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Related Concept Videos

TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
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Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
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Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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Regulation of Angiogenesis and Blood Supply

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Updated: Jun 12, 2026

Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-&#946; Signaling
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Basic FGF downregulates TSP50 expression via the ERK/Sp1 pathway.

Miao Wang1, Yong-Li Bao, Yin Wu

  • 1National Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun 130024, China.

Journal of Cellular Biochemistry
|May 28, 2010
PubMed
Summary

Basic fibroblast growth factor (bFGF) downregulates testes-specific protease 50 (TSP50) expression by activating the ERK/Sp1 pathway. This finding offers insights into TSP50 regulation for breast cancer therapy.

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Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-&#946; Signaling
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Published on: August 3, 2018

TGF-&#946;-mediated Endothelial to Mesenchymal Transition (EndMT) and the Functional Assessment of EndMT Effectors using CRISPR/Cas9 Gene Editing
07:05

TGF-β-mediated Endothelial to Mesenchymal Transition (EndMT) and the Functional Assessment of EndMT Effectors using CRISPR/Cas9 Gene Editing

Published on: February 26, 2021

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Signaling

Background:

  • Testes-specific protease 50 (TSP50) expression is elevated in breast cancer, promoting tumorigenesis.
  • Understanding TSP50's regulatory mechanisms is crucial for developing targeted tumor therapies.

Purpose of the Study:

  • To elucidate the mechanism by which basic fibroblast growth factor (bFGF) downregulates TSP50 expression.
  • To identify the signaling pathway involved in bFGF-mediated TSP50 transcriptional regulation.

Main Methods:

  • Utilized MDA-MB-231 and HEK293T cell lines.
  • Employed RT-PCR and promoter activity assays.
  • Investigated the roles of ERK and Sp1 signaling pathways, including inhibitor and dominant-negative mutant analyses.

Main Results:

  • bFGF downregulates TSP50 expression transcriptionally.
  • bFGF induces the phosphorylation of ERK and Sp1.
  • The ERK/Sp1 pathway is essential for bFGF-mediated TSP50 downregulation, with a key Sp1 site identified on the TSP50 promoter.

Conclusions:

  • bFGF downregulates TSP50 expression via the ERK-mediated phosphorylation of Sp1.
  • The identified bFGF/ERK/Sp1 signaling axis provides a potential therapeutic target for breast cancer treatment.