ライフサイエンスコーパス: ActRIIA

1 ActRIIA stimulates Smad1 activation in a kinase-dependen

2 ActRIIA(+/-)B(+/-) animals lack axial defects, but have

3 tudies revealed that MT2 cleaves ALK2, ALK3, ActRIIA, Bmpr2, Hfe, and, to a lesser extent, Hjv and Tf

4 growth differentiation factor 11 (GDF11), an ActRIIA ligand, was increased in splenic erythroblasts f

5 demonstrates however that both ActRIIB- and ActRIIA-deficient mice display a hypertrophic phenotype.

6 nt findings demonstrate that both BMPRII and ActRIIA are necessary for endoglin-mediated suppression

7 ptors, we also tested the role of BMPRII and ActRIIA as the type II receptor candidates for the three

8 ansfected with RGMa utilized both BMPRII and ActRIIA for BMP2 or BMP4 signaling.

9 sfection of small hairpin RNA for BMPRII and ActRIIA in MC3T3 cells suppressed the signaling of GDF6,

10 le receptor through the use of specific anti-ActRIIA or anti-ActRIIB antibodies achieves only a parti

11 umab (BYM338), as a human dual-specific anti-ActRIIA/ActRIIB antibody, at the molecular and cellular

12 by X-ray analysis, bimagrumab binds to both ActRIIA and ActRIIB ligand binding domains in a competit

13 xial vertebrae, and that Gdf11 binds to both ActRIIA and ActRIIB, and induces phosphorylation of Smad

14 the activins are capable of binding to both ActRIIA and ActRIIB, with different affinities.

15 two type I (ALK2 and ALK3) and two type II (ActRIIA and BMPR2) BMP receptors.

16 eport that RAP-011, an activin receptor IIA (ActRIIA) ligand trap, improved ineffective erythropoiesi

17 on of invasion: activin A receptor type IIA (ActRIIA) and bone morphogenetic protein receptor type II

18 (BMPRII), but not activin receptor type IIA (ActRIIA) or ActRIIB, based on changes in BMP signaling b

19 we observed similar gastrulation defects in ActRIIA(-/-)nodal(+/-) double mutants, which, if they de

20 Interestingly, ActRIIA is the predominant BMP type II receptor expresse

21 ollecting ducts, we observed coexpression of ActRIIA, Dragon, and BMP4 but not BMPRII.

22 ation of the soluble extracellular domain of ActRIIA fused to a murine IgG2a-Fc, increases bone forma

23 These findings demonstrate the importance of ActRIIA in addition to ActRIIB in mediating myostatin an

24 ngs suggest that RGMa facilitates the use of ActRIIA by endogenous BMP2 and BMP4 ligands that otherwi

25 not ActRIIB, and HJV enhances utilization of ActRIIA by BMP-2 and BMP-4.

26 via BMPRII and that increased utilization of ActRIIA leads to generation of an enhanced BMP signal.

27 he crystal structure of the type II receptor ActRIIA with dorsomorphin and demonstrate that dorsomorp

28 s signaling through the BMP type II receptor ActRIIA.

29 eptor for activin, type II activin receptor (ActRIIA), by administration of the soluble extracellular

30 ies that ActRIIB and its subfamily receptor, ActRIIA, cooperatively mediate the Gdf11 signal in patte

31 Here, mutations of activin receptors ActRIIA and ActRIIB are shown to disrupt the development

32 and betaB subunits and the activin receptors ActRIIA and ActRIIB was demonstrated by RT-PCR.

33 the three type II TGF-beta family receptors ActRIIA, ActRIIB, and BMPRII have been implicated in ALK

34 n that the type II TGF-beta family receptors ActRIIA, ActRIIB, and BMPRII interact with a large group

35 V selectively uses the BMP type II receptors ActRIIA and BMPRII, but not ActRIIB, and HJV enhances ut

36 The type II activin receptors, ActRIIA and ActRIIB, have been shown to play critical ro

37 on, and RGMa-mediated BMP signaling required ActRIIA expression.

38 We demonstrate that ActRIIA and BMPRII physically interact, and that each al

39 Further analyses revealed that ActRIIA(-/-)ActRIIB(+/-) and about 15% of the ActRIIA(-/

40 en together, these observations suggest that ActRIIA ligand traps may have therapeutic relevance in b

41 both receptor mutations by interbreeding the ActRIIA and ActRIIB knockout mutants.

42 ctRIIA(-/-)ActRIIB(+/-) and about 15% of the ActRIIA(-/-) embryos failed to form an elongated primiti