{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n LGALSL—a gene product also known as HSPC159 or GRP—encodes a galectin‐related protein that, despite maintaining a conserved galectin‐like fold, exhibits distinct carbohydrate‐binding properties compared to classical galectins. Functional studies indicate that LGALSL is implicated in diverse pathophysiological processes. For instance, expression analyses in patients with minimal change nephrotic syndrome revealed that LGALSL mRNA is markedly up‐regulated in peripheral blood mononuclear cells during the nephrotic phase, suggesting that it may serve as a secreted factor that contributes to immune modulation and inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In breast cancer, gain‐and loss‐of–function experiments demonstrated that LGALSL promotes cellular proliferation, epithelial–mesenchymal transition, and metastasis by engaging intracellular signaling cascades such as the PI3K/Akt pathway, thereby designating it as a potential therapeutic target."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Structural studies have revealed that, while LGALSL preserves the overall galectin fold, subtle alterations in the carbohydrate recognition domain likely underlie its modified glycan binding behavior relative to prototypical galectins."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Moreover, mapping studies in retinal disease candidate regions have identified LGALSL among a set of genes expressed in ocular tissues, implicating it in retinal biology and potentially in the pathogenesis of retinitis pigmentosa."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " In addition, evolutionary analyses in nonmammalian vertebrates such as chicken demonstrate that the conserved LGALSL gene may have diverged in its saccharide‐binding capabilities, a variation that could impact cell adhesion and intracellular signaling in a tissue‐specific context."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n Collectively, these findings support a multifunctional role for LGALSL in modulating immune responses, cellular proliferation, and tissue morphogenesis. Further elucidation of its molecular interactions and signaling pathways may provide critical insights into its involvement in disease processes and its potential as a therapeutic target.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Atsushi Komatsuda, Hideki Wakui, Keiko Iwamoto, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "HSPC159 promotes proliferation and metastasis by inducing epithelial-mesenchymal transition and activating the PI3K/Akt pathway in breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Sci (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/cas.13631"}], "href": "https://doi.org/10.1111/cas.13631"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29737572"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29737572"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Dongwen Zhou, Jianping Sun, Wei Zhao, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Confirmation of linkage and refinement of the RP28 locus for autosomal recessive retinitis pigmentosa on chromosome 2p14-p15 in an Indian family."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Vis (2004)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15215745"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15215745"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Gabriel García Caballero, Andrea Flores-Ibarra, Malwina Michalak, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Galectin-related protein: An integral member of the network of chicken galectins 1. From strong sequence conservation of the gene confined to vertebrates to biochemical characteristics of the chicken protein and its crystal structure."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbagen.2016.06.001"}], "href": "https://doi.org/10.1016/j.bbagen.2016.06.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27268118"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27268118"}]}]}]}