Academic literature on the topic 'Adipocytes Caveolae Caveolins'

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Journal articles on the topic "Adipocytes Caveolae Caveolins"

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Filippini, Antonio, and Alessio D’Alessio. "Caveolae and Lipid Rafts in Endothelium: Valuable Organelles for Multiple Functions." Biomolecules 10, no. 9 (2020): 1218. http://dx.doi.org/10.3390/biom10091218.

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Caveolae are flask-shaped invaginations of the plasma membrane found in numerous cell types and are particularly abundant in endothelial cells and adipocytes. The lipid composition of caveolae largely matches that of lipid rafts microdomains that are particularly enriched in cholesterol, sphingomyelin, glycosphingolipids, and saturated fatty acids. Unlike lipid rafts, whose existence remains quite elusive in living cells, caveolae can be clearly distinguished by electron microscope. Despite their similar composition and the sharing of some functions, lipid rafts appear more heterogeneous in te
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Volonte, Daniela, Charles F. McTiernan, Marek Drab, Michael Kasper, and Ferruccio Galbiati. "Caveolin-1 and caveolin-3 form heterooligomeric complexes in atrial cardiac myocytes that are required for doxorubicin-induced apoptosis." American Journal of Physiology-Heart and Circulatory Physiology 294, no. 1 (2008): H392—H401. http://dx.doi.org/10.1152/ajpheart.01039.2007.

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Caveolae are 50- to 100-nm invaginations of the plasma membrane. Caveolins are the structural protein components of caveolar membranes. The caveolin gene family is composed of three members: caveolin-1, caveolin-2, and caveolin-3. Caveolin-1 and caveolin-2 are coexpressed in many cell types, including adipocytes, endothelial cells, epithelial cells, and fibroblasts. In contrast, caveolin-3 expression is essentially restricted to skeletal and smooth muscle cells as well as cardiac myocytes. While the interaction between caveolin-1 and caveolin-2 has been documented previously, the reciprocal in
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Cohen, Alex W., Terry P. Combs, Philipp E. Scherer, and Michael P. Lisanti. "Role of caveolin and caveolae in insulin signaling and diabetes." American Journal of Physiology-Endocrinology and Metabolism 285, no. 6 (2003): E1151—E1160. http://dx.doi.org/10.1152/ajpendo.00324.2003.

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Caveolae are specialized membrane microdomains present within the plasma membrane of the vast majority of cell types. They have a unique composition in that they are highly enriched in cholesterol, sphingolipids, and their coat proteins the caveolins (-1, -2, and -3). In recent years it has been recognized that caveolae act as signaling platforms, serving as a concentrating point for numerous signaling molecules, as well as regulating flux through many distinct signaling cascades. Although caveolae are found in a variety of cell types, they are most abundant in adipose tissue. This fact has le
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Williams, Jamie J. L., and Timothy M. Palmer. "Cavin-1: caveolae-dependent signalling and cardiovascular disease." Biochemical Society Transactions 42, no. 2 (2014): 284–88. http://dx.doi.org/10.1042/bst20130270.

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Caveolae are curved lipid raft regions rich in cholesterol and sphingolipids found abundantly in vascular endothelial cells, adipocytes, smooth muscle cells and fibroblasts. They are multifunctional organelles with roles in clathrin-independent endocytosis, cholesterol transport, mechanosensing and signal transduction. Caveolae provide an environment where multiple receptor signalling components are sequestered, clustered and compartmentalized for efficient signal transduction. Many of these receptors, including cytokine signal transducer gp130 (glycoprotein 130), are mediators of chronic infl
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Bickel, Perry E. "Lipid rafts and insulin signaling." American Journal of Physiology-Endocrinology and Metabolism 282, no. 1 (2002): E1—E10. http://dx.doi.org/10.1152/ajpendo.2002.282.1.e1.

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Lipid rafts are domains within the plasma membrane that are enriched in cholesterol and lipids with saturated acyl chains. Specific proteins, including many signaling proteins, segregate into lipid rafts, and this process is important for certain signal transduction events in a variety of cell types. Within the past decade, data have emerged from many laboratories that implicate lipid rafts as critical for proper compartmentalization of insulin signaling in adipocytes. A subset of lipid rafts, caveolae, are coated with membrane proteins of the caveolin family. Direct interactions between resid
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ABOULAICH, Nabila, Julia P. VAINONEN, Peter STRÅLFORS, and Alexander V. VENER. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Biochemical Journal 383, no. 2 (2004): 237–48. http://dx.doi.org/10.1042/bj20040647.

