Food Sci Biotechnol
Department of Marine Life Science, College of Life Science, Gangneung-Wonju National University, Gangneung, 25457 Gangwon Republic of Korea.
Published: February 2025
This study investigated the anti-inflammatory effects of OJlipo1, a lipocalin-like protein derived from . Through cloning and expressing OJlipo1 in , and subsequent rigorous characterization including amino acid analysis and mass spectrometry, its potential against inflammation was evaluated. Studies on lipopolysaccharide-stimulated RAW 264.7 cells highlighted its capability to suppress nitric oxide synthase and cyclooxygenase-2 expression, as well as its interference with nuclear factor kappa B and mitogen-activated protein kinase pathways, which are essential for toll-like receptor 4 (TLR4) signaling. Utilizing TAK242, a TLR4 pathway inhibitor, reinforced OJlipo1's specific targeting mechanism. These findings underscore OJlipo1's significant anti-inflammatory potential, aligning with the traditional uses of , and suggest new therapeutic avenues, especially for diseases associated with TLR4 dysregulation. This validates the traditional application of in inflammation and positions OJlipo1 as a promising therapeutic candidate, enriching our understanding of its molecular underpinnings and therapeutic prospects.
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http://dx.doi.org/10.1007/s10068-024-01700-2 | DOI Listing |
Food Sci Biotechnol
February 2025
Department of Marine Life Science, College of Life Science, Gangneung-Wonju National University, Gangneung, 25457 Gangwon Republic of Korea.
This study investigated the anti-inflammatory effects of OJlipo1, a lipocalin-like protein derived from . Through cloning and expressing OJlipo1 in , and subsequent rigorous characterization including amino acid analysis and mass spectrometry, its potential against inflammation was evaluated. Studies on lipopolysaccharide-stimulated RAW 264.
View Article and Find Full Text PDFACS Chem Biol
April 2024
Laboratoire Molécules de Communication et Adaptation des Micro-organismes UMR 7245, Muséum National d'Histoire Naturelle, CNRS, Sorbonne Universités; CP54, 57 rue Cuvier, 75005 Paris, France.
Fungal paracyclophane-decahydrofluorene-containing natural products are complex polycyclic metabolites derived from similar hybrid PKS-NRPS pathways. Herein we studied the biosynthesis of pyrrocidines, one representative of this family, by gene inactivation in the producer coupled to thorough metabolic analysis and molecular modeling of key enzymes. We characterized nine pyrrocidines and analogues as well as in mutants a variety of accumulating metabolites with new structures including rare -decalin, cytochalasan, and fused 6/15/5 macrocycles.
View Article and Find Full Text PDFJ Med Chem
April 2024
Department of Dermatology & Venerology, West China Hospital, Sichuan University, Chengdu 610041, China.
Lipid transfer proteins (LTPs) are crucial players in nonvesicular lipid trafficking. LTPs sharing a lipocalin lipid transfer domain (lipocalin-like proteins) have a wide range of biological functions, such as regulating immune responses and cell proliferation, differentiation, and death as well as participating in the pathogenesis of inflammatory, metabolic, and neurological disorders and cancer. Therefore, the development of small-molecule inhibitors targeting these LTPs is important and has potential clinical applications.
View Article and Find Full Text PDFContact (Thousand Oaks)
October 2023
Department of Biology/Chemistry, Bioanalytical Chemistry Section, Osnabrück University, Osnabrück, Germany.
Ceramides, as key components of cellular membranes, play essential roles in various cellular processes, including apoptosis, cell proliferation, and cell signaling. Ceramides are the precursors of all complex sphingolipids in eukaryotic cells. They are synthesized in the endoplasmic reticulum and are further processed at the Golgi apparatus.
View Article and Find Full Text PDFBiochimie
May 2023
School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou, 510640, PR China. Electronic address:
Triabin, a lipocalin-like thrombin inhibitor from the saliva of the blood-sucking triatomine bug Triatoma pallidipennis, exhibits effective inhibition comparable to hirudin despite binding exclusively at exosite I. Interestingly, it was reported that higher triabin doses would not inhibit thrombin completely, which makes it a promising antithrombotic candidate agent with a larger therapeutic window. However, few structural and functional studies about triabin have been reported in the past three decades, mostly due to the lack of a reliable and practicable recombinant expression technology for this seemingly small protein.
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