{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Lipocalin 15 (LCN15) is a member of the evolutionarily conserved lipocalin family that shares the characteristic eight‐stranded β–barrel structure common to proteins serving as carriers for small hydrophobic ligands. Although direct functional studies on LCN15 are limited, its structural relatedness to several well‐characterized lipocalins provides important clues about its potential roles. For example, lipocalins expressed in the male reproductive tract have been implicated in facilitating sperm maturation and fertility, while other family members participate in pheromone binding, immune modulation, and the transport of lipids, retinoids, and steroid hormones."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In an extensive transcriptomic study of the olfactory epithelium, prominent over‐expression of lipocalins was observed, reinforcing the widespread role of this protein family in binding and shuttling small hydrophobic molecules that serve as odorant carriers, among other functions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n Importantly, high-resolution structural analysis of α1-microglobulin revealed that its closest structural relatives include the complement component C8γ, L–prostaglandin D synthase, and Lipocalin 15. This observation suggests that LCN15 might share similar ligand-binding capabilities that could be harnessed in transporting bioactive lipids, mediating haem scavenging, or contributing to redox-mediated detoxification processes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In summary, although the precise physiological functions of LCN15 remain to be elucidated, its conserved structure and close relation to other multifunctional lipocalins imply that it may play roles in binding hydrophobic molecules, modulating cellular signaling, and protecting tissues by facilitating the transport and sequestration of potentially reactive compounds. Further targeted studies will be required to define the specific ligands and contextual functions of LCN15 in human physiology.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Katherine G Hamil, Qiang Liu, P Sivashanmugam, et al. "}, {"type": "b", "children": [{"type": "t", "text": "LCN6, a novel human epididymal lipocalin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Reprod Biol Endocrinol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1477-7827-1-112"}], "href": "https://doi.org/10.1186/1477-7827-1-112"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14617364"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14617364"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Georgia Charkoftaki, Yewei Wang, Monica McAndrews, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Update on the human and mouse lipocalin (LCN) gene family, including evidence the mouse Mup cluster is result of an \"evolutionary bloom\"."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Genomics (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s40246-019-0191-9"}], "href": "https://doi.org/10.1186/s40246-019-0191-9"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30782214"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30782214"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Tsviya Olender, Ifat Keydar, Jayant M Pinto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The human olfactory transcriptome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Genomics (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12864-016-2960-3"}], "href": "https://doi.org/10.1186/s12864-016-2960-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27515280"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27515280"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Winfried Meining, Arne Skerra "}, {"type": "b", "children": [{"type": "t", "text": "The crystal structure of human α(1)-microglobulin reveals a potential haem-binding site."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20120448"}], "href": "https://doi.org/10.1042/BJ20120448"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22512701"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22512701"}]}]}]}