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Caveolae, the specialized invaginations of plasma membranes, formed sealed vesicles with outwards-orientated cytosolic surface after isolation from primary human adipocytes. This morphology allowed differential, vectorial identification of proteins at the opposite membrane surfaces by proteolysis and MS. Extracellular-exposed caveolae-specific proteins CD36 and copper-containing amine oxidase were concealed inside the vesicles and resisted trypsin treatment. The cytosol-orientated caveolins were efficiently digested by trypsin, producing peptides amenable to direct MS sequencing. Isolation of
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Meshulam, Tova, Michael R. Breen, Libin Liu, Robert G. Parton, and Paul F. Pilch. "Caveolins/caveolae protect adipocytes from fatty acid-mediated lipotoxicity." Journal of Lipid Research 52, no. 8 (2011): 1526–32. http://dx.doi.org/10.1194/jlr.m015628.

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Thorn, Hans, Karin G. Stenkula, Margareta Karlsson, et al. "Cell Surface Orifices of Caveolae and Localization of Caveolin to the Necks of Caveolae in Adipocytes." Molecular Biology of the Cell 14, no. 10 (2003): 3967–76. http://dx.doi.org/10.1091/mbc.e03-01-0050.

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Caveolae are noncoated invaginations of the plasma membrane that form in the presence of the protein caveolin. Caveolae are found in most cells, but are especially abundant in adipocytes. By high-resolution electron microscopy of plasma membrane sheets the detailed structure of individual caveolae of primary rat adipocytes was examined. Caveolin-1 and -2 binding was restricted to the membrane proximal region, such as the ducts or necks attaching the caveolar bulb to the membrane. This was confirmed by transfection with myc-tagged caveolin-1 and -2. Essentially the same results were obtained wi
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Hulstrøm, V., C. Prats, and J. Vinten. "Adipocyte size and cellular expression of caveolar proteins analyzed by confocal microscopy." American Journal of Physiology-Cell Physiology 304, no. 12 (2013): C1168—C1175. http://dx.doi.org/10.1152/ajpcell.00273.2012.

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Caveolae are abundant in adipocytes and are involved in the regulation of lipid accumulation, which is the main volume determinant of these cells. We have developed and applied a confocal microscopic technique for measuring individual cellular expression of the caveolar proteins cavin-1 and caveolin-1 along with the size of individual adipocytes. The technique was applied on collagenase isolated adipocytes from ad libitum fed Sprague-Dawley rats of different age (4–26 wk) and weight (103–629 g). We found that cellular expression of caveolar proteins was variable (SD of log expression in the ra
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González-Muñoz, Elena, Carmen López-Iglesias, Maria Calvo, Manuel Palacín, Antonio Zorzano, and Marta Camps. "Caveolin-1 Loss of Function Accelerates Glucose Transporter 4 and Insulin Receptor Degradation in 3T3-L1 Adipocytes." Endocrinology 150, no. 8 (2009): 3493–502. http://dx.doi.org/10.1210/en.2008-1520.

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Caveolae are a specialized type of lipid rafts that are stabilized by oligomers of caveolin protein. Caveolae are particularly enriched in adipocytes. Here we analyzed the effects of caveolin-1 knockdown and caveolae ablation on adipocyte function. To this end, we obtained several multiclonal mouse 3T3-L1 cell lines with a reduced expression of caveolin-1 (95% reduction) by a small interfering RNA approach using lentiviral vectors. Control cell lines were obtained by lentiviral infection with lentiviral vectors encoding appropriate scrambled RNAs. Caveolin-1 knockdown adipocytes showed a drast
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Dissertations / Theses on the topic "Adipocytes Caveolae Caveolins"

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Thorn, Hans. "Caveolae structure and importance in insulin action /." Linköping : Univ, 2004. http://www.bibl.liu.se/liupubl/disp/disp2004/med875s.pdf.

