Ask about this productRelated genes to: TGFB1I1 antibody
- Gene:
- TGFB1I1 NIH gene
- Name:
- transforming growth factor beta 1 induced transcript 1
- Previous symbol:
- -
- Synonyms:
- Hic-5, TSC-5, ARA55, HIC-5
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-23
- Date modifiied:
- 2016-10-05
Related products to: TGFB1I1 antibody
Related articles to: TGFB1I1 antibody
- Naturally occurring isoforms of the proto-oncogene Erb-B2 Receptor Tyrosine Kinase 2 (ERBB2, HER2) incite unique pathways of tumor progression in mouse models of breast cancer. Although each isoform has been shown to progress to metastasis, the N-terminally truncated isoform (p95) was previously shown to be biased toward early distant dissemination prior to detection. Here we show how HER2 isoforms differentially promote go-or-grow phenotypes through biased utilization of tyrosine autophosphorylation sites in the intracellular tail of HER2. Fluorescently barcoded humanized full-length HER2 (WT), exon-16 splice HER2 isoform (d16), and p95 expressing tumor cell lines were derived from HER2 Crainbow mice, then utilized for a series of functional assays including proliferation, tumor growth rate, cell motility, collective cell migration, cellular morphology, and invasive potential. Quantitative analysis reveals biased tumor cell behaviors across each genotype. WT tumor cells are biased toward proliferation and collective migration, d16 cells are biased toward proliferation and individual motility, and p95 tumor cells are biased toward individual motility and invasion. Single cell analysis reveals a myogenic-like state transition in p95 cells accompanied by an increased nuclear translocation of the Myocardin Related Transcription Factor A (MRTFA). MRTFA knockdown, as well as knockdown of a downstream effector, Transforming growth factor beta 1 induced transcript 1 (TGFB1I1), both inhibit the p95 invasive phenotype. Furthermore, intracellular residue tyrosine 1139 (Y1139) is necessary for MRTFA translocation, and when edited in p95 cells (Y1139F) invasion and motility phenotypes are subsequently lost. Our data illustrate the importance of functionally selective signaling in HER2 and highlight the need for therapeutics that intercept metastasis by targeting HER2 biased signaling. - Source: PubMed
Publication date: 2026/07/23
Fernandes Joseph DBresnahan ErinZawada HillaryGinzel Joshua DLyerly H KimRogers Bruce WKavuri Shyam MIntrone Allison JSadecki Melanie RMori HidetoshiDoherty GlennBorowsky Alexander DFlores Kevin BBravo-Cordero Jose JavierSnyder Joshua C - Type I collagen is the most abundant form of collagen and forms the organic component of bone. Pathogenic variants in genes encoding its constituent polypeptide chains, and , can result in autosomal dominant osteogenesis imperfecta and other connective tissue disorders. Although osteogenesis imperfecta is clinically well-described, the molecular basis of clinical heterogeneity among patients is not well understood. We undertook a global proteomic approach to uncover alterations in osteogenesis imperfecta patient bone-derived stromal cells as well as their secretome. We performed multiplexed tandem mass tag (TMT)-based proteomics analysis of cells from three patients along with three controls to investigate global changes in the proteome of these cells as well as their secretome. This was combined with analysis of proline hydroxylation to catalog the modification of type I collagens in this disorder. We observed significant changes in both the cellular and secreted proteomes including the levels of proteins involved in osteoblast proliferation such as nitric oxide synthase-interacting protein (NOSIP), secreted frizzled-related protein 1 (SRFP1) and transforming growth factor beta-1-induced transcript 1 protein (TGFB1I1) as well as others involved in endoplasmic reticulum homeostasis such as protein disulfide isomerase A6 (PDIA6) and reticulophagy regulator 3 (RETREG3). Notably, a number of alterations were observed in proline hydroxylation in intracellular collagens - COL1A1 and COL1A2. These findings expand our current understanding of the cellular pathophysiology in osteogenesis imperfecta and could lead to the identification of novel therapeutic targets. - Source: PubMed
Publication date: 2026/07/22
Garapati KishoreMun Dong-GiDevasahayam Arokia Balaya RexSaraswat MayankRenuse SantoshTrahan GregoryKandasamy Richard KDeyle David RPandey Akhilesh - Stomach adenocarcinoma (STAD) represents a significant global health challenge, characterized by high heterogeneity in its tumor microenvironment. This study aimed to create a cell composition assessment tool and identify STAD-associated biomarkers by combined analysis of single-cell RNA sequencing (scRNA-seq) and bulk RNA-seq data. - Source: PubMed
Publication date: 2026/07/15
Wu SiyiCai ManzhongCai JiajiaChen Yong'an - Tuberculosis continues to pose a severe global public health challenge. This study aims to explore the shared hub genes of latent tuberculosis infection (LTBI) and active tuberculosis (ATB). - Source: PubMed
Publication date: 2026/05/20
Yang XingzhenChang MingLiu Fengzhen - Nonalcoholic steatohepatitis (NASH) is a metabolic disease characterized by hepatic steatosis and inflammation among other features. Dysregulated lipid metabolism is crucial in the pathogenesis of NASH. However, its regulatory mechanisms remain intricate and poorly elucidated. Hepatic stellate cells (HSCs) have been reported to contribute to hepatocellular lipid metabolism dysregulation and aggravate NASH progression. However, the potential mechanisms remain unclear. Here, we demonstrate that hydrogen peroxide-inducible clone 5 (Hic-5), which is highly expressed in HSCs within the liver, is elevated in NASH patients and mouse models. Hic-5 deficiency alleviates hepatic steatosis, and liver metabolomics revealed reduced fatty acid levels. Meanwhile, RNA-sequencing revealed that Hic-5 deficiency increases AMPK phosphorylation. Additionally, HSC-specific overexpression of Hic-5 exacerbates NASH severity. Co-culture experiments indicated that Hic-5 increases hepatocellular fatty acid synthesis. Cellular transcriptomic analysis and validation revealed that prostaglandin E2 (PGE2), secreted by HSCs, mediates hepatocellular fatty acid synthesis. Mechanistically, the N-terminal domain of Hic-5 binds c-Src, leading to phosphorylation of PTEN, which is bound to the C-terminal domain. This event subsequently induces phosphorylation and nuclear translocation of the transcription factor SP1, ultimately increasing PGE2 secretion. Finally, Hic-5 promotes hepatocellular fatty acid synthesis by activating the PGE2-EP4 axis. Pharmacological inhibition of EP4 in HSC-specific Hic-5 overexpression mice fed with HFD diet (HFD) significantly attenuated NASH progression. These findings increase our understanding of molecular mechanisms linking hepatic lipid metabolism dysregulation and may offer therapeutic potential for treating NASH. - Source: PubMed
Publication date: 2026/02/09
Huang ZhiweiTan PengGu BoyuanLiu ShengluLi HanChen JiatongRen BingyuSun LeiWen JianLi YuFu Wenguang