Glycosylation is one of the essential modifications of proteins and lipids. It is carried out mainly in the endoplasmic reticulum and Golgi apparatus, and requires a specific molecular machinery associating several hundreds of glycosyltransferases, glycosidases, transporters and regulating proteins. Modifications of glycosylation are found in numerous diseases, notably in cancers. All types of glycosylation can be affected and this leads to dysfunctions of cellular metabolism. In this review, we present the current knowledge on the regulation of glycosylation mechanisms and illustrate how the alteration of these regulatory mechanisms can lead to abnormal protein and lipid glycosylation, and take part in the development of cancers.
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http://dx.doi.org/10.1051/medsci/2021082 | DOI Listing |
J Recept Signal Transduct Res
January 2025
Laboratory of Clinical Pharmaceutics, Gifu Pharmaceutical University, Gifu, Japan.
Lysyl oxidase (LOX), a copper-containing secretory oxidase, plays a key role in the regulation of extracellular stiffness through cross-linking with collagen and elastin. Among the LOX family of enzymes, LOX-like 4 (LOXL4) exhibits pro-tumor and anti-tumor properties; therefore, the functional role of LOXL4 in tumor progression is still under investigation. Here, we first determined that transforming growth factor-β1 (TGF-β1) significantly decreased LOXL4 expression in human breast cancer MDA-MB-231 cells, which suggested that decreased LOXL4 may participate in tumor progression.
View Article and Find Full Text PDFSci Rep
January 2025
Department of Life Technologies, Division of Biotechnology, University of Turku, Medisiina D, 5th floor, Kiinamyllynkatu 10, 20520, Turku, Finland.
Glycosylation changes of circulating proteins carrying the CA19-9 antigen may offer new targets for detection methods to be explored for the diagnosis of epithelial ovarian cancer (EOC). Search for assay designs for targets initially captured by a CA19-9 antigen reactive antibody from human body fluids by probing with fluorescent nanoparticles coated with lectins or antibodies to known EOC associated proteins. CA19-9 antigens were immobilized from ascites fluids, ovarian cyst fluids or serum samples using monoclonal antibody C192 followed by probing of carrier proteins using anti-MUC16, anti-MUC1 and, anti STn antibodies and seven lectins, all separately coated on nanoparticles.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, No. 2025 Chengluo Avenue, Chengdu 610106, China. Electronic address:
Steamed egg (SE), a traditional egg dish, exhibits steaming time-dependent textural properties. This study investigated the molecular mechanisms underlying SE gel formation and deterioration through quantitative proteomics combined with physicochemical characterization. Results showed optimal gel formation at 11 min steaming, while prolonged steaming (23 min) led to gel cracking and sensory deterioration.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832003, China; Key Laboratory of Characteristics Agricultural Product Processing and Quality Control (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs, Shihezi University, Shihezi, Xinjiang 832000, China; Key Laboratory for Food Nutrition and Safety Control of Xinjiang Production and Construction Corps, Shihezi University, Shihezi, Xinjiang 832000, China. Electronic address:
The limited solubility, rapid metabolism, and poor bioavailability of curcumin restrict its application. In this study, we synthesized chickpea protein isolate (CPI)-citrus pectin (CP) conjugates to prepare an emulsion delivery system that enhances the stability and bioavailability of curcumin. The CPI-CP emulsion achieved a curcumin encapsulation efficiency of 86.
View Article and Find Full Text PDFCarbohydr Res
January 2025
Faculty of Chemistry, University of Wrocław, Wrocław, 50-383, Poland.
Triggered by the urgent need to tackle the global crisis of multidrug-resistant bacterial infections, in this work, we present a way to overcome chloramphenicol resistance by introducing modifications based on the glycosylation of its hydroxyl groups. The synthesized derivatives demonstrate complete resistance to the action of recombinant chloramphenicol acetyltransferase (CAT) from Escherichia coli and efficacy against methicillin-resistant Staphylococcus aureus (MRSA), Escherichia coli ESBL, and Pseudomonas aeruginosa ATCC 27853. Glycosylation gives chloramphenicol an additional advantage - the stable glycosidic form is less toxic to human dermal fibroblasts and has significantly better water solubility than non-glycosylated chloramphenicol.
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