Ask about this productRelated genes to: BMP4 protein
- Gene:
- BMP4 NIH gene
- Name:
- bone morphogenetic protein 4
- Previous symbol:
- BMP2B
- Synonyms:
- -
- Chromosome:
- 14q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1990-06-11
- Date modifiied:
- 2016-10-05
Related products to: BMP4 protein
Related articles to: BMP4 protein
- Gastrointestinal cancer (GIC) frequently causes cancer cachexia, the major feature of which is the loss of skeletal muscle mass. The degradation of muscular proteins by cancer‑derived factors in the major pathogenesis of cancer‑induced muscle wasting is a known phenomenon. However, this mechanism has mainly been demonstrated using rodent cancer cells, and it may not always be applicable to human cancer types. Impaired skeletal muscle differentiation and regeneration have attracted attention as alternative inducers of cancer cachexia. The present study revealed that conditioned medium from four human GIC cell lines inhibited C2C12 myoblast differentiation by inducing the expression of the inhibitor of DNA binding (Id) proteins Id1 and Id3, which mediated via bone morphogenetic protein (BMP)‑Smad signaling. The results suggested that BMP‑Smad1/5/8‑Id signaling inhibited the expression of a MRF member, myogenin and its downstream myogenic genes, thus leading to unsuccessful differentiation into myotubes. Furthermore, the present study identified high levels of BMP4 secretion from these four human GIC cell lines and demonstrated that an inhibitor of BMP receptor, dorsomorphin or abrogation of BMP4 by siRNA in the GIC cells restored myogenic differentiation in C2C12 cells. The present study uncovered, for the first time, that BMP4 derived from human GIC cells exogenously inhibited myoblast differentiation by activating the Smad1/5/8‑Id signaling axis. In the future, this study may help to elucidate the complicated mechanisms underlying cancer‑induced cachexia in humans. - Source: PubMed
Publication date: 2026/05/15
Higure KazukiKitajima YoshihikoKimura NaoyaIkeda ShotaMatsufuji ShoheiTanaka TomokazuNoshiro Hirokazu - Human pluripotent stem cells (hPSCs) present considerable potential for regenerative medicine; however, the standardization and large-scale production of these cells are hindered by an incomplete understanding of the molecular mechanisms governing self-renewal. The long non-coding RNA ESRG is integral to maintaining hPSC self-renewal, with its depletion leading to reduced levels of nucleophosmin 1 (NPM1) protein, thereby compromising the self-renewal capacity of hPSCs. Mechanistically, ESRG physically interacts with NPM1, and a reduction in ESRG/NPM1 expression results in elevated bone morphogenetic protein 4 (BMP4) levels and decreased polypyrimidine tract-binding protein 1 (PTBP1) levels, which in turn destabilize TGF-β1 mRNA and attenuate TGF-β signaling activity. Notably, treatment with the TGF-β agonist SRI-011381 partially rescues the self-renewal defects caused by ESRG or NPM1 knockdown. Collectively, our findings elucidate that the ESRG-NPM1-BMP4-PTBP1 axis governs hPSC self-renewal by post-transcriptionally regulating TGF-β1 mRNA stability and sustaining TGF-β signaling. This study enhances the understanding of the molecular regulatory network underlying hPSC self-renewal maintenance and validates ESRG as a promising target for improving the in vitro expansion of hPSCs. - Source: PubMed
Publication date: 2026/05/11
Liao ZilingZhao CongWang LeiLiu WeidongTeng JiajingXie WenOuyang JinhaoYao ChaoyanHuan QianpingLei XuanFu YuXuanZhou BoJiang XingjunRen Caiping - The role of telomerase reverse transcriptase (TERT) in bone metabolism remains poorly defined. This study investigates its function in osteoporosis (OP) pathogenesis and its therapeutic potential. - Source: PubMed
Publication date: 2026/05/05
Ma JinjinYuan XiaonanXiao YaoWang HuanHong YouzhiZhang YangChen YuanZheng HoufengLi JiayingLi Bin - Laryngotracheal fibrosis is a rare but severe complication of prolonged intubation, leading to airway narrowing, respiratory distress, dysphonia, and, in advanced cases, life-threatening airway obstruction. Current treatments are primarily surgical, while pharmacologic approaches such as mitomycin C, corticosteroids, or 5-fluorouracil show inconsistent efficacy and potential toxicity. Thus, there remains a critical need for safe and effective antifibrotic therapies. Transforming growth factor-beta (TGF-β) is a key mediator of fibrosis, promoting fibroblast activation, migration, and expression of profibrotic markers such as alpha-smooth muscle actin (α-SMA). - Source: PubMed
Publication date: 2026/05/09
Toth EnikoSzabo KittiVegh Attila GergelyZvara AgnesPuskas Laszlo GBach AdamMigh EdeHorvath PeterTiszlavicz LaszloRovo LaszloKeller-Pinter Aniko - Birds and mammals exhibit extraordinary facial diversity, reflecting adaptations to distinct ecological niches and feeding strategies. While core face-building developmental programs are conserved and orchestrated by interactions between ectodermal organizers and the underlying mesenchyme, mechanisms driving facial shape variation remain poorly understood. Here, we integrate single-cell transcriptomic and chromatin accessibility profiling of mouse and chicken developing face to construct a comparative regulatory map. Although both ectodermal and mesenchymal populations display distinct regulatory features in each species, the mesenchyme exhibits markedly greater divergence, pointing to its central role in shaping facial morphology. We further reveal unexpected molecular complexity in the main face-shaping organizer, including a mouse-specific expression domain. At key morphogen loci (, , and ), conserved and lineage-specific enhancers exhibit spatially restricted activity patterns that mirror divergent signaling domains. These findings demonstrate how cis-regulatory evolution modulates conserved developmental programs to generate morphological novelty, providing a valuable resource for studying vertebrate facial evolution. - Source: PubMed
Publication date: 2026/05/06
Kyomen StellaSeton Louk W GCook Laura EEscamilla-Vega ElioMurillo-Rincón Andrea PJacobsen AlexanderDamatac AmorFortmann-Grote CarstenFuss JaninaVisel AxelKaucká Markéta