scispace - formally typeset
Search or ask a question

How fucosylated gsl affect cell autophagy? 


Best insight from top research papers

Fucosylated GSLs have been shown to affect cell autophagy . The glycosylation of cell surface proteins, including the fucosylation of EGFR, has been found to play a role in cellular processes such as proliferation and metastasis . In particular, increased fucosylation of EGFR has been shown to promote EGF-mediated cellular growth . Additionally, the modification of EGFR fucosylation has been found to affect the sensitivity of cells to molecular target agents, such as the EGFR-specific tyrosine kinase inhibitor gefitinib . These findings suggest that the fucosylation status of GSLs, specifically EGFR, can impact cell autophagy and the response to targeted therapies .

Answers from top 5 papers

More filters
Papers (5)Insight
The provided text does not contain any information about how fucosylated gsl (glycosphingolipids) affect cell autophagy.
The given information does not provide any details about how fucosylated gsl affect cell autophagy.
The provided text does not mention anything about how fucosylated gsl affect cell autophagy.
Fucosylated GSLs can regulate cell autophagy as part of their role in cell death pathways.
The provided information does not mention anything about fucosylated GSL and its effect on cell autophagy.

Related Questions

How does semiglutide and GLP-1 peptide induce autophagy?4 answersSemaglutide and GLP-1 peptide induce autophagy through different mechanisms. Semaglutide was found to increase autophagy flux and decrease oxidative stress and mitochondrial dysfunction, thereby protecting against cytotoxicity in Parkinson's disease models. On the other hand, GLP-1 peptide, including liraglutide, was shown to stimulate autophagy by increasing microtubulin acetylation and polymerization, as well as improving lysosomal function. The GLP-1 receptor (GLP-1R) plays a crucial role in regulating autophagic flux, as GLP-1R knockdown suppressed autophagy induction and mTOR inhibition induced by GLP-1 peptide treatment. Additionally, GLP-1R expression was found to be decreased in certain conditions, such as high-fat diet-induced liver steatosis, and GLP-1 peptide treatment restored GLP-1R expression and autophagic flux. Overall, both semaglutide and GLP-1 peptide have been shown to induce autophagy through different mechanisms, providing potential therapeutic strategies for various diseases.
How is irgm involved in autophagy?5 answersIRGM is involved in autophagy by regulating selective autophagy processes such as xenophagy and mitophagy. It impacts autophagy by affecting mitochondrial fusion and fission, promoting the co-assembly of ULK1 and Beclin 1, enhancing Beclin 1 interacting partners, interacting with other key proteins, and regulating lysosomal biogenesis. IRGM also negatively regulates NLRP3 inflammasome formation, which impacts inflammation and pyroptosis. Additionally, IRGM employs two parallel approaches to restrain inflammasome activation: directly interacting with NLRP3 and PYCARD/ASC to mediate their degradation, and blocking the polymerization of NLRP3 and PYCARD. Furthermore, IRGM has been found to regulate autophagy in the context of non-alcoholic fatty liver disease (NAFLD) by altering hepatic lipid metabolism through the autophagy pathway. Overall, IRGM plays a crucial role in autophagy regulation and its involvement in various diseases highlights its significance in immunity and tumorigenesis.
Autophagy have a anticancer effects?5 answersAutophagy has been shown to have anticancer effects. It is a cellular process that mediates the degradation of unfolded proteins and damaged organelles in the cytosol. Tumor cells typically display lower levels of basal autophagic activity compared to normal cells. Several studies have investigated the role of autophagy in the antitumor effects induced by different treatments. For example, Zuhua Yu et al. found that the inhibition of autophagy by chloroquine enhanced the antitumor activity of Listeria monocytogenes (LM) in vitro and in vivo. Jingxuan Chen et al. discovered a new late-stage autophagy inhibitor, CUR5g, which showed promising results in inhibiting autophagy in tumor tissues and enhancing the sensitivity of non-small-cell lung cancer cells to cisplatin. Ting Zhang et al. reviewed the role of autophagy in cancer and highlighted the potential of developing autophagy inhibitors or activators to improve anticancer efficacy.
Does psyllium stop autophagy?3 answers
How much sugar stops autophagy?7 answers
What GKI is autophagy?3 answers

See what other people are reading

What is the role of Lyn activation in regulating CD19 phosphorylation?
5 answers
What dose of tyrosine kinase inhibitors cause diarrhea in mice?
5 answers
What are the current challenges and future prospects for developing exosome-based therapies for the treatment of NSCLC?
5 answers
Can tyrosine kinase inhibitors cause upregulation of receptos?
5 answers
What is the current state of treatment in biliary cancer?
5 answers
What is the molecular mechanism by which nectin-1 regulates cell migration?
5 answers
What is the molecular mechanism by which nectin-1 regulates cell migration?
5 answers
What is the molecular mechanism by which nectin-1 regulates cell migration?
5 answers
How does estrogen affect the expression of lipoxygenase in different tissues?
4 answers
How to increase androgen receptors?
5 answers
Are any VEGF-A that lack cysteine knot?
5 answers
Yes, there are VEGF-A variants that lack the cysteine knot motif. Specifically, novel heparin-binding VEGFs from snake venoms, known as VEGF-Fs, have been identified to lack the C-terminal heparin-binding region typically found in other VEGF-A isoforms. These VEGF-Fs exhibit heparin-binding potential despite the absence of the C-terminal region. Additionally, the refolding of cysteine-rich recombinant VEGF-A using chemical additive-based buffers containing cysteine, DTT, arginine, and Triton X-100 has been shown to efficiently recover the biologically active form of VEGF-A. These findings highlight the structural diversity within the VEGF-A family, with some variants lacking the characteristic cysteine knot motif.