Ask about this productRelated genes to: Lgals4 Blocking Peptide
- Gene:
- LGALS4 NIH gene
- Name:
- galectin 4
- Previous symbol:
- -
- Synonyms:
- GAL4
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-08-24
- Date modifiied:
- 2016-05-13
Related products to: Lgals4 Blocking Peptide
Related articles to: Lgals4 Blocking Peptide
- Intervertebral disc (IVD) degeneration is associated with severe clinical symptoms including chronic back pain. Galectins are a family of carbohydrate-binding proteins, some of which can induce functional disease markers in IVD cells and other musculoskeletal tissues. Galectin-4 and -8 were shown to trigger disease-promoting activity in chondrocytes, but their effects on IVD cells have not been investigated yet. - Source: PubMed
Publication date: 2026/08/06
Strauss ChristineDjojic DanielStadlmann JohannesGrohs Josef GeorgAlphonsus JürgenSchmidt SebastianAndré SabinePichler Katharina MargaretaSavic-Ivanovic SaraCezanne MelanieRothbauer MarioWindhager ReinhardToegel Stefan - Galectins are β-galactoside-binding lectins that play essential roles in innate immunity. Among them, tandem-repeat galectins (TrGals), typically composed of two distinct carbohydrate-recognition domains (CRDs) connected by a linker peptide, are well established as key regulators of pathogen recognition and host defense in mammals. However, their structural diversity and immunological functions in teleost fish remain poorly understood. In this study, five TrGals (Gal-4, Gal-8a, Gal-8b, Gal-9, and Gal-9like) were identified in grass carp. Sequence and structural analysis revealed that Gal-8a/b, Gal-9, and Gal-9like possess the canonical two-CRD architecture, whereas Gal-4 uniquely contains four highly similar tandem-repeat domains. All five TrGals were broadly expressed across examined tissues, with predominant expression in the liver. Upon Aeromonas hydrophila infection, Gal-4, Gal-8a, Gal-8b, and Gal-9 were rapidly up-regulated at early time points (3-6 h). To elucidate the functional significance of CRD number, recombinant full-length CiGal-4 (CiGal4-full) and three truncated variants containing one, two, or three CRDs (CiGal4-1CRD, CiGal4-2CRD, and CiGal4-3CRD) were generated and systematically characterized. All recombinant proteins contained the conserved β-sheet structure typical of galectin CRDs. Functional assays revealed that CiGal4-full displayed the strongest growth-inhibitory activity against all tested bacteria, whereas CiGal4-1CRD showed the weakest effect. Notably, CiGal4-2CRD exhibited the most potent bactericidal activity, surpassing the full-length protein, while CiGal4-3CRD showed no further enhancement. CiGal4-full and CiGal4-2CRD showed superior carbohydrate-binding activities compared with the other variants. Collectively, these results reveal that CRD copy number alone does not linearly determine galectin function. Instead, domain organization and conformational coordination are critical for optimizing antimicrobial activity. This study provides new insights into the structure-function relationships and evolutionary diversification of galectins in teleosts and highlights their potential as novel antimicrobial and immunomodulatory agents in aquaculture. - Source: PubMed
Publication date: 2026/08/04
Xu HongzhouYang TianLiu HaixiaLi HuanjieCheng PingShen YuxinWang DiFan ZijunLiu Heyi - Frailty is a well-established clinical risk factor for dementia, but its underlying mechanisms remain poorly defined. We aimed to investigate whether proteomic signatures and individual proteins linked to frailty could predict and characterize the association between frailty and dementia. - Source: PubMed
Publication date: 2026/07/17
Zhang XiruHuang QingmeiHuang JielinZhang PeidongFeng XinLi ZhihaoRaper Daniel M SMao Chen - Lectin-glycosaminoglycan (GAG) interactions remain incompletely understood despite their potential roles in cell signaling and immune regulation. In this study, we performed a comprehensive profiling of the binding specificity of 49 types of human endogenous lectins-including SIGLECs, C-type lectins, and galectins-for GAGs using GAG microarrays. GAGs containing 6-O-sulfation, such as heparin (HP), chondroitin sulfate C (CSC), and chondroitin sulfate E (CSE), exhibited broad binding to multiple SIGLECs and C-type lectins, whereas non-sulfated or low-sulfated GAGs exhibited minimal interactions, indicating a strong dependence on sulfation patterns. In contrast, most galectins displayed little or no detectable binding to GAG. Notably, galectin-4 (Gal-4) uniquely exhibited significant affinity for 6-O-sulfated GAGs, particularly HP. Surface plasmon resonance analysis revealed high-affinity binding of Gal-4 to HP (Kd = 4.70 × 10 M), substantially stronger than its carbohydrate recognition domains, indicating cooperative contributions of both N- and C-terminal CRDs of Gal-4. Molecular dynamics simulations further supported a binding mode involving both N- and C-terminal domains. Consistent with these findings, Gal-4 bound to endogenous HP-positive mast cells, and this interaction was competitively inhibited by HP. Together, these results identify Gal-4 as a unique galectin with a noncanonical capacity to recognize sulfated GAGs, revealing an alternative glycan-recognition mechanism beyond the conventional β-galactoside paradigm. - Source: PubMed
Publication date: 2026/06/29
Sano KanaeNagatomo MeriShigematsu KatsunobuYamasaki KazuhikoAnh Dinh Xuan TuanShibuya AkiraOtsuka YuyaMinamisawa ToshikazuTateno Hiroaki - Prostate cancer (PC) progression and mortality are largely driven by therapeutic resistance, increasingly linked to dynamic tumor-stroma interactions. However, the molecular basis of cancer-fibroblast crosstalk remains incompletely understood, particularly the contribution of Interleukin (IL)-30, an emerging regulator of PC aggressiveness. Here, we demonstrate that IL30 produced by PC cells reprograms stromal fibroblasts via IL6Rα/gp130 signaling, activating AKT and TGF-β/BMP pathways to drive their proliferation and differentiation into pro-angiogenic cancer-associated fibroblasts (CAFs). Reciprocally, these fibroblasts amplify IL30-mediated tumor aggressiveness by enhancing oncogenic transcriptional programs and by promoting cancer cell migration. Notably, while fibroblast co-culture suppresses epithelial-mesenchymal transition (EMT)-associated genes in PC cells, including NOTCH1, SNAI1/2 and ZEB1, IL30 overexpression overrides this effect, inducing EMT regulators alongside key PC-associated genes, such as IL6, LGALS4, HAL, and SHBG, whose expression correlates with IL30 levels in clinical bone metastasis datasets. Using a two-organ-on-chip platform linking PC-fibroblast spheroids to a bone marrow-like niche, we show that fibroblasts enhance PC cell migration and colonization of the bone marrow microenvironment, effects potentiated by IL30 overexpression and largely abrogated by its genetic depletion. Collectively, these findings identify an IL30-driven tumor-stroma signaling axis that promotes microenvironmental remodeling and metastatic progression, highlighting a potential therapeutic target to counteract PC progression and treatment resistance. - Source: PubMed
Publication date: 2026/06/24
Ciummo Stefania LiviaSorrentino CarloMarchetti SimonaFieni CristianoLanuti PaolaDi Carlo Emma