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Journal articles on the topic 'Adipocytes Caveolae Caveolins'

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Published: 4 June 2021

Last updated: 14 February 2022

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1

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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2

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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9

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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Jufvas, Åsa, Meenu R. Rajan, Cecilia Jönsson, Peter Strålfors, and Maria V. Turkina. "Scaffolding protein IQGAP1: an insulin-dependent link between caveolae and the cytoskeleton in primary human adipocytes?" Biochemical Journal 473, no. 19 (2016): 3177–88. http://dx.doi.org/10.1042/bcj20160581.

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The ubiquitously expressed IQ motif-containing GTPase activating protein-1 (IQGAP1) is a scaffolding protein implicated in an array of cellular functions, in particular by binding to cytoskeletal elements and signaling proteins. A role of IQGAP1 in adipocytes has not been reported. We therefore investigated the cellular IQGAP1 interactome in primary human adipocytes. Immunoprecipitation and quantitative mass spectrometry identified caveolae and caveolae-associated proteins as the major IQGAP1 interactors alongside cytoskeletal proteins. We confirmed co-localization of IQGAP1 with the defining

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Müller, Günter, Christian Jung, Susanne Wied, Stefan Welte, Holger Jordan, and Wendelin Frick. "Redistribution of Glycolipid Raft Domain Components Induces Insulin-Mimetic Signaling in Rat Adipocytes." Molecular and Cellular Biology 21, no. 14 (2001): 4553–67. http://dx.doi.org/10.1128/mcb.21.14.4553-4567.2001.

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ABSTRACT Caveolae and caveolin-containing detergent-insoluble glycolipid-enriched rafts (DIG) have been implicated to function as plasma membrane microcompartments or domains for the preassembly of signaling complexes, keeping them in the basal inactive state. So far, only limited in vivo evidence is available for the regulation of the interaction between caveolae-DIG and signaling components in response to extracellular stimuli. Here, we demonstrate that in isolated rat adipocytes, synthetic intracellular caveolin binding domain (CBD) peptide derived from caveolin-associated pp59Lyn (10 to 10

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Hajduch, Eric, Sophie Turban, Xavier Le Liepvre та ін. "Targeting of PKCζ and PKB to caveolin-enriched microdomains represents a crucial step underpinning the disruption in PKB-directed signalling by ceramide". Biochemical Journal 410, № 2 (2008): 369–79. http://dx.doi.org/10.1042/bj20070936.

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Elevated ceramide concentrations in adipocytes and skeletal muscle impair PKB (protein kinase B; also known as Akt)-directed insulin signalling to key hormonal end points. An important feature of this inhibition involves the ceramide-induced activation of atypical PKCζ (protein kinase C-ζ), which associates with and negatively regulates PKB. In the present study, we demonstrate that this inhibition is critically dependent on the targeting and subsequent retention of PKCζ–PKB within CEM (caveolin-enriched microdomains), which is facilitated by kinase interactions with caveolin. Ceramide also re

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Scherer, P. E., M. P. Lisanti, G. Baldini, M. Sargiacomo, C. C. Mastick, and H. F. Lodish. "Induction of caveolin during adipogenesis and association of GLUT4 with caveolin-rich vesicles." Journal of Cell Biology 127, no. 5 (1994): 1233–43. http://dx.doi.org/10.1083/jcb.127.5.1233.

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Caveolae, also termed plasmalemmal vesicles, are small, flask-shaped, non-clathrin-coated invaginations of the plasma membrane. Caveolin is a principal component of the filaments that make up the striated coat of caveolae. Using caveolin as a marker protein for the organelle, we found that adipose tissue is the single most abundant source of caveolae identified thus far. Caveolin mRNA and protein are strongly induced during differentiation of 3T3-L1 fibroblasts to adipocytes; during adipogenesis there is also a dramatic increase in the complexity of the protein composition of caveolin-rich mem

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15

Kandror, K. V., J. M. Stephens, and P. F. Pilch. "Expression and compartmentalization of caveolin in adipose cells: coordinate regulation with and structural segregation from GLUT4." Journal of Cell Biology 129, no. 4 (1995): 999–1006. http://dx.doi.org/10.1083/jcb.129.4.999.

