Recycling of galectin-3 in epithelial cells

Hönig, Ellena; Schneider, Katharina; Jacob, Ralf

doi:10.1016/j.ejcb.2015.05.004

Cited by 29 publications

(21 citation statements)

References 80 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Owing to the fact that galectin-3 also alters polarized trafficking of glycoproteins (Hoenig et al, 2015), a correlation between the polarized distribution and the subcellular concentration of β1-integrin seems plausible. To test this directly, we analysed the surface distribution of β1-integrin in galectin-3-overexpressing and galectin-3-knockout cells by surface biotinylation.…”

Section: Galectin-3 Interacts With Integrins At the Apical Membrane Dmentioning

confidence: 99%

Galectin-3 modulates the polarized surface delivery of β1-integrin in epithelial cells

Hönig

Ringer

Dewes

et al. 2018

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

Epithelial cells require a precise intracellular transport and sorting machinery to establish and maintain their polarized architecture. This machinery includes β-galactoside-binding galectins for targeting of glycoprotein to the apical membrane. Galectin-3 sorts cargo destined for the apical plasma membrane into vesicular carriers. After delivery of cargo to the apical milieu, galectin-3 recycles back into sorting organelles. We analysed the role of galectin-3 in the polarized distribution of β1-integrin in MDCK cells. Integrins are located primarily at the basolateral domain of epithelial cells. We demonstrate that a minor pool of β1-integrin interacts with galectin-3 at the apical plasma membrane. Knockdown of galectin-3 decreases apical delivery of β1-integrin. This loss is restored by supplementation with recombinant galectin-3 and galectin-3 overexpression. Our data suggest that galectin-3 targets newly synthesized β1-integrin to the apical membrane and promotes apical delivery of β1-integrin internalized from the basolateral membrane. In parallel, knockout of galectin-3 results in a reduction in cell proliferation and an impairment in proper cyst development. Our results suggest that galectin-3 modulates the surface distribution of β1-integrin and affects the morphogenesis of polarized cells.

show abstract

Section: Galectin-3 Interacts With Integrins At the Apical Membrane Dmentioning

confidence: 99%

Galectin-3 modulates the polarized surface delivery of β1-integrin in epithelial cells

Hönig

Ringer

Dewes

et al. 2018

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…Secretion of Gal-3 in circulating systems was also elevated in a mouse model of radiation-induced lung fibrosis [ 10 ]. In addition, Gal-3 has been shown to be a binding partner of β-catenin and Axin to play a central role in Wnt/B-catenin signaling that is involved in upregulating extracellular matrix (ECM) constituents and matrix metalloproteinases (MMP) [ 11 , 12 ]. In summary, these data indicate that Gal-3 has a potent regulatory role in inflammation and fibrogenesis.…”

Section: Introductionmentioning

confidence: 99%

Association of Serum Galectin-3 with the Acute Exacerbation of Chronic Obstructive Pulmonary Disease

Feng

et al. 2017

Med Sci Monit

View full text Add to dashboard Cite

BackgroundAcute exacerbation of chronic obstructive pulmonary disease (AECOPD) aggravates the overall severity in COPD patients, resulting in severe morbidity and mortality. However, there are no objective biomarkers currently available to predict the development of AECOPD. Several studies have indicated that galectin-3 (Gal-3) is involved in diseases characterized by excessive inflammatory response and fibrosis. The objective of this study was to examine the dynamic changes of Gal-3 in acute exacerbation and convalescence phases of COPD.Material/MethodsSerum levels of Gal-3, high sensitivity C-reactive protein (hsCRP), and prohormone of brain natriuretic peptide (pro-BNP) were determined using multiplex enzyme-linked immunosorbent assay kits. Serum levels of Gal-3 in 44 patients with COPD were further analyzed and correlated with the parameters of lung function and the biomarkers of systemic inflammation.ResultsThe mean level of serum Gal-3 was significantly higher in acute exacerbation of COPD compared with the level in COPD convalescence phase (32.10±9.83 versus 29.02±8.68 ng/mL, p<0.01). Serum levels of Gal-3 positively correlated with hsCRP (r=0.354, p=0.018 for total patients) and pro-BNP (r=0.319, p=0.035 for total patients) in AECOPD. In addition, the level of Gal-3 was the highest in the current smoker group, and the lowest in the never-smoker group in either the acute exacerbation phase (33.91±3.55 versus 29.12±11.73 ng/mL, p=0.036) or the convalescence phase (30.94±3.40 versus 27.76±9.68 ng/mL, p=0.045) of COPD.ConclusionsOur results indicated that serum Gal-3 is increased in AECOPD patients, which is also positively associated with systemic inflammation and smoking in patients with COPD, suggesting that Gal-3 might be a valuable biomarker for AECOPD.

show abstract

“…Evidence has also suggested that N -glycans and O -glycans act as lumenal apical sorting signals in transcytosis, perhaps enabled by binding to the galectins such as galectin-3 (Honig et al 2015) and galectin-4 (Perez Bay et al 2014). Raft clustering, implicated in the biogenesis of apical membrane domains (Schuck and Simons 2004), may also contribute to transcytosis of GPI-APs (Galmes et al 2013).…”

Section: The Transcytotic Pathwaymentioning

confidence: 99%

Membrane Transport across Polarized Epithelia

García-Castillo

Chinnapen

Lencer

2017

Cold Spring Harb Perspect Biol

View full text Add to dashboard Cite

Polarized epithelial cells line diverse surfaces throughout the body forming selective barriers between the external environment and the internal milieu. To cross these epithelial barriers, large solutes and other cargoes must undergo transcytosis, an endocytic pathway unique to polarized cell types, and significant for the development of cell polarity, uptake of viral and bacterial pathogens, transepithelial signaling, and immunoglobulin transport. Here, we review recent advances in our knowledge of the transcytotic pathway for proteins and lipids. We also discuss briefly the promise of harnessing the molecules that undergo transcytosis as vehicles for clinical applications in drug delivery.

show abstract

Recycling of galectin-3 in epithelial cells

Cited by 29 publications

References 80 publications

Galectin-3 modulates the polarized surface delivery of β1-integrin in epithelial cells

Galectin-3 modulates the polarized surface delivery of β1-integrin in epithelial cells

Association of Serum Galectin-3 with the Acute Exacerbation of Chronic Obstructive Pulmonary Disease

Membrane Transport across Polarized Epithelia

Contact Info

Product

Resources

About