubMed Web of Science ®Google Scholar
• Su GH, Bansal R, Murphy KM, ACVR1B (ALK4, activin receptor type 1B) gene mutations in pancreatic carcinoma. Proc Natl Acad Sci USA 2001;98(6):3254-7
   PubMed Web of Science ®Google Scholar
• Wildi S, Kleeff J, Maruyama H, Overexpression of activin A in stage IV colorectal cancer. Gut 2001;49(3):409-17
   PubMed Web of Science ®Google Scholar
• Reis FM, Cobellis L, Tameirao LC, Serum and tissue expression of activin A in postmenopausal women with breast cancer. J Clin Endocrinol Metab 2002;87(5):2277-82
   PubMed Web of Science ®Google Scholar
• Seder CW, Hartojo W, Lin L, Upregulated INHBA expression may promote cell proliferation and is associated with poor survival in lung adenocarcinoma. Neoplasia 2009;11(4):388-96
   PubMed Web of Science ®Google Scholar
• Pirisi M, Fabris C, Luisi S, Evaluation of circulating activin-A as a serum marker of hepatocellular carcinoma. Cancer Detect Prev 2000;24(2):150-5
   PubMedGoogle Scholar
• Yuen MF, Norris S, Evans LW, Transforming growth factor-beta 1, activin and follistatin in patients with hepatocellular carcinoma and patients with alcoholic cirrhosis. Scand J Gastroenterol 2002;37(2):233-8
   PubMed Web of Science ®Google Scholar
• Murata T, Saito S, Shiozaki M, Anti-activin A antibody (IgY) specifically neutralizes various activin A activities. Proc Soc Exp Biol Med 1996;211(1):100-7
   PubMed Web of Science ®Google Scholar
• Bogdanovich S, Krag TO, Barton ER, Functional improvement of dystrophic muscle by myostatin blockade. Nature 2002;420(6914):418-21
   PubMed Web of Science ®Google Scholar
• Muenster U, Korupolu R, Rastogi R, Antagonism of activin by activin chimeras. Vitam Horm 2011;85:105-28
   PubMed Web of Science ®Google Scholar
• Makanji Y, Walton KL, Chan KL, Generation of a specific activin antagonist by modification of the activin A propeptide. Endocrinology 2011;152(10):3758-68
   PubMed Web of Science ®Google Scholar
• Hemmati-Brivanlou A, Melton DA. A truncated activin receptor inhibits mesoderm induction and formation of axial structures in Xenopus embryos. Nature 1992;359(6396):609-14
   PubMed Web of Science ®Google Scholar
• Donaldson CJ, Vaughan JM, Corrigan AZ, Activin and inhibin binding to the soluble extracellular domain of activin receptor II. Endocrinology 1999;140(4):1760-6
   PubMed Web of Science ®Google Scholar
• Pearsall RS, Canalis E, Cornwall-Brady M, A soluble activin type IIA receptor induces bone formation and improves skeletal integrity. Proc Natl Acad Sci USA 2008;105(19):7082-7
   PubMed Web of Science ®Google Scholar
• Souza TA, Chen X, Guo Y, Proteomic identification and functional validation of activins and bone morphogenetic protein 11 as candidate novel muscle mass regulators. Mol Endocrinol 2008;22(12):2689-702
   PubMed Web of Science ®Google Scholar
• Mulivor AW, Barbosa D, Kumar R, RAP-011, a soluble activin receptor type IIA murine IgG-Fc fusion protein, prevents chemotherapy induced anemia. Blood 2009;114(22):abstract 161
   Google Scholar
• Li Q, Kumar R, Underwood K, Prevention of cachexia-like syndrome development and reduction of tumor progression in inhibin-deficient mice following administration of a chimeric activin receptor type II-murine Fc protein. Mol Hum Reprod 2007;13(9):675-83
   PubMed Web of Science ®Google Scholar
• Raje N, Vallet S. Sotatercept, a soluble activin receptor type 2A IgG-Fc fusion protein for the treatment of anemia and bone loss. Curr Opin Mol Ther 2010;12(5):586-97
   PubMed Web of Science ®Google Scholar
• Fajardo RJ, Manoharan RK, Pearsall RS, Treatment with a soluble receptor for activin improves bone mass and structure in the axial and appendicular skeleton of female cynomolgus macaques (Macaca fascicularis). Bone 2010;46(1):64-71
   PubMed Web of Science ®Google Scholar
• Lotinun S, Pearsall RS, Davies MV, A soluble activin receptor Type IIA fusion protein (ACE-011) increases bone mass via a dual anabolic-antiresorptive effect in Cynomolgus monkeys. Bone 2010;46(4):1082-8
   PubMed Web of Science ®Google Scholar
