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Molecular Regulation of NO Synthase in the Heart
Published in Malcolm J. Lewis, Ajay M. Shah, Endothelial Modulation of Cardiac Function, 2020
Jean-Luc Balligand, Thomas W. Smith
The recent finding (Shaul et al., 1996) that palmitoylated and myristoylated NOS3 is localized to caveolae, which are plasmalemmal microdomains where other signaling molecules such as G-proteins are also compartmentalized (Schnitzer et al., 1995) raises the question of the possible involvement of one (or several) isoforms of caveolin in the regulation and subcellular translocation of NOS3. Caveolin, the principal component of caveolar membranes, has been shown to cycle between plasma membrane caveolae and the Golgi complex (Conrad et al., 1995), where NOS3 has also been localized (Sessa et al., 1995). Caveolin also directly interacts with heterotrimeric G-proteins and can recruit Ga-i2 onto reconstituted caveolin-rich membranes in vitro (Li et al., 1996). The tempting hypothesis that caveolin could also target acylated NOS3 to the membrane caveolae would be strongly supported by the demonstration of a direct interaction between recombinant NOS3 and caveolin, which is still lacking.
Cytotoxicology Studies of 2-D Nanomaterials
Published in Suresh C. Pillai, Yvonne Lang, Toxicity of Nanomaterials, 2019
Priyanka Ganguly, Ailish Breen, Suresh C. Pillai
NMs of size <200 nm are taken up via the caveolae-dependent endocytosis. This endocytosis method is a clathrin-independent intake method which is a mixture of pinocytosis and endocytosis facilitated by caveolae and glycolipid rafts. The caveolae are cholesterol and sphingolipid-rich invaginations of the plasma membrane and the glycolipid rafts are cholesterol-rich membrane fractions. The presence of the integral membrane protein caveolin helps to distinguish the invaginated domains of the plasma membrane. This technique of intake is able to avert the digestion in lysosomes of the ingested NMs. Thus, this receptor-independent endocytosis could be utilised effectually for drug or DNA delivery applications (Nabi and Le, 2003; Pelkmans et al., 2005; Richard et al., 2005; Singh et al., 2003). Rejman et al. reported the significance of the size of the particles in different endocytosis routes (Rejman et al., 2004). This study revealed that the entry portal is determined by the size of the particles. Therefore, an appropriate evaluation of other kinetic factors of internalisation could expand the drug delivery efficacy.
Gateways of Pathogenic Bacterial Entry into Host Cells—Salmonella
Published in K. Balamurugan, U. Prithika, Pocket Guide to Bacterial Infections, 2019
Balakrishnan Senthilkumar, Duraisamy Senbagam, Chidambaram Prahalathan, Kumarasamy Anbarasu
Caveolae, a 21–24 kDa integral membrane flask-shaped projection in the plasma membrane of endothelial cells, consist of three caveolin proteins named as caveolin 1, 2, and 3. Caveolin 1 and 2 are expressed together as a hetero oligomer in the plasma membrane, and caveolin 3 was expressed only in muscle tissue (Tang et al. 1996; Smart et al. 1999). Caveolin-1, a scaffolding protein expressed within the caveolar membrane, interacts with signaling proteins, such as epidermal growth factor receptor, G-proteins, Src-like kinases, Ha-Ras, insulin receptors, and integrins for regulating their activities (Smart et al. 1999). Caveolar endocytosis is an endocytosis mechanism including nutrients and pathogens in most of the prokaryotes and parasites via endoplasmic reticulum (ER) → golgi → cytoplasm not fuse with lysosome, letting helps the pathogens to escape from lysosomal degradation (Schnitzer et al. 1994).
