China
Africa
Explore chapters and articles related to this topic
Detection of Lysosomal Membrane Permeabilization
Published in Bruno Gasnier, Michael X. Zhu, Ion and Molecule Transport in Lysosomes, 2020
Anne-Marie Ellegaard, Line Groth-Pedersen, Marja Jäättelä
When LMP occurs, not only are the lysosomal contents released to the cytosol, but the soluble cytosolic proteins also gain access to the inside of the lysosomes. Among these are the galectin family proteins, which bind with high affinity to beta-galactosides. These sugars are not present in the cytosol, but the glycocalyx on the inside of the lysosomal membrane is rich in beta-galactosides. Consequently, when LMP occurs, the galectins gain access to lysosomal lumen, bind to beta-galactosides and rapidly accumulate inside the lysosomes. As demonstrated in Figure 8.2g, by visualizing galectins, even small levels of LMP can be detected as a punctate pattern in the cells (Aits et al., 2015b). This can be done either by immunocytochemical stainings or overexpression of a fluorescently tagged galectin. Here, we will concentrate on the immunocytochemical staining of galectins, but overexpression of fluorescently tagged galectin is more suitable in some experimental settings such as large-scale screening.
Molecular basis and biomarkers of disease activity
Published in Seema Chopra, Endometriosis, 2020
Other glycoprotein biomarkers include galectin-9, glycodelin A, and follistatin. Galectin-9 is basically an immunomodulatory protein. Studies have found its levels to be significantly elevated in endometriosis as compared with normal healthy women. However, the levels were also found to be elevated in females with other gynecological diseases, thereby suggesting that using high levels of galectin-9 may not be of practical utility to diagnose endometriosis [8].
Non-Hodgkin Lymphoma
Published in Tariq I. Mughal, Precision Haematological Cancer Medicine, 2018
The mechanisms responsible for rituximab resistance, and indeed other monoclonal antibodies, remain poorly understood. Remarkably, in murine models, there appears to be little correlation between the expression of CD20, nor gene expression profiles, between the responders and those who develop resistance. Interestingly, galectin-1 (Gal-1), an immune modulator, has appeared to play a role in the development of immunotherapy-resistance, at least in a murine model (so far).
Association between high galectin expression and poor prognosis in hematologic cancers: a systematic review and meta-analysis
Published in Hematology, 2023
Haotian Liu, Qiuying Dai, Yixian Li, Zhenfei Tang, Tiantian She
Previous studies have demonstrated the vital role of galectins in various biological and pathophysiological processes in vivo, including infection, inflammation, angiogenesis, immune escape, and tumor progression [13]. Galectins were observed to be expressed to varying degrees in heart disease [14–17], kidney disease [18–20] and various cancers [21–28]. Studies have shown that galectin can serve as a biomarker for diagnosis and prognosis, as well as a potential therapeutic target in multiple diseases [10]. Gal-3, as an early biomarker for thyroid cancer, is valuable in assisting the clinical diagnosis of thyroid cancer [29]. Gal-1 [30–33], Gal-3 [34–36], Gal-9 [37–39] and Gal-12 [40] also showed prognostic potential in acute myeloid leukemia (AML), chronic lymphocytic leukemia (CLL), classic Hodgkin lymphoma (CHL), non-Hodgkin lymphoma (NHL) and other hematologic cancers. However, a systematic review assessing the effect of galectins in the prognosis of hematologic cancers is still lacking.
Galectin-3 levels in school aged children with autism spectrum disorder
Published in International Journal of Developmental Disabilities, 2023
Abdülbaki Artık, Orhan Kocaman, Halil Kara, Sibel Çiğdem Tuncer
Another possible mechanism underlying the association between serum galectin-3 concentrations and ASD is changes in inflammatory parameters in ASD. Galectin-3 is clearly important in nervous system development and neuroinflammation (Dunn et al.2019). Galectin-3 plays a crucial role with both pro- and anti-inflammatory actions in inflammatory pathways (Boscher et al.2011). Galectin-3 was suggested to lead to increased inflammatory response by suppressing the anti-inflammatory cytokine interleukin-10 (IL-10) production (Jiang et al.2009). An in vitro survey also documented that galectin-3 induces IL-6 expression, whereas galectin-3 inhibition decreases IL-1β expression, implying that galectin-3 regulates the expression concentrations of cytokines associated with ASD (Chen et al.2013). Because these cytokines are involved in promoting inflammation in the central nervous system (Dunn et al.2019), increased galectin-3 may indicate worsening of neuroinflammation in OSB.
Interplay between EGFR, E-cadherin, and PTP1B in epidermal homeostasis
Published in Tissue Barriers, 2023
Tessa Arnaud, Fernando Rodrigues-Lima, Mireille Viguier, Frédérique Deshayes
However, there are other possible interactions through post-translational modifications such as glycosylation. Indeed, three canonical N-glycosylation sites in its extracellular domain were reported on EGFR in the UniProt database and several evidence that EGFR functions are linked to the N-glycosylation status of EGFR have been published.44 These results and the importance of EGFR glycosylation and E-cadherin glycosylation have been nicely illustrated recently by Manwar-Hussain and colleagues.49 Interestingly, we recently identified a galectin as a new partner of EGFR. Galectins are a family of proteins characterized by a common affinity for β-galactoside containing carbohydrates and an evolutionary conserved Carbohydrate Recognition Domain (CRD).39 Among them, galectin-7, which is restricted to the pluristratified epithelia, has newly been shown to impair EGFR phosphorylation through a direct interaction with the carbohydrates of EGFR extracellular domain.43 Moreover, galectin-7 was already known to regulate cell adhesion through the direct regulation of E-cadherin.38 Evidence has now been established by protein recombinant experiments and in silico data that this molecule establishes a bridge between E-cadherin and EGFR regulating the proliferation/differentiation balance notably in the skin43 (Figure 1c).