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Native rat adipocytes and the mouse adipocyte cell line, 3T3-L1, possess transport vesicles of apparently uniform composition and size which translocate the tissue-specific glucose transporter isoform, GLUT4, from an intracellular pool to the cell surface in an insulin-sensitive fashion. Caveolin, the presumed structural protein of caveolae, has also been proposed to function in vesicular transport. Thus, we studied the expression and subcellular distribution of caveolin in adipocytes. We found that rat fat cells express the highest level of caveolin protein of any tissue studied, and caveolin

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Razani, Babak, Xiao Bo Wang, Jeffery A. Engelman, et al. "Caveolin-2-Deficient Mice Show Evidence of Severe Pulmonary Dysfunction without Disruption of Caveolae." Molecular and Cellular Biology 22, no. 7 (2002): 2329–44. http://dx.doi.org/10.1128/mcb.22.7.2329-2344.2002.

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ABSTRACT Caveolin-2 is a member of the caveolin gene family with no known function. Although caveolin-2 is coexpressed and heterooligomerizes with caveolin-1 in many cell types (most notably adipocytes and endothelial cells), caveolin-2 has traditionally been considered the dispensable structural partner of the widely studied caveolin-1. We now directly address the functional significance of caveolin-2 by genetically targeting the caveolin-2 locus (Cav-2) in mice. In the absence of caveolin-2 protein expression, caveolae still form and caveolin-1 maintains its localization in plasma membrane c

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Mastick, C. C., M. J. Brady, and A. R. Saltiel. "Insulin stimulates the tyrosine phosphorylation of caveolin." Journal of Cell Biology 129, no. 6 (1995): 1523–31. http://dx.doi.org/10.1083/jcb.129.6.1523.

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The specialized plasma membrane structures termed caveolae and the caveolar-coat protein caveolin are highly expressed in insulin-sensitive cells such as adipocytes and muscle. Stimulation of 3T3-L1 adipocytes with insulin significantly increased the tyrosine phosphorylation of caveolin and a 29-kD caveolin-associated protein in caveolin-enriched Triton-insoluble complexes. Maximal phosphorylation occurred within 5 min, and the levels of phosphorylation remained elevated for at least 30 min. The insulin-dose responses for the tyrosine phosphorylation of caveolin and the 29-kD caveolin-associat

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Pradhan, Bhola Shankar, and Tomasz J. Prószyński. "A Role for Caveolin-3 in the Pathogenesis of Muscular Dystrophies." International Journal of Molecular Sciences 21, no. 22 (2020): 8736. http://dx.doi.org/10.3390/ijms21228736.

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Caveolae are the cholesterol-rich small invaginations of the plasma membrane present in many cell types including adipocytes, endothelial cells, epithelial cells, fibroblasts, smooth muscles, skeletal muscles and cardiac muscles. They serve as specialized platforms for many signaling molecules and regulate important cellular processes like energy metabolism, lipid metabolism, mitochondria homeostasis, and mechano-transduction. Caveolae can be internalized together with associated cargo. The caveolae-dependent endocytic pathway plays a role in the withdrawal of many plasma membrane components t

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Brännmark, Cecilia, Emma I. Kay, Unn Örtegren Kugelberg, et al. "Adiponectin is secreted via caveolin 1-dependent mechanisms in white adipocytes." Journal of Endocrinology 247, no. 1 (2020): 25–38. http://dx.doi.org/10.1530/joe-20-0078.

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Here we have investigated the role of the protein caveolin 1 (Cav1) and caveolae in the secretion of the white adipocyte hormone adiponectin. Using mouse primary subcutaneous adipocytes genetically depleted of Cav1, we show that the adiponectin secretion, stimulated either adrenergically or by insulin, is abrogated while basal (unstimulated) release of adiponectin is elevated. Adiponectin secretion is similarly affected in wildtype mouse and human adipocytes where the caveolae structure was chemically disrupted. The altered ex vivo secretion in adipocytes isolated from Cav1 null mice is accomp

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Capozza, Franco, Alex W. Cohen, Michelle W. C. Cheung, et al. "Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells." American Journal of Physiology-Cell Physiology 288, no. 3 (2005): C677—C691. http://dx.doi.org/10.1152/ajpcell.00232.2004.

