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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Activin A receptor, type IIB

ActRIIB, ACVR2B, activin receptor type IIB, activin receptor IIB
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: SFRP1, myostatin, ActRIIA, fibrillin-1, ALK4
Papers using ActRIIB antibodies
Misexpression of chick Vg1 in the marginal zone induces primitive streak formation
Dodd Jane et al., In Neural Development, 1996
... Sigma); rat α-Netrin-1 (R&D Systems); rabbit α-ActRII (H65) and goat α-ActRIIB (N16) (Santa Cruz); mouse α-ActRIIB (abcam, Cambridge, MA USA); and ...
Papers on ActRIIB
Activin B induces noncanonical SMAD1/5/8 signaling via BMP type I receptors in hepatocytes: evidence for a role in hepcidin induction by inflammation in male mice.
Babitt et al., Reggio nell'Emilia, Italy. In Endocrinology, Feb 2016
Activin B stimulates hepcidin via classical Activin type II receptors ACVR2A and ACVR2B, noncanonical BMP type I receptors ALK2 and ALK3, and SMAD5.
Activin decoy receptor ActRIIB:Fc lowers FSH and therapeutically restores oocyte yield, prevents oocyte chromosome misalignments and spindle aberrations, and increases fertility in midlife female SAMP8 mice.
Merchenthaler et al., Baltimore, United States. In Endocrinology, Jan 2016
Activin is a molecule that raises FSH, and ActRIIB:Fc is an activin decoy receptor that binds and sequesters activin.
Identification of plasma microRNA expression profile in radiographic axial spondyloarthritis-a pilot study.
Haseeb et al., Cleveland, United States. In Clin Rheumatol, Jan 2016
The most repressed miRNA was miR-16 and is predicted to regulate the expression of activin A receptor (ACVR2B), a receptor for growth, and differentiation factor-5 (GDF-5).
Nodal promotes functional luteolysis via downregulation of progesterone and prostaglandins E2 and promotion of PGF2 alpha synthetic pathways in mare corpus luteum.
Ferreira-Dias et al., Olsztyn, Poland. In Endocrinology, Jan 2016
Expression pattern of Nodal and its receptors ACVR2B, Alk7 and Alk4, as well as Nodal physiological role, demonstrate the involvement of this pathway in functional luteolysis.
Growth and differentiation factor 11 (GDF11): Functions in the regulation of erythropoiesis and cardiac regeneration.
Vergely et al., Dijon, France. In Pharmacol Ther, Dec 2015
The binding of activins to activin type IIA (ActRIIA) or type IIB (ActRIIB) receptors induces the recruitment and phosphorylation of an activin type I receptor which then phosphorylates the Smad2 and Smad3 intracellular signaling proteins.
The soluble form of BMPRIB is a novel therapeutic candidate for treating bone related disorders.
Tomizuka et al., Machida, Japan. In Sci Rep, Dec 2015
Recently, several soluble BMP receptors, such as ActRIIA-Fc, ActRIIB-Fc, and ALK1-Fc, are undergoing clinical trials.
Transforming growth factor-β superfamily ligand trap ACE-536 corrects anemia by promoting late-stage erythropoiesis.
Kumar et al., Cambridge, United States. In Nat Med, 2014
Here we investigated regulation of erythropoiesis using a ligand-trapping fusion protein (ACE-536) containing the extracellular domain of human activin receptor type IIB (ActRIIB) modified to reduce activin binding.
Myostatin/activin pathway antagonism: molecular basis and therapeutic potential.
Goldberg et al., Thousand Oaks, United States. In Int J Biochem Cell Biol, 2013
Binding of myostatin and activin to the ActRIIB receptor complex on muscle cell membrane leads to activation of Smad2/3-mediated transcription, which in turn stimulates FoxO-dependent transcription and enhanced muscle protein breakdown via ubiquitin-proteasome system and autophagy.
Blockade of the activin receptor IIb activates functional brown adipogenesis and thermogenesis by inducing mitochondrial oxidative metabolism.
Feige et al., Basel, Switzerland. In Mol Cell Biol, 2012
ActRIIB inhibition enhanced energy expenditure only at ambient temperature or in the cold, where nonshivering thermogenesis is minimal, suggesting that brown fat activation plays a prominent role in the metabolic actions of ActRIIB inhibition.
Expression of inhibin/activin proteins and receptors in the human hypothalamus and basal forebrain.
Stopa et al., Providence, United States. In J Neuroendocrinol, 2012
Activin type IIB receptors are clearly demonstrable throughout the adult human hypothalamus and basal forebrain.
Interference with myostatin/ActRIIB signaling as a therapeutic strategy for Duchenne muscular dystrophy.
Hoogaars et al., Paris, France. In Curr Gene Ther, 2012
Since the discovery of the myostatin/ActRIIB signaling pathway 15 years ago, numerous strategies were developed to block its inhibitory function during skeletal muscle growth.
Activin receptor signaling: a potential therapeutic target for osteoporosis.
Baron et al., Boston, United States. In Curr Mol Pharmacol, 2012
The binding of activins to activin type IIA (ActRIIA) or type IIB (ActRIIB) receptors induces the recruitment and phosphorylation of an activin type I receptor (ALK4 and/or ALK7), which then phosphorylates the Smad2 and Smad3 intracellular signaling proteins.
Hormone therapy and maximal eccentric exercise alters myostatin-related gene expression in postmenopausal women.
Schroeder et al., Los Angeles, United States. In J Strength Cond Res, 2012
After eccentric exercise, postmenopausal women not using hormone therapy (HT) expressed lower levels of ActRIIb while postmenopausal women using HT showed a heightened response.
miR-192, miR-194, miR-215, miR-200c and miR-141 are downregulated and their common target ACVR2B is strongly expressed in renal childhood neoplasms.
Guertl et al., Graz, Austria. In Carcinogenesis, 2012
The interaction between all five miRNAs and ACVR2B was verified by an in vitro assay.
BMP3 suppresses osteoblast differentiation of bone marrow stromal cells via interaction with Acvr2b.
Rosen et al., Boston, United States. In Mol Endocrinol, 2012
findings best fit a model in which BMP3, produced by mature bone cells, acts to reduce BMP signaling through Acvr2b in skeletal progenitor cells, limiting their differentiation to mature osteoblasts
Crystal structure of activin receptor type IIB kinase domain.
Han, United States. In Vitam Horm, 2010
discussion of crystal structure of kinase domain of ActRIIB; structural analysis may be of help in developing selective inhibitors [REVIEW]
Reversing cachexia.
Tisdale, Birmingham, United Kingdom. In Cell, 2010
Zhou et al. (2010) now identify a new target for treating cachexia, the activin type-2 receptor (ActRIIB).
Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival.
Han et al., Thousand Oaks, United States. In Cell, 2010
Here, we show that in several cancer cachexia models, pharmacological blockade of ActRIIB pathway not only prevents further muscle wasting but also completely reverses prior loss of skeletal muscle and cancer-induced cardiac atrophy.
Loss-of-function mutations in the EGF-CFC gene CFC1 are associated with human left-right laterality defects.
Casey et al., Bethesda, United States. In Nat Genet, 2000
5), LEFTB (formerly LEFTY2; ref. 6) and ACVR2B (encoding activin receptor IIB; ref. 7).
Cloning of a second type of activin receptor and functional characterization in Xenopus embryos.
Kintner et al., Los Angeles, United States. In Science, 1992
A complementary DNA coding for a second type of activin receptor (ActRIIB) has been cloned from Xenopus laevis that fulfills the structural criteria of a transmembrane protein serine kinase.
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