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Aboulaich, Nabila. "Expanding role of caveolae in control of adipocyte metabolism : proteomics of caveolae." Doctoral thesis, Linköping : Univ, 2006. http://www.bibl.liu.se/liupubl/disp/disp2006/med968s.pdf.

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Yeow, Ivana E.-Ting. "The role of EHD proteins in caveolae, and the role of caveolae in adipocytes." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/275895.

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Caveolae are 50-60 nm flask-shaped invaginations of the plasma membrane that protect the plasma membrane from damage under stretch forces. They are highly abundant in cells that experience high levels of stress forces such as adipocytes, endothelial cells and muscle cells. Caveolae are generated by the oligomerisation and association of caveolin and cavin proteins, which form the caveolar coat complex at the caveolar bulb and are progressively well characterised. However, less is known about the proteins that localise to the caveolar neck. Using the CRIPSR/Cas9 system to generate gene knock-in
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Chikani, Gentle P. "LEPTIN RECEPTORS IN CAVEOLAE: REGULATION OF LIPOLYSIS IN 3T3-L1 ADIPOCYTES." UKnowledge, 2004. http://uknowledge.uky.edu/gradschool_theses/382.

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The present study has tested the hypothesis that leptin receptors are localized in caveolae and that caveolae are involved in the leptin-induced stimulation of lipolysis in 3T3-L1 adipocytes. Leptin, a peptide hormone, is secreted primarily by adipocytes and has been postulated to regulate food intake and energy expenditure via hypothalamic-mediated effects. Exposure to leptin increases the lipolytic activity in 3T3-L1 adipocytes. We isolated caveolae from 3T3-L1 adipocytes using a detergent free sucrose gradient centrifugation method. Leptin receptors were localized in the same gradient fract
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Simões, Francisco Manuel de Carvalho. "Cavin 1 and cavin 2 roles on adipocyte cell function." Master's thesis, Faculdade de Ciências e Tecnologia, 2011. http://hdl.handle.net/10362/6568.

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Dissertação para obtenção do Grau de Mestre em Genética Molecular e Biomedicina<br>Caveolae are a specialized type of lipid rafts found in numerous cell types. These structures have been implicated as playing a role in a variety of metabolic regulation processes and are typically characterized by their association with the caveolin and cavin protein families. Caveolae are particularly enriched in adipocytes and here we analyze the effects of cavin 1 and cavin 2 knockdown in adipocyte functioning. We obtained several multiclonal mouse 3T3-L1 cell lines with reduced expression of cavin 1 or cav
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Briand, Nolwenn. "Rôle de Caveoline-1 dans la contrôle de la capacité de stockage lipidique adipocytaire." Phd thesis, Université Pierre et Marie Curie - Paris VI, 2012. http://tel.archives-ouvertes.fr/tel-00827746.

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Les cavéolines et les protéines cavines forment le manteau d'invaginations membranaires appelées cavéoles. Dans le tissu adipeux (TA), ces structures sont très abondantes dans les adipocytes et les cellules endothéliales. Une perte d'expression de cavéoline-1 a pour conséquence une lipoatrophie sévère chez les souris invalidées pour ce gène (Cav1(-/-)), ce qui a conduit à suggérer un rôle important de Cav1 pour le contrôle de la capacité de stockage du TA. Par ailleurs, les souris Cav1(-/-) présentent des défauts vasculaires, phénotype totalement corrigé par une réexpression spécifique de Cav1
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Chiu, Kuan-Ting, and 邱冠霆. "High Mobility Group Box 1 Negatively Regulates Lipolysis in Adipocytes : Role of Caveolin-1." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/w72cax.

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碩士<br>國立陽明大學<br>生理學研究所<br>97<br>Obesity is characterized by excess fat accumulation in white adipose tissue, which increases the risk of various diseases. Adipocytes release various adipokines such as adiponectin to regulate lipid homeostasis. High mobility group box 1 (HMGB1) is not only a key protein for stabilization of chromosome and regulation of transcription in nucleus, but also released into the extracellular space via exocytosis to modulate inflammatory response. However, the exact role and underlying mechanisms of HMGB1 in adipogenesis are largely unknown. Caveolin-1 (Cav-1) is major
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