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It is generally well accepted that caveolin-3 expression is muscle specific, whereas caveolin-1 and -2 are coexpressed in a variety of cell types, including adipocytes, endothelial cells, epithelial cells, and fibroblasts. Caveolin-1 and -2 are known to form functional hetero-oligomeric complexes in cells where they are coexpressed, whereas caveolin-3 forms homo-oligomeric high molecular mass complexes. Although caveolin-2 might be expected to interact in a similar manner with caveolin-3, most studies indicate that this is not the case. However, this view has recently been challenged as it has

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Palacios-Ortega, Sara, Maider Varela-Guruceaga, Miriam Algarabel, Fermín Ignacio Milagro, J. Alfredo Martínez, and Carlos de Miguel. "Effect of TNF-Alpha on Caveolin-1 Expression and Insulin Signaling During Adipocyte Differentiation and in Mature Adipocytes." Cellular Physiology and Biochemistry 36, no. 4 (2015): 1499–516. http://dx.doi.org/10.1159/000430314.

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Background/Aims: Tumor necrosis factor-α (TNF-α)-mediated chronic low-grade inflammation of adipose tissue is associated with obesity and insulin resistance. Caveolin-1 (Cav-1) is the central component of adipocyte caveolae and has an essential role in the regulation of insulin signaling. The effects of TNF-α on Cav-1 expression and insulin signaling during adipocyte differentiation and in mature adipocytes were studied. Methods: 3T3-L1 cells were differentiated (21 days) in the presence TNF-α (10 ng/mL) and mature adipocytes were also treated with TNF-α for 48 hours. Cav-1 and insulin recepto

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Sato, M., D. S. Hutchinson, B. A. Evans та R. J. Summers. "Functional domains of the mouse β3-adrenoceptor associated with differential G-protein coupling". Biochemical Society Transactions 35, № 5 (2007): 1035–37. http://dx.doi.org/10.1042/bst0371035.

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Localization of G-protein-coupled receptors within membrane microdomains is associated with differential signalling pathway activation. We have shown that two mouse β3-AR (β3-adrenoceptor) isoforms encoded by alternatively spliced mRNAs differ in their signalling properties; the β3a-AR couples only with Gs, whereas the β3b-AR couples with both Gs and Gi. Our previous studies indicated that the β3a-AR is restrained from coupling with Gi due to the interaction of residues in the C-terminus with other protein(s). We have investigated the hypothesis that the β3a-AR interacts with caveolin. Disrupt

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Robinson, J. M. "What Can Epitope Specific Antibodies Tell us About the Organization of Caveolin in Cells?" Microscopy and Microanalysis 7, S2 (2001): 1030–31. http://dx.doi.org/10.1017/s1431927600031226.

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There are three members of the caveolin (CAV) gene family that give rise to four polypeptides. These polypeptides are CAV-1α, CAV-1β, CAV-2, and CAV-3. The CAV-1β isoform is a truncated form of CAV-1α that lacks 31 amino acids at the N-terminus of the molecule. The CAV- 1β molecule arises through an alternative splicing mechanism.Caveolae are specialized plasma membrane microdomains that are expressed at high levels in some cell types (e.g., endothelium, adipocytes, fibroblasts). These specialized regions of the plasma membrane have a characteristic omega-shaped appearance with diameters rangi

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Huang, Zhi Hua, DeSheng Gu, and Theodore Mazzone. "Role of adipocyte-derived apoE in modulating adipocyte size, lipid metabolism, and gene expression in vivo." American Journal of Physiology-Endocrinology and Metabolism 296, no. 5 (2009): E1110—E1119. http://dx.doi.org/10.1152/ajpendo.90964.2008.

