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Membranes: a meeting point for lipids, proteins and therapies
Open accessAbstract
Membranes constitute a meeting point for lipids and proteins. Not only do they define the entity of cells and cytosolic organelles but they also display a wide variety of important functions previously ascribed to the activity of proteins alone. Indeed, lipids have commonly been considered a mere support for the transient or permanent association of membrane proteins, while acting as a selective cell/organelle barrier. However, mounting evidence demonstrates that lipids themselves regulate the location and activity of many membrane proteins, as well as defining membrane microdomains that serve as spatio-temporal platforms for interacting signalling proteins. Membrane lipids are crucial in the fission and fusion of lipid bilayers and they also act as sensors to control environmental or physiological conditions. Lipids and lipid structures participate directly as messengers or regulators of signal transduction. Moreover, their alteration has been associated with the development of numerous diseases. Proteins can interact with membranes through lipid co-/post-translational modifications, and electrostatic and hydrophobic interactions, van der Waals forces and hydrogen bonding are all involved in the associations among membrane proteins and lipids. The present study reviews these interactions from the molecular and biomedical point of view, and the effects of their modulation on the physiological activity of cells, the aetiology of human diseases and the design of clinical drugs. In fact, the influence of lipids on protein function is reflected in the possibility to use these molecular species as targets for therapies against cancer, obesity, neurodegenerative disorders, cardiovascular pathologies and other diseases, using a new approach called membrane-lipid therapy.
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“The depolarized resting Vm in cancer cells relative to that in non-cancer cells is thought to be caused by altered lipid and sterol membrane composition, which results in an influx of sodium ions into the cell and a collection of negative charges on the cell coat [70].”
From Permeabilizing Cell Membranes with Electric Fields (2021) · cites this paper as [70]
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Metadata
- Authors
- Escribá, P. V., González‐Ros, J. M., Goñi, F. M., Kinnunen, P. K. J., Vigh, L., Sánchez‐Magraner, L., Fernández, A. M., Busquets, X., Horváth, I., & Barceló‐Coblijn, G.
- Affiliations
- Research Institute of Health Sciences (ES)
- University of the Basque Country (ES)
- University of Helsinki (FI)
- HUN-REN Szegedi Biológiai Kutatóközpont (HU)
- Corresponding author
- Escribá, Pablo V.
- Goñi, Félix M.
- Kinnunen, Paavo K. J.
- Barceló‐Coblijn, Gwendolyn
- ORCID
- Venue
- Journal of Cellular and Molecular Medicine
- Publisher
- Wiley
- Published
- 2008-05-21
- Volume
- 12
- Issue
- 3
- Pages
- 829-875
- ISSN
- 1582-1838 (ISSN-L)
- 1582-4934
- PMC
- PMC4401130
- OpenAlex
- W2008091140
- Cited by
- 454
- References
- 347
- Citations by year
- 2026: 22 · 2025: 39 · 2024: 22 · 2023: 35 · 2022: 35 · 2021: 29 · 2020: 30 · 2019: 32 · 2018: 33 · 2017: 23 · 2016: 24 · 2015: 34 · 2014: 17 · 2013: 22 · 2012: 18
- FWCI
- 1.00
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Cellular and Molecular Medicine (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- membrane lipids, membrane proteins, protein-lipid interactions, lipid rafts, signal transduction, lipid sensing, cancer therapy, obesity, neurodegenerative diseases, cardiovascular disease
- MeSH terms
- Animals, Drug Therapy, Humans, Membrane Lipids, Membrane Proteins, Models, Biological, Molecular Structure
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