Results 51 to 60 of about 65,797 (247)

Synapsin-Promoted Caveolin-1 Overexpression Maintains Mitochondrial Morphology and Function in PSAPP Alzheimer’s Disease Mice

open access: yesCells, 2021
Mitochondrial dysfunction plays a pivotal role in the Alzheimer’s Disease (AD) pathology. Disrupted mitochondrial dynamics (i.e., fusion/fission balance), which are essential for normal mitochondria structure and function, are documented in AD.
Shanshan Wang   +5 more
doaj   +1 more source

Caveolin as a Potential Drug Target for Cardiovascular Protection

open access: yesFrontiers in Physiology, 2012
Caveolae and caveolin are key players in a number of disease processes. Current research indicates that caveolins play a significant role in cardiovascular disease and dysfunction.
Stephanie L Sellers   +2 more
doaj   +1 more source

The trafficking and targeting of P2X receptors [PDF]

open access: yes, 2013
The functional expression of P2X receptors at the plasma membrane is dependent on their trafficking along secretory and endocytic pathways. There are seven P2X receptor subunits, and these differ in their subcellular distributions because they have very ...
Murrell-Lagnado, Ruth D   +1 more
core   +3 more sources

The role of lipid metabolism in neuronal senescence

open access: yesFEBS Open Bio, EarlyView.
Disrupted lipid metabolism, through alterations in lipid species or lipid droplet accumulation, can drive neuronal senescence. However, lipid dyshomeostasis can also occur alongside neuronal senescence, further amplifying tissue damage. Delineating how lipid‐induced senescence emerges in neurons and glial cells, and how it contributes to ageing and ...
Dikaia Tsagkari   +2 more
wiley   +1 more source

Sirtuin1 protects endothelial Caveolin-1 expression and preserves endothelial function via suppressing miR-204 and endoplasmic reticulum stress. [PDF]

open access: yes, 2017
Sirtuin1 (Sirt1) is a class III histone deacetylase that regulates a variety of physiological processes, including endothelial function. Caveolin1 (Cav1) is also an important determinant of endothelial function. We asked if Sirt1 governs endothelial Cav1
Gabani, Mohanad   +10 more
core   +3 more sources

Intercompartmental communication in senescence

open access: yesFEBS Open Bio, EarlyView.
Senescent cells experience structural changes in the plasma membrane, endoplasmic reticulum, mitochondria, lysosomes, nucleus, and cytoskeleton. These alterations disrupt crosstalk among cellular compartments, impairing vesicular trafficking, contact sites, and molecular flow.
Krystyna Mazan‐Mamczarz   +3 more
wiley   +1 more source

Caveolin-1 Dependent Endocytosis Enhances the Chemosensitivity of HER-2 Positive Breast Cancer Cells to Trastuzumab Emtansine (T-DM1).

open access: yesPLoS ONE, 2015
The humanized monoclonal antibody-drug conjugate trastuzumab emtansine (T-DM1, Kadcyla) has been approved by the U.S. FDA to treat human epidermal growth factor receptor 2 (HER-2)-positive metastatic breast cancer.
Yuan-Chiang Chung   +4 more
doaj   +1 more source

Hepatitis B virus X protein suppresses caveolin-1 expression in hepatocellular carcinoma by regulating DNA methylation

open access: yesBMC Cancer, 2012
Background To understand the molecular mechanisms of caveolin-1 downregulation by hepatitis B virus X protein (HBx). Methods The DNA methylation status of the caveolin-1 promoter was examined by nested methylation-specific PCR of 33 hepatitis B virus ...
Yan Jun   +5 more
doaj   +1 more source

Lipid compartments and lipid metabolism as therapeutic targets against coronavirus

open access: yesFrontiers in Immunology, 2023
Lipids perform a series of cellular functions, establishing cell and organelles’ boundaries, organizing signaling platforms, and creating compartments where specific reactions occur.
Daniella Cesar-Silva   +5 more
doaj   +1 more source

Analysis of CD44-containing lipid rafts: Recruitment of annexin II and stabilization by the actin cytoskeleton [PDF]

open access: yes, 1999
CD44, the major cell surface receptor for hyaluronic acid (HA), was shown to localize to detergent-resistant cholesterol-rich microdomains, called lipid rafts, in fibroblasts and blood cells.
Oliferenko, S.   +8 more
core   +1 more source

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