Galectin‐1 Is Implicated in the Protein Kinase C ε/Vimentin‐Controlled Trafficking of Integrin‐β1 in Glioblastoma Cells

Fortin, Shannon P.; Mercier, Marie Le; Camby, Isabelle; Spiegl-Kreinecker, Sabine; Berger, Walter; Lefranc, Florence; Kiss, Róbert

doi:10.1111/j.1750-3639.2008.00227.x

Cited by 56 publications

(46 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Inhibition of galectin expression, using siRNA or antisense sequences, showed significant results in colon [233], ovarian [234], esophageal [235], hepatocarcinoma [236], glioma [237], glioblastoma [238], and melanoma [239] cell lines. Anti-galectin mAbs and Gal-3 recombinant were also effective in vitro studies with diverse cell lines [240-242].…”

Section: Discussionmentioning

confidence: 99%

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Silva-filho¹,

Sena²,

Lima

et al. 2017

Cell Physiol Biochem

View full text Add to dashboard Cite

Post-translational and co-translational enzymatic addition of glycans (glycosylation) to proteins, lipids, and other carbohydrates, is a powerful regulator of the molecular machinery involved in cell cycle, adhesion, invasion, and signal transduction, and is usually seen in both in vivo and in vitro cancer models. Glycosyltransferases can alter the glycosylation pattern of normal cells, subsequently leading to the establishment and progression of several diseases, including cancer. Furthermore, a growing amount of research has shown that different oxygen tensions, mainly hypoxia, leads to a markedly altered glycosylation, resulting in altered glycan-receptor interactions. Alteration of intracellular glucose metabolism, from aerobic cellular respiration to anaerobic glycolysis, inhibition of integrin 3α1β translocation to the plasma membrane, decreased 1,2-fucosylation of cell-surface glycans, and galectin overexpression are some consequences of the hypoxic tumor microenvironment. Additionally, increased expression of gangliosides carrying N-glycolyl sialic acid can also be significantly affected by hypoxia. For all these reasons, it is possible to realize that hypoxia strongly alters glycobiologic events within tumors, leading to changes in their behavior. This review aims to analyze the complexity and importance of glycoconjugates and their molecular interaction network in the hypoxic context of many solid tumors.

show abstract

Section: Discussionmentioning

confidence: 99%

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Silva-filho¹,

Sena²,

Lima

et al. 2017

Cell Physiol Biochem

View full text Add to dashboard Cite

show abstract

“…Furthermore, galectin-1, a homodimeric adhesion molecule, is linked with the trafficking of 1-integrin, which is controlled by a PKC /vimentindependent pathway. These molecular responses are important for glioma cell migration [209]. In PMA-induced adhesion and migration of glioma cells, PKC shows different response compared to PKC in regard to ERK activation.…”

Section: Gastrointestinal Stromal Tumormentioning

confidence: 99%

Protein Kinase C (PKC) Isozymes and Cancer

Kang

2014

New Journal of Science

View full text Add to dashboard Cite

Protein kinase C (PKC) is a family of phospholipid-dependent serine/threonine kinases, which can be further classified into three PKC isozymes subfamilies: conventional or classic, novel or nonclassic, and atypical. PKC isozymes are known to be involved in cell proliferation, survival, invasion, migration, apoptosis, angiogenesis, and drug resistance. Because of their key roles in cell signaling, PKC isozymes also have the potential to be promising therapeutic targets for several diseases, such as cardiovascular diseases, immune and inflammatory diseases, neurological diseases, metabolic disorders, and multiple types of cancer. This review primarily focuses on the activation, mechanism, and function of PKC isozymes during cancer development and progression.

show abstract

“…Active trafficking maintains pools of active and inactive integrins that are used by the cell during adhesion and motility Margadant et al, 2011). Vimentin, a binding partner of nestin, regulates the integrin recycling pathway (Fortin et al, 2010;Ivaska et al, 2005;Kim et al, 2010). Accordingly, we investigated whether nestin regulates integrin trafficking.…”

Section: Nestin Does Not Affect Integrin Trafficking or Degradationmentioning

confidence: 99%

Nestin regulates prostate cancer cell invasion by influencing FAK and integrin localisation and functions

Hyder

Lazaro

Pylvänäinen

et al. 2014

Journal of Cell Science

View full text Add to dashboard Cite

BSTRACTNestin, an intermediate filament protein and marker of undifferentiated cells, is expressed in several cancers. Nestin is important for neuronal survival and is a regulator of myogenesis but its function in malignancy is ambiguous. We show that nestin downregulation leads to a redistribution of phosphorylated focal adhesion kinase (pFAK, also known as PTK2) to focal adhesions and alterations in focal adhesion turnover. Nestin downregulation also leads to an increase in the protein levels of integrin a5b1 at the cell membrane, activation of integrin b1 and an increase in integrin clustering. These effects have striking consequences for cell invasion, as nestin downregulation leads to a significant increase in pFAK-and integrin-dependent matrix degradation and cell invasion. Our results indicate that nestin regulates the localisation and functions of FAK and integrin. Because nestin has been shown to be prevalent in a number of specific cancers, our observations have broad ramifications for the roles of nestin in malignant transformation.

show abstract

Galectin‐1 Is Implicated in the Protein Kinase C ε/Vimentin‐Controlled Trafficking of Integrin‐β1 in Glioblastoma Cells

Cited by 56 publications

References 33 publications

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Protein Kinase C (PKC) Isozymes and Cancer

Nestin regulates prostate cancer cell invasion by influencing FAK and integrin localisation and functions

Contact Info

Product

Resources

About