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Adipocytes isolated from apolipoprotein E (apoE)-knockout (EKO) mice display alterations in triglyceride (TG) metabolism and gene expression. The present studies were undertaken to evaluate the impact of endogenously produced adipocyte apoE on these adipocyte parameters in vivo, independent of the profoundly disturbed metabolic milieu of EKO mice. Adipose tissue from wild-type (WT) or EKO mice was transplanted into WT recipients, which were then fed chow or high-fat diet for 8–10 wk. After a chow diet, freshly isolated transplanted EKO adipocytes were significantly ( P < 0.05) smaller (70%)

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Vainonen, Julia P., Nabila Aboulaich, Maria V. Turkina, Peter Strålfors, and Alexander V. Vener. "N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes." Biochemical and Biophysical Research Communications 320, no. 2 (2004): 480–86. http://dx.doi.org/10.1016/j.bbrc.2004.05.196.

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Kampf, J. Patrick, Danielle Parmley, and Alan M. Kleinfeld. "Free fatty acid transport across adipocytes is mediated by an unknown membrane protein pump." American Journal of Physiology-Endocrinology and Metabolism 293, no. 5 (2007): E1207—E1214. http://dx.doi.org/10.1152/ajpendo.00259.2007.

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The role of cell membranes in regulating the flux of long chain free fatty acids (FFA) into and out of adipocytes is intensely debated. Four different membrane proteins including, FABPpm, CD36/FAT, caveolin-1, and FATP have been identified as facilitating FFA transport. Moreover, CD36 and caveolin-1 are also reported to mediate transport in conjunction with lipid rafts. The principal evidence for these findings is a correlation of the level of FFA uptake with the expression level of these proteins and with the integrity of lipid rafts. The 3T3-L1 and 3T3-F442A cell lines in their preadipocyte

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Briand, N., C. Prado, G. Mabilleau, et al. "Caveolin-1 Expression and Cavin Stability Regulate Caveolae Dynamics in Adipocyte Lipid Store Fluctuation." Diabetes 63, no. 12 (2014): 4032–44. http://dx.doi.org/10.2337/db13-1961.

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Le Lay, Soazig, Eric Hajduch, Margaret R. Lindsay, et al. "Cholesterol-Induced Caveolin Targeting to Lipid Droplets in Adipocytes: A Role for Caveolar Endocytosis." Traffic 7, no. 5 (2006): 549–61. http://dx.doi.org/10.1111/j.1600-0854.2006.00406.x.

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Murata, Takahisa, Michelle I. Lin, Yan Huang, et al. "Reexpression of caveolin-1 in endothelium rescues the vascular, cardiac, and pulmonary defects in global caveolin-1 knockout mice." Journal of Experimental Medicine 204, no. 10 (2007): 2373–82. http://dx.doi.org/10.1084/jem.20062340.

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Caveolin-1 (Cav-1) is the principal structural component of caveolae organelles in smooth muscle cells, adipocytes, fibroblasts, epithelial cells, and endothelial cells (ECs). Cav-1–deficient (Cav-1 knockout [KO]) mice are viable and show increases of nitric oxide (NO) production in vasculature, cardiomyopathy, and pulmonary dysfunction. In this study, we generated EC-specific Cav-1–reconstituted (Cav-1 RC) mice and reexamined vascular, cardiac, and pulmonary phenotypes. Cav-1 KO pulmonary arteries had decreased smooth muscle contractility and increased endothelial NO synthase activation and h

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Cohen, Alex W., Babak Razani, Xiao Bo Wang, et al. "Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue." American Journal of Physiology-Cell Physiology 285, no. 1 (2003): C222—C235. http://dx.doi.org/10.1152/ajpcell.00006.2003.

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Several lines of evidence suggest that a functional relationship exists between caveolin-1 and insulin signaling. However, it remains unknown whether caveolin-1 is normally required for proper insulin receptor signaling in vivo. To address this issue, we examined the status of insulin receptor signaling in caveolin-1 (–/–)-deficient (Cav-1 null) mice. Here, we show that Cav-1 null mice placed on a high-fat diet for 9 mo develop postprandial hyperinsulinemia. An insulin tolerance test (ITT) revealed that young Cav-1 null mice on a normal chow diet are significantly unresponsive to insulin, comp

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Ahmad, Faiyaz, Rebecka Lindh, Yan Tang та ін. "Differential regulation of adipocyte PDE3B in distinct membrane compartments by insulin and the β3-adrenergic receptor agonist CL316243: effects of caveolin-1 knockdown on formation/maintenance of macromolecular signalling complexes". Biochemical Journal 424, № 3 (2009): 399–410. http://dx.doi.org/10.1042/bj20090842.