• Hashimoto O, Nakamura T, Shoji H, A novel role of follistatin, an activin-binding protein, in the inhibition of activin action in rat pituitary cells. Endocytotic degradation of activin and its acceleration by follistatin associated with cell-surface heparin sulfate. J Biol Chem 1997;272(21):13835-42
   PubMed Web of Science ®Google Scholar
• Chantry AD, Heath D, Mulivor AW, Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo. J Bone Miner Res 2010;25(12):2633-46
   PubMedGoogle Scholar
• Ruckle J, Jacobs M, Kramer W, Single-dose, randomized, double-blind, placebo-controlled study of ACE-011 (ActRIIA-IgG1) in postmenopausal women. J Bone Miner Res 2009;24(4):744-52
   PubMed Web of Science ®Google Scholar
• Kim KT, Borgstein NG, Yang Y, ACE-011, a soluble activin receptor type IIa IgG-Fc fusion protein, increases hemoglobin and hematocrit levels in postmenopausal healthy women. Blood 2008;112(11):abstract 3866
   Google Scholar
• Abdulkadyrov KM, Salogub GN, Khuazheva NK, ACE-011, a soluble activin receptor type IIa IgG-Fc fusion protein, increases hemoglobin (Hb) and improves bone lesions in multiple myeloma patients receiving myelosuppressive chemotherapy: preliminary analysis. Blood 2009;114(22):abstract 749
   Google Scholar
• Bonafoux D, Lee WC. Strategies for TGF-β modulation: a review of recent patents. Expert Opin Ther Patents 2009;19(12):1759-69
   PubMed Web of Science ®Google Scholar
• Buijs JT, Stayrook KR, Guise TA. TGF-β in the bone microenvironment: role in breast cancer metastases. Cancer Microenviron 2011;4(3):261-81
   PubMedGoogle Scholar
• Inman GJ, Nicolas FJ, Callahan JF, SB-431542 is a potent and specific inhibitor of transforming growth factor-beta superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7. Mol Pharmacol 2002;62(1):65-74
   PubMed Web of Science ®Google Scholar
• Vogt J, Traynor R, Sapkota GP. The specificities of small molecule inhibitors of the TGFβ and BMP pathways. Cell Signal 2011;23(11):1831-42
   PubMed Web of Science ®Google Scholar
• Bueno L, de Alwis DP, Pitou C, Semi-mechanistic modelling of the tumour growth inhibitory effects of LY2157299, a new type I receptor TGF-β kinase antagonist, in mice. Eur J Cancer 2008;44(1):142-50
   PubMed Web of Science ®Google Scholar
• Zhou L, McMahon C, Bhagat T, Reduced SMAD7 leads to overactivation of TGF-β signaling in MDS that can be reversed by a specific inhibitor of TGF-β receptor I kinase. Cancer Res 2011;71(3):955-63
   PubMed Web of Science ®Google Scholar
• Calvo-Aller E, Baselga J, Glatt S, First human dose escalation study in patients with metastatic malignancies to determine safety and pharmacokinetics of LY2157299, a small molecule inhibitor of the transforming growth factor-β receptor I kinase. J Clin Oncol 2008;26(15 Suppl):abstract 1455
   Google Scholar
• Rodon Ahnert J, Baselga J, Calvo E, First human dose (FHD) study of the oral transforming growth factor-β receptor I kinase inhibitor LY2157299 in patients with treatment-refractory malignant glioma. J Clin Oncol 2011;29(Suppl):abstract 3011
   Google Scholar
• Ludwig H, Van Belle S, Barrett-Lee P, The European Cancer Anaemia Survey (ECAS): a large, multinational, prospective survey defining the prevalence, incidence, and treatment of anaemia in cancer patients. Eur J Cancer 2004;40(15):2293-306
   PubMed Web of Science ®Google Scholar
• Durie BG. New approaches to treatment for multiple myeloma: durable remission and quality of life as primary goals. Clin Lymphoma Myeloma 2005;6(3):181-90
   PubMedGoogle Scholar
• Hussein MA. Multiple myeloma: most common end-organ damage and management. J Natl Compr Canc Netw 2007;5(2):170-8
   PubMedGoogle Scholar
• Kyle RA, Yee GC, Somerfield MR, American Society of Clinical Oncology 2007 clinical practice guideline update on the role of bisphosphonates in multiple myeloma. J Clin Oncol 2007;25(17):2464-72
   PubMed Web of Science ®Google Scholar
• Terpos E, Sezer O, Croucher PI, The use of bisphosphonates in multiple myeloma: recommendations of an expert panel on behalf of the European Myeloma Network. Ann Oncol 2009;20(8):1303-17
   PubMed Web of Science ®Google Scholar
• Suragani RNVS, Mulivor A, Pearsall RS, Kumar R. RAP-536 promotes terminal erythroid differentiation and reduces anemia in myelodysplastic syndromes. Blood 2011;118(21):abstract 610
   Google Scholar