IP Library Granted Patent US 8,629,109
Granted Patent B2
US 8,629,109 · App. 13/176,718 · Granted Jan 14, 2014

Method for promoting bone growth using activin-actriia antagonists

Inventors: John Knopf (Carlisle, MA); Jasbir Seehra (Lexington, MA)
Assignee: Acceleron Pharma Inc.
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Quick Facts
Patent No.
US 8,629,109
App. No.
13/176,718
Granted
Jan 14, 2014
Kind
B2
Abstract

In certain aspects, the present invention provides compositions and methods for promoting bone growth and increasing bone density.

Claims (129)

1. A method for treating bone fractures, comprising administering to a subject in need thereof an effective amount of a polypeptide comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 2.

2. The method of claim 1 , further comprising administering a second bone active-agent.

3. The method of claim 2 , wherein the bone active-agent is selected from a bisphosphonate, an estrogen, a selective estrogen receptor modulator, a parathyroid hormone, a calcitonin, a calcium supplement, and a vitamin D supplement.

4. The method of claim 2 , wherein the second bone active-agent is administered conjointly with the polypeptide.

5. The method of claims 4 , wherein the polypeptide and the second bone active-agent are administered as a single co-formulation.

6. The method of claim 4 , wherein the polypeptide and the second bone active-agent are administered simultaneously.

7. The method of claim 4 , wherein the polypeptide and the second bone active-agent are administered at separate times.

8. The method of claim 1 , wherein the polypeptide includes one or more modified amino acid residues selected from a glycosylated amino acid, a PEGylated amino acid, a farnesylated amino acid, an acetylated amino acid, a biotinylated amino acid, or an amino acid conjugated to a lipid moiety.

9. The method of claim 1 , wherein the polypeptide is administered no more frequently than once per month.

10. The method of claim 1 , wherein the polypeptide is administered no more frequently than once every three months.

11. The method of claim 1 , wherein the polypeptide is administered no more frequently than once every six months.

12. The method of claim 1 , wherein the polypeptide is at least 98% pure as determined by size-exclusion chromatography.

13. The method of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 2.

14. The method of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 2.

15. The method of claim 1 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 2.

16. The method of claim 1 , wherein the polypeptide is glycosylated and has a glycosylation pattern identical to a glycosylation pattern obtained by expressing the polypeptide in a Chinese hamster ovary (CHO) cell line.

17. The method of claim 1 , wherein the N-terminus of the polypeptide is ILGRSETQE (SEQ ID NO: 11).

18. The method of claim 1 , wherein the polypeptide further comprises a domain that enhances one or more of in vivo stability, in vivo half-life, uptake/administration, tissue localization or distribution, or formation of protein complexes.

19. The method of claim 18 , wherein the domain is an immunoglobulin Fc domain.

20. The method of claim 18 , wherein the domain is serum albumin.

21. The method of claim 1 , wherein the serum half-life of the polypeptide is greater than two weeks.

22. The method of claim 1 , wherein the serum half-life of the polypeptide is 20-30 days.

23. The method of claim 1 , wherein the polypeptide has one or more of the following characteristics: (i) binds to an ActRIIa ligand with a K D of at least 10 −7 M; and (ii) inhibits ActRIIa signaling.

24. The method of claim 1 , wherein the polypeptide is soluble.

25. The method of claim 1 , wherein the polypeptide is an antagonist of activin A.

26. The method of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 95% identical to SEQ ID NO: 7.

27. The method of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 7.

28. The method of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 7.

29. The method of claim 1 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 7.

30. The method of claim 1 , wherein the polypeptide binds to activin.

31. The method of claim 1 , wherein the polypeptide is recombinantly expressed using a Tissue Plasminogen Activator (TPA) leader sequence.

32. The method of claim 31 , wherein the TPA leader sequence comprises the amino acid sequence of SEQ ID NO:9.

33. A method for increasing bone strength, comprising administering to a subject in need thereof an effective amount of a polypeptide comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 2.

34. The method of claim 33 , further comprising administering a second bone active-agent.

35. The method of claim 34 , wherein the bone active-agent is selected from a bisphosphonate, an estrogen, a selective estrogen receptor modulator, a parathyroid hormone, a calcitonin, a calcium supplement, and a vitamin D supplement.

36. The method of claim 34 , wherein the second bone active-agent is administered conjointly with the polypeptide.

37. The method of claims 34 , wherein the polypeptide and the second bone active-agent are administered as a single co-formulation.

38. The method of claim 34 , wherein the polypeptide and the second bone active-agent are administered simultaneously.

39. The method of claim 34 , wherein the polypeptide and the second bone active-agent are administered at separate times.

40. The method of claim 33 , wherein the polypeptide includes one or more modified amino acid residues selected from a glycosylated amino acid, a PEGylated amino acid, a farnesylated amino acid, an acetylated amino acid, a biotinylated amino acid, or an amino acid conjugated to a lipid moiety.

