BMPR1A

Case study 1: Elaine Langenfeld, 2013

Bone morphogenetic proteins (BMPs) are highly conserved morphogens that are essential for normal development. BMP-2 is highly expressed in the majority of non-small cell lung carcinomas (NSCLC) but not in normal lung tissue or benign lung tumors. The effects of the BMP signaling cascade on the growth and survival of cancer cells is poorly understood.

BMP signaling is basally active in lung cancer cell lines, which can be effectively inhibited with selective antagonists of the BMP type I receptors. Lung cancer cell lines express alk2, alk3, and alk6 and inhibition of a single BMP receptor was not sufficient to decrease signaling. Inhibition of more than one type I receptor was required to decrease BMP signaling in lung cancer cell lines. BMP receptor antagonists and silencing of BMP type I receptors with siRNA induced cell death, inhibited cell growth, and caused a significant decrease in the expression of inhibitor of differentiation (Id1, Id2, and Id3) family members

Fig1. H1299 cells treated with 1 μM DMSO or 1 μM of selective BMP type I receptor antagonist for 12, 24, and 48 hours.

Fig2. Western blot analysis for Id1 in H1299 cells with knockdown of a single type I BMP receptor or combination knockdown of alk2 and alk3, or all 3 BMP type I receptors.

Case study 2: Heon-Woo Lee, 2023

Components of bone morphogenetic protein (BMP) signalling have been implicated in both pathogenesis of pulmonary arterial hypertension (PAH) and endothelial-mesenchymal transition (EndoMT). In particular, the importance of BMP type 2 receptor in these processes has been extensively analysed. However, the contribution of BMP type 1 receptors (BMPR1s) to the onset of PAH and EndoMT remains poorly understood. BMPR1A, one of BMPR1s, was recently implicated in the pathogenesis of PAH, and was found to be down-regulated in the lungs of PAH patients, neither the downstream mechanism nor its contribution to EndoMT has been described. Therefore, the researchers aim to delineate the role of endothelial BMPR1A in modulating EndoMT and pathogenesis of PAH.

BMPR1A knockdown in endothelial cells (ECs) induces hallmarks of EndoMT. Mechanistically, they identify ZEB1 as a primary target for BMPR1A in this setting; upon BMPR1A activation, ID2 physically interacts and sequesters ZEB1 to attenuate transcription of Tgfbr2, which in turn lowers the responses of ECs towards transforming growth factor beta (TGFβ) stimulation and prevents excessive EndoMT

Fig3. Western blots showing the expression of TGFBR2, SM22α, and ZEB1 and BMPR1A in control, BMPR1A, ZEB1, or BMPR1A/ZEB1 siRNA-treated PAECs.

Fig4. Western blots showing the expression of EndoMT markers (αSMA, SM22α, and TGFBR2) and BMPR1A in control, BMPR1A, TGFBR2, or BMPR1A/TGFBR2 siRNA-treated PAECs.

Fig1. Schematic representation of the TGF-β/BMP signaling cascade. (Thomas D Mueller, 2012)

Fig2. Model for signaling through ligand-mediated receptor hetero-oligomers and preformed complexes (PFCs). BMP receptor heterotetramers form prior to ligand binding. (Marcelo Ehrlich, 2012)

BMPR1A involved in several pathways and played different roles in them. We selected most pathways BMPR1A participated on our site, such as Cytokine-cytokine receptor interaction, TGF-beta signaling pathway, Hippo signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with BMPR1A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

BMPR1A has several biochemical functions, for example, ATP binding, RNA polymerase II transcription factor activity, sequence-specific DNA binding, SMAD binding. Some of the functions are cooperated with other proteins, some of the functions could acted by BMPR1A itself. We selected most functions BMPR1A had, and list some proteins which have the same functions with BMPR1A. You can find most of the proteins on our site.

BMPR1A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with BMPR1A here. Most of them are supplied by our site. Hope this information will be useful for your research of BMPR1A.

BMP2; GDF5; BMP4; BMP2; BMP2; FSTL1; HSP90AB1