Synonyms for actriib or Related words with actriib
Examples of "actriib"
Luspatercept is a recombinant fusion protein derived from human activin receptor type IIb (
) linked to a protein derived from immunoglobulin G.
The signaling complex for bone morphogenetic proteins (BMP) start with a ligand binding with a high affinty type I receptor (ALK1-7) followed by the recruitment of a type II receptor(ActRIIA,
, BMPRII). The first receptor kinase domain is then trans-phosphorylated by the apposed, activating type II receptor kinase domain. GDF2 binds ALK1 and
with the highest affinity in the BMPs, it also binds, with a lower affinity ALK2, also known has Activin A receptor, type I (ACVR1), and the other type II receptors BMPRII and ActRIIA. GDF2 and BMP10 are the only ligands from the TGF-β superfamily that can bind to both type I and II receptors with equally high affinity. This non-discriminative formation of the signaling complex open the possibility of a new mechanism. In cell type with low expression level of
, GDF2 might still signal due to its affinity to ALK1, then form complex with type II receptors.
ACE-031 is an engineered decoy receptor used in attempts to treat children with Duchenne Muscular Dystrophy (DMD). The ACE-031 receptor circulates outside the muscle-fiber membrane. Because this receptor binds to myostatin, it lowers the amount of myostatin that can bind to the native receptor in the membrane (
), preventing myostatin from delivering the muscle growth-limiting signal.
Myostatin is produced as promyostatin, a precursor protein kept inactive by the latent TGF-β binding protein 3 (LTBP3). Pathological cardiac stress promotes N-terminal cleavage by furin convertase to create a biologically active C-terminal fragment. The mature myostatin is then segregated from the latent complex via proteolytic cleavage by BMP-1 and tolloid metallopreoteinases. Free myostatin is able to bind its receptor,
, and increase SMAD2/3 phosphorylation. The latter produces a heteromeric complex with SMAD4, inducing myostatin translocation into the cardiomyocyte nucleus to modulate transcription factor activity. Manipulating the muscle creatinine kinase promoter can modulate myostatin expression, although it has only been observed in male mice thus far.
Human anatomy is asymmetric with the heart located on the left side and the liver on the right. Asymmetry is a feature common to all vertebrates and even paired-symmetric organs such as lungs display asymmetries in the number of lobes. Evidence that nodal signaling is responsible for left-right specification comes from genetic analysis of organisms deficient in left-right specification. These genetic studies led to identification of mutations in components in the nodal signaling pathway such as
, Criptic, and FoxH1 in mouse. These studies found that the left-right symmetry is created as a result of nodal antagonist expression on the right side of the embryo which is balanced by nodal upregulating itself on the other half of the embryo. The result is a nodal gradient that is high on the ventral side of the embryo and, through antagonist action, declines as a gradient to the midline.
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