Request Demo

Last update 08 May 2025

LGALS8

Last update 08 May 2025

Basic Info

Synonyms

Gal-8, galectin 8, Galectin-8

+ [6]

Introduction

Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture (PubMed:22246324, PubMed:28077878). Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324, PubMed:28077878). Required to restrict infection of bacterial invasion such as S.typhimurium (PubMed:22246324). Also required to restrict infection of Picornaviridae viruses (PubMed:28077878). Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans (PubMed:21288902).

Drugs associated with LGALS8

HG-1058

Target

LGALS4 x LGALS8

Mechanism

LGALS4 modulators [+1]

Active Org.-

Originator Org.

Human Genome Sciences, Inc.

Active Indication-

Inactive Indication

Immune System Diseases [+3]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

HG-1059

Target

LGALS8 x MAGEA10

Mechanism

LGALS8 modulators [+1]

Active Org.-

Originator Org.

Human Genome Sciences, Inc.

Active Indication-

Inactive Indication

Immune System Diseases [+2]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with LGALS8

100 Translational Medicine associated with LGALS8

0 Patents (Medical) associated with LGALS8

382

Literatures (Medical) associated with LGALS8

01 Jun 2025·European Journal of Cell Biology

Galectin-8 drives ERK-dependent mitochondrial fragmentation, perinuclear relocation and mitophagy, with metabolic adaptations for cell proliferation

Article

Author: Retamal, Claudio ; Veloso-Bahamondes, Francisco ; Tapia, Diego ; Pérez-Molina, Francisca ; González, Alfonso ; Oyanadel, Claudia ; Randow, Felix ; Díaz-Valdivia, Nicole ; Cancino, Jorge ; Soza, Andrea ; de la Peña, Adely

Mitochondria adapt to the cell proliferative demands induced by growth factors through dynamic changes in morphology, distribution, and metabolic activity. Galectin-8 (Gal-8), a carbohydrate-binding protein that promotes cell proliferation by transactivating the EGFR-ERK signaling pathway, is overexpressed in several cancers. However, its impact on mitochondrial dynamics during cell proliferation remains unknown. Using MDCK and RPTEC kidney epithelial cells, we demonstrate that Gal-8 induces mitochondrial fragmentation and perinuclear redistribution. Additionally, mitochondria adopt donut-shaped morphologies, and live-cell imaging with two Keima-based reporters demonstrates Gal-8-induced mitophagy. ERK signaling inhibition abrogates all these Gal-8-induced mitochondrial changes and cell proliferation. Studies with established mutant versions of Gal-8 and CHO cells reveal that mitochondrial changes and proliferative response require interactions between the N-terminal carbohydrate recognition domain of Gal-8 and α-2,3-sialylated N-glycans at the cell surface. DRP1, a key regulator of mitochondrial fission, becomes phosphorylated in MDCK cells or overexpressed in RPTEC cells in an ERK-dependent manner, mediating mitochondrial fragmentation and perinuclear redistribution. Bafilomycin A abrogates Gal-8-induced cell proliferation, suggesting that mitophagy serves as an adaptation to cell proliferation demands. Functional analysis under Gal-8 stimulation shows that mitochondria maintain an active electron transport chain, partially uncoupled from ATP synthesis, and an increased membrane potential, indicative of healthy mitochondria. Meanwhile, the cells exhibit increased extracellular acidification rate and lactate production via aerobic glycolysis, a hallmark of an active proliferative state. Our findings integrate mitochondrial dynamics with metabolic adaptations during Gal-8-induced cell proliferation, with potential implications for physiology, disease, and therapeutic strategies.

01 Jun 2025·Archives of Medical Research

Galectins: A New Frontier in Gastroesophageal Reflux Disease Research

Article

Author: Mahdi, Batool Mutar ; Salih, Wafaa Hazim ; Al-Khalidy, Huda Saleem Hantoosh Hameed

BACKGROUNDGastroesophageal reflux disease (GERD) is a common chronic condition characterized by abnormal reflux and regurgitation of stomach contents into the esophagus. Its prevalence is increasing worldwide and poses a high economic burden.AIMTo explore the potential correlation between galectin-1, galectin-3, galectin-8, galectin-9, and GERD, highlighting their potential role as biomarkers in disease diagnosis, and pathogenesis.MATERIALS AND METHODSA prospective cross-sectional study was conducted on 40 patients with GERD disease and 40 healthy control subjects from January 2023-May 2024 at Al-Kindy Teaching Hospital-Gastroenterology Unit. Venous blood was collected from patients and controls. Serums of both groups were quantified for galectin-1, galectin-3, galectin-8, and galectin-9 using a human ELISA kit.RESULTSGalectin-1 showed no statistically significant difference in the median levels between patients with GERD and controls (p = 0.567). A significant difference was found in the median levels of galectin-3, with higher levels in patients with GERD compared to controls (p = 0.0037). The most significant was galectin-3, AUC = 0.684 (95% CI: 0.570-0.784), p = 0.003, had a significant moderate discriminatory ability in differentiating between patients with GERD and healthy controls with cutoff value <13.682, sensitivity = 74.4%, specificity = 55%, and accuracy = 61.7%.CONCLUSIONSThis study suggests that serum galectin-3 is the best potential noninvasive diagnostic biomarker for the prediction and identification of GERD.

01 Mar 2025·Virology

Galectin-8 and GEL01 as potential adjuvants to enhance the immune response induced by a DNA vaccine against bovine alphaherpesvirus Type-1

Article

Author: Quattrocchi, Valeria ; Tribulatti, María Virginia ; Langellotti, Cecilia Ana ; Cheuquepán, Felipe Andrés ; Moore, Prando Dadin ; Zamorano, Patricia Inés ; Gammella, Mariela ; Carabelli, Julieta ; Campetella, Oscar ; Bidart, Juan Esteban ; Soria, Ivana ; Kornuta, Claudia Alejandra ; Hecker, Yanina Paola ; Prato, Cecilia Arahí

Bovine alphaherpesvirus-1 (BoAHV-1) causes several symptoms in cattle, leading to significant costs for the livestock industry. In this study, we used a plasmid encoding a secreted form of BoAHV-1 glycoprotein D (pCIgD) as a DNA vaccine. To enhance the potency of the pCIgD vaccine, we used Montanide™ GEL01 PR (GEL01) and introduced Galectin-8 (Gal-8), a lectin considered a novel adjuvant due to its immunostimulatory effects, into the formulation. Animals were vaccinated with pCIgD, pCIgD with Gal-8 (pCIgD-Gal-8), pCIgD with Gal-8 and GEL01 (pCIgD-Gal-8-GEL01), or the control plasmid pCIneo. The immune response was first assessed in a mouse model and then in bovines. The results showed that combining Gal-8 and GEL01 with pCIgD modulated immune responses at both the humoral and cellular levels in both animal models. This study evaluates the efficacy of a DNA vaccine with Gal-8 and GEL01 as potential adjuvants to enhance immune protection against BoAHV-1.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

LGALS8

Basic Info

Related

Analysis