41. The method of claim 33 , wherein the polypeptide is administered no more frequently than once per month.

42. The method of claim 33 , wherein the polypeptide is administered no more frequently than once every three months.

43. The method of claim 33 , wherein the polypeptide is administered no more frequently than once every six months.

44. The method of claim 33 , wherein the polypeptide is at least 98% pure as determined by size-exclusion chromatography.

45. The method of claim 33 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 2.

46. The method of claim 33 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 2.

47. The method of claim 33 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 2.

48. The method of claim 33 , wherein the polypeptide is glycosylated and has a glycosylation pattern identical to a glycosylation pattern obtained by expressing the polypeptide in a Chinese hamster ovary (CHO) cell line.

49. The method of claim 33 , wherein the N-terminus of the polypeptide is ILGRSETQE (SEQ ID NO: 11).

50. The method of claim 33 , wherein the polypeptide further comprises a domain that enhances one or more of in vivo stability, in vivo half-life, uptake/administration, tissue localization or distribution, or formation of protein complexes.

51. The method of claim 50 , wherein the domain is an immunoglobulin Fc domain.

52. The method of claim 50 , wherein the domain is serum albumin.

53. The method of claim 33 , wherein the serum half-life of the polypeptide is greater than two weeks.

54. The method of claim 33 , wherein the serum half-life of the polypeptide is 20-30 days.

55. The method of claim 33 , wherein the polypeptide has one or more of the following characteristics: (i) binds to an ActRIIa ligand with a K D of at least 10 −7 M; and (ii) inhibits ActRIIa signaling.

56. The method of claim 33 , wherein the polypeptide is soluble.

57. The method of claim 33 , wherein the polypeptide binds to activin.

58. The method of claim 33 , wherein the polypeptide is an antagonist of activin A.

59. The method of claim 33 , wherein the polypeptide comprises an amino acid sequence that is at least 95% identical to SEQ ID NO: 7.

60. The method of claim 33 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 7.

61. The method of claim 33 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 7.

62. The method of claim 33 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 7.

63. The method of claim 33 , wherein the polypeptide is recombinantly expressed using a Tissue Plasminogen Activator (TPA) leader sequence.

64. The method of claim 63 , wherein the TPA leader sequence comprises the amino acid sequence of SEQ ID NO:9.

65. A method for increasing bone mineral density comprising administering to a subject in need thereof an effective amount of a polypeptide comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 2.

66. The method of claim 65 , further comprising administering a second bone active-agent.

67. The method of claim 66 , wherein the bone-active agent is selected from a bisphosphonate, an estrogen, a selective estrogen receptor modulator, a parathyroid hormone, a calcitonin, a calcium supplement, and a vitamin D supplement.

68. The method of claim 66 , wherein the second bone active-agent is administered conjointly with the polypeptide.

69. The method of claims 66 , wherein the polypeptide and the second bone active-agent are administered as a single co-formulation.

70. The method of claim 66 , wherein the polypeptide and the second bone active-agent are administered simultaneously.

71. The method of claim 66 , wherein the polypeptide and the second bone active-agent are administered at separate times.

72. The method of claim 65 , wherein the polypeptide includes one or more modified amino acid residues selected from a glycosylated amino acid, a PEGylated amino acid, a farnesylated amino acid, an acetylated amino acid, a biotinylated amino acid, or an amino acid conjugated to a lipid moiety.

73. The method of claim 65 , wherein the polypeptide is administered no more frequently than once per month.

74. The method of claim 65 , wherein the polypeptide is administered no more frequently than once every three months.

75. The method of claim 65 , wherein the polypeptide is administered no more frequently than once every six months.

76. The method of claim 65 , wherein the polypeptide is at least 98% pure as determined by size-exclusion chromatography.

77. The method of claim 65 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 2.

78. The method of claim 65 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 2.

79. The method of claim 65 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 2.

80. The method of claim 65 , wherein the polypeptide is glycosylated and has a glycosylation pattern identical to a glycosylation pattern obtained by expressing the polypeptide in a Chinese hamster ovary (CHO) cell line.

81. The method of claim 65 , wherein the N-terminus of the polypeptide is ILGRSETQE (SEQ ID NO: 11).

82. The method of claim 65 , wherein the polypeptide further comprises a domain that enhances one or more of in vivo stability, in vivo half-life, uptake/administration, tissue localization or distribution, or formation of protein complexes.

83. The method of claim 82 , wherein the domain is an immunoglobulin Fc domain.

84. The method of claim 82 , wherein the domain is serum albumin.

85. The method of claim 65 , wherein the serum half-life of the polypeptide is greater than two weeks.

86. The method of claim 65 , wherein the serum half-life of the polypeptide is 20-30 days.

87. The method of claim 65 , wherein the polypeptide has one or more of the following characteristics: (i) binds to an ActRIIa ligand with a K D of at least 10 −7 M; and (ii) inhibits ActRIIa signaling.

88. The method of claim 65 , wherein the polypeptide is soluble.

89. The method of claim 65 , wherein the polypeptide binds to activin.

90. The method of claim 65 , wherein the polypeptide is an antagonist of activin A.

91. The method of claim 65 , wherein the polypeptide comprises an amino acid sequence that is at least 95% identical to SEQ ID NO: 7.

