TSPAN4 influences glioblastoma progression through regulating EGFR stability
These videos have been matched automatically. Contact us if they are not relevant.
These videos have been matched automatically. Contact us if they are not relevant.
View abstract on PubMed
Summary
This summary is machine-generated.Tetraspanin 4 (TSPAN4) promotes glioblastoma (GBM) progression by stabilizing epidermal growth factor receptor (EGFR). High TSPAN4 expression correlates with poor GBM prognosis, suggesting TSPAN4 as a potential therapeutic target.
Area Of Science
- Oncology
- Molecular Biology
- Cell Biology
Background
- Glioblastoma (GBM) presents significant challenges in treatment due to high mortality and low cure rates.
- Tetraspanin 4 (TSPAN4) is identified as a migrasome marker, but its role in cancer, particularly GBM, remains unclear.
Purpose Of The Study
- To investigate the role of TSPAN4 in glioblastoma progression.
- To elucidate the molecular mechanisms by which TSPAN4 influences GBM growth and invasion.
Main Methods
- Analysis of TSPAN4 expression in clinical GBM samples.
- In vitro studies involving TSPAN4 knockdown and overexpression in GBM cells.
- In vivo tumorigenicity assays.
- Investigation of TSPAN4's interaction with epidermal growth factor receptor (EGFR) and downstream signaling pathways.
Main Results
- TSPAN4 is highly expressed in GBM and associated with poor patient prognosis.
- TSPAN4 knockdown inhibits GBM cell proliferation, invasion, and tumorigenicity.
- TSPAN4 interacts with EGFR, regulating its stability and inactivating downstream pathways (MEK/ERK, STAT3, AKT).
Conclusions
- TSPAN4 significantly promotes GBM progression by enhancing EGFR stability.
- TSPAN4 represents a potential therapeutic target for glioblastoma treatment.
These videos have been matched automatically. Contact us if they are not relevant.
These videos have been matched automatically. Contact us if they are not relevant.
Related Concept Videos
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
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...
Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits. Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl...
Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...