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In adipocytes, PDE3B (phosphodiesterase 3B) is an important regulatory effector in signalling pathways controlled by insulin and cAMP-increasing hormones. Stimulation of 3T3-L1 adipocytes with insulin or the β3-adrenergic receptor agonist CL316243 (termed CL) indicated that insulin preferentially phosphorylated/activated PDE3B associated with internal membranes (endoplasmic reticulum/Golgi), whereas CL preferentially phosphorylated/activated PDE3B associated with caveolae. siRNA (small interfering RNA)-mediated KD (knockdown) of CAV-1 (caveolin-1) in 3T3-L1 adipocytes resulted in down-regulati

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Nagajyothi, Fnu, Mahalia S. Desruisseaux, Linda A. Jelicks, et al. "Perspectives on Adipose Tissue, Chagas Disease and Implications for the Metabolic Syndrome." Interdisciplinary Perspectives on Infectious Diseases 2009 (2009): 1–6. http://dx.doi.org/10.1155/2009/824324.

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The contribution of adipose tissue an autocrine and endocrine organ in the pathogenesis of infectious disease and metabolic syndrome is gaining attention. Adipose tissue and adipocytes are one of the major targets ofT. cruziinfection. Parasites are detected 300 days postinfection in adipose tissue. Infection of adipose tissue and cultured adipocytes triggered local expression of inflammatory mediators resulting in the upregulation of cytokine and chemokine levels. Adipose tissue obtained from infected mice display an increased infiltration of inflammatory cells. Adiponectin, an adipocyte speci

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Bridges, Dave, Louise Chang, Irfan J. Lodhi, Natalie A. Clark, and Alan R. Saltiel. "TC10 Is Regulated by Caveolin in 3T3-L1 Adipocytes." PLoS ONE 7, no. 8 (2012): e42451. http://dx.doi.org/10.1371/journal.pone.0042451.

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Le Lay, Soazig, Cédric M. Blouin, Eric Hajduch, and Isabelle Dugail. "Filling up adipocytes with lipids. Lessons from caveolin-1 deficiency." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1791, no. 6 (2009): 514–18. http://dx.doi.org/10.1016/j.bbalip.2008.10.008.

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Chamberlain, Luke H., and Gwyn W. Gould. "The Vesicle- and Target-SNARE Proteins That Mediate Glut4 Vesicle Fusion Are Localized in Detergent-insoluble Lipid Rafts Present on Distinct Intracellular Membranes." Journal of Biological Chemistry 277, no. 51 (2002): 49750–54. http://dx.doi.org/10.1074/jbc.m206936200.

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Insulin stimulates the fusion of intracellular vesicles containing the glucose transporter Glut4 with the plasma membrane in adipocytes and muscle cells. Glut4 vesicle fusion is thought to be catalyzed by the interaction of the vesicle solubleN-ethyl-maleimide-sensitive fusion protein attachment protein receptor VAMP2 with the target solubleN-ethyl-maleimide-sensitive fusion protein attachment protein receptors SNAP-23 and syntaxin 4. Here, we use combined membrane fractionation, detergent solubility, and sucrose gradient flotation to demonstrate that the large majority (>70%) of SNAP-23 an

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Yue, Lili, and Theodore Mazzone. "Endogenous adipocyte apolipoprotein E is colocalized with caveolin at the adipocyte plasma membrane." Journal of Lipid Research 52, no. 3 (2010): 489–98. http://dx.doi.org/10.1194/jlr.m011809.

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Le Lay, Soazig, Nolwenn Briand, Cédric M. Blouin, et al. "The lipoatrophic caveolin-1 deficient mouse model reveals autophagy in mature adipocytes." Autophagy 6, no. 6 (2010): 754–63. http://dx.doi.org/10.4161/auto.6.6.12574.

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Storey, Stephen M., Avery L. McIntosh, Subramanian Senthivinayagam, Kenneth C. Moon, and Barbara P. Atshaves. "The phospholipid monolayer associated with perilipin-enriched lipid droplets is a highly organized rigid membrane structure." American Journal of Physiology-Endocrinology and Metabolism 301, no. 5 (2011): E991—E1003. http://dx.doi.org/10.1152/ajpendo.00109.2011.

