ArticlePloS one2011
A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Fatty acid-binding protein is essential for molting and male mating in Dermanyssus gallinae and confers protection as a vaccine antigen.Pest management science · 2026Article
- A Comprehensive Exploration of Bioluminescence Systems, Mechanisms, and Advanced Assays for Versatile Applications.Biochemistry research international · 2024Review
- Long-Read Genome Sequencing ofZoological studies · 2023Article
- Luminescent characteristics and mitochondrial COI barcodes of nine cohabitated Taiwanese fireflies.PeerJ · 2022Article
- Species-Specific Flash Patterns Track the Nocturnal Behavior of Sympatric Taiwanese Fireflies.Biology · 2022Article
- Azadirachtin-A fromACS omega · 2019Article
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- Short- and mid-wavelength artificial light influences the flash signals of Aquatica ficta fireflies (Coleoptera: Lampyridae).PloS one · 2018Article
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Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIntracellular fatty acid-binding proteins (FABPs) are considered to be an important energy source supplier in lipid metabolism; however, they have never been reported in any bioluminescent tissue before. In this study, we determined the structural and functional characteristics of a novel FABP (lcFABP) from the light organ of adult Taiwanese firefly, Luciola cerata, and showed anatomical association of lcFABP with photocytes. PRINCIPAL
findingsOur results demonstrated the primary structure of lcFABP deduced from the cDNA clone of light organ shares structural homologies with other insect and human FABPs. In vitro binding assay indicated the recombinant lcFABP binds saturated long chain fatty acids (C₁₄-C₁₈) more strongly than other fatty acids and firefly luciferin. In addition, tissue distribution screening assay using a rabbit antiserum specifically against the N-terminal sequence of lcFABP confirmed the light organ-specific expression of lcFABP. In the light organ, the lcFABP constituted about 15% of total soluble proteins, and was detected in both cytosol and nucleus of photocytes.
conclusionsThe specific localization of abundant lcFABP in the light organ suggests that sustained bioluminescent flashes in the light organ might be a high energy demanding process. In photocytes, lcFABP might play a key role in providing long chain fatty acids to peroxisomes for the luciferase-catalyzed long chain acyl-CoA synthetic reaction.
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