Ask about this productRelated genes to: Lgals4 antibody
- 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 antibody
Related articles to: Lgals4 antibody
- Microbial cell surfaces exhibit a remarkable diversity of complex carbohydrate structures, with most strains producing unique glycan coats distinct from those found on mammalian cells. However, some microbes employ carbohydrate-based molecular mimicry, potentially as a strategy to evade adaptive immune responses. This phenomenon is particularly intriguing in microbes capable of generating ABO blood group-like glycans. While molecular mimicry of host glycans may reduce adaptive immune recognition of specific host-like glycan epitopes expressed by bacteria, innate immune lectins known as galectins have been shown to recognize these glycan structures expressed by bacteria, suggesting that they may contribute to host defense against microbes that utilize molecular mimicry. Flow cytometry using fluorescently labeled galectins provides a powerful tool for examining galectin-bacteria interactions, including engagement of microbes that express blood group-like antigens. Herein, we describe the approaches used for investigating lectin-microbial interactions by flow cytometry. - Source: PubMed
Paul AnuJan Hau-MingMuthusamy SasikalaWu Shang-ChuenAlton Abraham BScott William OStowell Carter JJajosky Ryan PPaz DominiqueArthur Connie M - 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