Effects of caffeic acid phenethyl ester use and inhibition of p42/44 MAP kinase signal pathway on caveolin 1 gene expression and antioxidant system in chronic renal failure model of rats
Published in Drug and Chemical Toxicology, 2023
Yilmaz Cigremis, Hasan Ozen, Merve Durhan, Selahattin Tunc, Evren Kose
Caveolae are 50–80 nm diameter sack-like invaginations of the plasma membrane that are present in many cell types (Lamaze et al. 2017). They are highly important in membrane trafficking and play important roles in cellular bioactivities. Caveolae are composed of caveolins (CAV) and cavins. Three types of caveolins, CAV1, CAV2, and CAV3 are described. CAV1 is expressed in many cell types, such as adipocytes, endothelial cells, pneumocytes, fibroblasts, and smooth muscle cells (Cohen 2004). It is also shown to be normally expressed in distal convoluted tubules, collecting ducts, and parietal cells of Bowman capsule of normal human kidney (Tamaskar et al. 2007). Although CAV1−/− knockout mice were reported to be viable and fertile, lack of caveolae or caveolins were shown to cause muscle, pulmonary, or lipid disorders (Le Lay and Kurzchalia 2005). A wide distribution of CAV1, therefore, signifies its importance in cellular transmembrane activities.
Effect of ultraviolet radiation on the Nrf2 signaling pathway in skin cells
Published in International Journal of Radiation Biology, 2021
Alena Ryšavá, Jitka Vostálová, Alena Rajnochová Svobodová
Caveolins are the structural and scaffolding proteins of caveolae, small (50- to 100-nm) omega-shaped invaginations of the cell surface plasma membrane, rich in glycosphingolipids and cholesterol. Caveolae occur in a variety of cell types, including fibroblasts, epithelial and endothelial cells (Cohen et al. 2004; Volonte et al. 2013). There are three isoforms of caveolins (1-3). Cav-1 is the principal component of caveolae, with an unusual hairpin-like conformation that participates in vesicular trafficking and signals transduction events. It is expressed ubiquitously and Cav-1-enriched cellular organelles include the mitochondrion, the nucleus, the Golgi complex, and the endoplasmic reticulum (Wang et al. 2017). As has been documented, Cav-1 is an OS-related protein, as OS modulates the expression, posttranslational modification and degradation of Cav-1. Under basal conditions, Cav-1 constitutively interacts with Nrf2 in both the cytosol and nucleus. Under OS, ROS/RNS decreases Cav-1 expression, induces its proteasomal degradation and phosphorylation and also inhibits its palmitoylation, which decreases Cav-1 membrane association. These events result in reduced Cav-1-Nrf2 interaction, reviewed recently by (Wang et al. 2017) (Figure 3). In addition, Cav-1 knockdown affects the interaction between Nrf2 and Keap1 and increases Nrf2 transcription activity. Mutation of the Cav-1 binding motif on Nrf2 effectively attenuates their interaction and results in higher transcription activity of Nrf2-targeted genes. It also induces higher levels of antioxidant enzymes compared to wild-type control (Li et al. 2012).
Ultrasonically controlled albumin-conjugated liposomes for breast cancer therapy
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Nahid S. Awad, Vinod Paul, Mohammad H. Al-Sayah, Ghaleb A. Husseini
To internalize molecules from outside the cell, cells use a process called endocytosis. Via this process, cells can take up macromolecules, proteins and ligands [37]. The main endocytic routes are the clathrin-mediated endocytosis and the caveolae-mediated endocytosis. Caveolae are specialized membrane domains enriched in certain lipids cholesterol and proteins [38]. Caveolae can mediate endocytosis through a receptor-dependent or -independent fashion [39]. Caveolin-1 (Cav-1) is one of the main functional components of caveolae and plays an important role in caveolae formation. It expected that to induce tumour formation, rapid proliferation is required, and, therefore, downregulation of caveolin-1 expression may be necessary. The level of caveolin-1 is related to the invasiveness of the tumour [40]. According to Chatterjee et al. [41], nanoparticle conjugate of paclitaxel to HSA exhibits efficacy in pancreatic cancer, non–small cell lung cancer and breast cancer. The study found that Cav-1 protein levels correlated positively with cancer sensitivity to their albumin base nanoparticles and, therefore, caveolae are essential for the cancer uptake of albumin. In general, albumin binds to a cell-surface, 60-kDa glycoprotein (gp60) receptor (albondin). gp60 is localized in the caveolae and binds to caveolin-1 (an intracellular protein) with subsequent formation of the caveolae [42,43].