Publications by authors named "Ludivine Perrocheau"

Article Synopsis
  • - RdCVF is a protective protein secreted by rod photoreceptors that helps prevent cone cell degeneration, which is crucial in retinitis pigmentosa (RP) leading to blindness.
  • - The study found that RdCVF interacts with Basigin-1, which in turn facilitates glucose entry into cone cells through the GLUT1 transporter, enhancing their survival through aerobic glycolysis.
  • - A specific mutation in RdCVF prevents it from binding to Basigin-1, disrupting glucose uptake and contributing to cone cell death in RP, highlighting a novel way to protect nerve cells by boosting glucose metabolism.
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Rod-derived cone viability factor (RdCVF) is produced by the Nxnl1 gene that codes for a second polypeptide, RdCVFL, by alternative splicing. Although the role of RdCVF in promoting cone survival has been described, the implication of RdCVFL, a putative thioredoxin enzyme, in the protection of photoreceptors is presently unknown. Using a proteomics approach we identified 90 proteins interacting with RdCVFL including the microtubule-binding protein TAU.

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Lipid transfer proteins (LTPs) are ubiquitous plant lipid-binding proteins that have been associated with multiple developmental and stress responses. Although LTPs typically bind fatty acids and fatty acid derivatives in a non-covalent way, studies on the LTPs of barley seeds have identified an abundantly occurring covalently modified form, LTP1b, the lipid ligand of which has resisted clarification. In the present study, this adduct was identified as the alpha-ketol 9-hydroxy-10-oxo-12(Z)-octadecenoic acid.

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Barley lipid transfer protein (LTP1) is a heat-stable and protease-resistant albumin that concentrates in beer, where it participates in the formation and stability of beer foam. Whereas the barley LTP1 does not display any foaming properties, the corresponding beer protein is surface-active. Such an improvement is related to glycation by Maillard reactions on malting, acylation on mashing, and structural unfolding on brewing.

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Proteins determine the quality of barley in malting and brewing end-uses. In this regard, water-soluble barley proteins play a major role in the formation, stability, and texture of head foams. Our objective was to survey the barley seed proteins that could be involved in the foaming properties of beer.

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