92. The method of claim 65 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 7.

93. The method of claim 65 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 7.

94. The method of claim 65 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 7.

95. The method of claim 65 , wherein the polypeptide is recombinantly expressed using a Tissue Plasminogen Activator (TPA) leader sequence.

96. The method of claim 95 , wherein the TPA leader sequence comprises the amino acid sequence of SEQ ID NO:9.

97. A method for treating a bone-related disorder, comprising administering to a subject in need thereof an effective amount of a polypeptide comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 2, wherein the bone-related disorder is associated with low bone density or decreased bone strength.

98. The method of claim 97 , wherein the bone-related disorder is selected from osteoporosis, hypogonadal bone loss, tumor-induced bone loss, cancer therapy-induced bone loss, bony metastases, hyperparathyroidism, Cushing's disease, thyrotoxicosis, chronic diarrheal state or malabsorption, renal tubular acidosis, anorexia nervosa, and Paget's disease.

99. The method of claim 97 , further comprising administering a second bone active-agent.

100. The method of claim 99 , wherein the bone active-agent is selected from a bisphosphonate, an estrogen, a selective estrogen receptor modulator, a parathyroid hormone, a calcitonin, a calcium supplement, and a vitamin D supplement.

101. The method of claim 99 , wherein the second bone active-agent is administered conjointly with the polypeptide.

102. The method of claims 99 , wherein the polypeptide and the second bone active-agent are administered as a single co-formulation.

103. The method of claim 99 , wherein the polypeptide and the second bone active-agent are administered simultaneously.

104. The method of claim 99 , wherein the polypeptide and the second bone active-agent are administered at separate times.

105. The method of claim 97 , wherein the polypeptide includes one or more modified amino acid residues selected from a glycosylated amino acid, a PEGylated amino acid, a farnesylated amino acid, an acetylated amino acid, a biotinylated amino acid, or an amino acid conjugated to a lipid moiety.

106. The method of claim 97 , wherein the polypeptide is administered no more frequently than once per month.

107. The method of claim 97 , wherein the polypeptide is administered no more frequently than once every three months.

108. The method of claim 97 , wherein the polypeptide is administered no more frequently than once every six months.

109. The method of claim 97 , wherein the polypeptide is at least 98% pure as determined by size-exclusion chromatography.

110. The method of claim 97 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 2.

111. The method of claim 97 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 2.

112. The method of claim 97 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 2.

113. The method of claim 97 , wherein the polypeptide is glycosylated and has a glycosylation pattern identical to a glycosylation pattern obtained by expressing the polypeptide in a Chinese hamster ovary (CHO) cell line.

114. The method of claim 97 , wherein the N-terminus of the polypeptide is ILGRSETQE (SEQ ID NO: 11).

115. The method of claim 97 , wherein the polypeptide further comprises a domain that enhances one or more of in vivo stability, in vivo half-life, uptake/administration, tissue localization or distribution, or formation of protein complexes.

116. The method of claim 115 , wherein the domain is an immunoglobulin Fc domain.

117. The method of claim 115 , wherein the domain is serum albumin.

118. The method of claim 97 , wherein the serum half-life of the polypeptide is greater than two weeks.

119. The method of claim 97 , wherein the serum half-life of the polypeptide is 20-30 days.

120. The method of claim 97 , wherein the polypeptide has one or more of the following characteristics: (i) binds to an ActRIIa ligand with a K D of at least 10 −7 M; and (ii) inhibits ActRIIa signaling.

121. The method of claim 97 , wherein the polypeptide is soluble.

122. The method of claim 97 , wherein the polypeptide binds to activin.

123. The method of claim 97 , wherein the polypeptide is an antagonist of activin A.

124. The method of claim 97 , wherein the polypeptide comprises an amino acid sequence that is at least 95% identical to SEQ ID NO: 7.

125. The method of claim 97 , wherein the polypeptide comprises an amino acid sequence that is at least 97% identical to SEQ ID NO: 7.

126. The method of claim 97 , wherein the polypeptide comprises an amino acid sequence that is at least 99% identical to SEQ ID NO: 7.

127. The method of claim 97 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 7.

128. The method of claim 97 , wherein the polypeptide is recombinantly expressed using a Tissue Plasminogen Activator (TPA) leader sequence.

129. The method of claim 128 , wherein the TPA leader sequence comprises the amino acid sequence of SEQ ID NO:9.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Aug 3, 2011
From: KNOPF, JOHN; SEEHRA, JASBIR
To: ACCELERON PHARMA INC.
Reel/Frame 026692/0707 →
Continuity (6)
Continuation 12284862 · Sep 24, 2008
Continuation 11603485 · Nov 22, 2006
Provisional Application 60739462 · Nov 23, 2005
Provisional Application 60783322 · Mar 17, 2006
Provisional Application 60844855 · Sep 15, 2006
Related Publication 20120058115A1 · Mar 8, 2012