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The significance of lipid droplets (LD) in lipid metabolism, cell signaling, and membrane trafficking is increasingly recognized, yet the role of the LD phospholipid monolayer in LD protein targeting and function remains unknown. To begin to address this issue, two populations of LD were isolated by ConA sepharose affinity chromatography: 1) functionally active LD enriched in perilipin, caveolin-1, and several lipolytic proteins, including ATGL and HSL; and 2) LD enriched in ADRP and TIP47 that contained little to no lipase activity. Coimmunoprecipitation experiments confirmed the close associ

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Watson, Robert T., Satoshi Shigematsu, Shian-Huey Chiang, et al. "Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation." Journal of Cell Biology 154, no. 4 (2001): 829–40. http://dx.doi.org/10.1083/jcb.200102078.

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Recent studies indicate that insulin stimulation of glucose transporter (GLUT)4 translocation requires at least two distinct insulin receptor–mediated signals: one leading to the activation of phosphatidylinositol 3 (PI-3) kinase and the other to the activation of the small GTP binding protein TC10. We now demonstrate that TC10 is processed through the secretory membrane trafficking system and localizes to caveolin-enriched lipid raft microdomains. Although insulin activated the wild-type TC10 protein and a TC10/H-Ras chimera that were targeted to lipid raft microdomains, it was unable to acti

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Chang, Chia-Chu, Chen-Yu Chen, Hui-Chin Wen, et al. "Caveolin-1 Secreted from Adipose Tissues and Adipocytes Functions as an Adipogenesis Enhancer." Obesity 25, no. 11 (2017): 1932–40. http://dx.doi.org/10.1002/oby.21970.

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Palacios-Ortega, Sara, Maider Varela-Guruceaga, J. Alfredo Martínez, Carlos de Miguel, and Fermín I. Milagro. "Effects of high glucose on caveolin-1 and insulin signaling in 3T3-L1 adipocytes." Adipocyte 5, no. 1 (2015): 65–80. http://dx.doi.org/10.1080/21623945.2015.1122856.

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Kanzaki, Makoto, and Jeffrey E. Pessin. "Caveolin-associated Filamentous Actin (Cav-actin) Defines a Novel F-actin Structure in Adipocytes." Journal of Biological Chemistry 277, no. 29 (2002): 25867–69. http://dx.doi.org/10.1074/jbc.c200292200.

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Bayer-Garner, Ilene, Michael Morgan, and Bruce R. Smoller. "Caveolin Expression is Common among Benign and Malignant Smooth Muscle and Adipocyte Neoplasms." Modern Pathology 15, no. 1 (2002): 1–5. http://dx.doi.org/10.1038/modpathol.3880481.

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Hill, Michelle M., Sharon F. Clark, and David E. James. "Insulin-regulatable phosphoproteins in 3T3-L1 adipocytes form detergent-insoluble complexes not associated with caveolin." Electrophoresis 18, no. 14 (1997): 2629–37. http://dx.doi.org/10.1002/elps.1150181419.

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Gómez-Ruiz, Ana, Fermín I. Milagro, Javier Campión, J. Alfredo Martínez, and Carlos de Miguel. "Caveolin expression and activation in retroperitoneal and subcutaneous adipocytes: Influence of a high-fat diet." Journal of Cellular Physiology 225, no. 1 (2010): 206–13. http://dx.doi.org/10.1002/jcp.22241.

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Blouin, Cédric M., Soazig Le Lay, Anita Eberl, et al. "Lipid droplet analysis in caveolin-deficient adipocytes: alterations in surface phospholipid composition and maturation defects." Journal of Lipid Research 51, no. 5 (2009): 945–56. http://dx.doi.org/10.1194/jlr.m001016.

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Covey, Scott D., Rachelle H. Brunet, Shephali G. Gandhi, et al. "Cholesterol depletion inhibits fatty acid uptake without affecting CD36 or caveolin-1 distribution in adipocytes." Biochemical and Biophysical Research Communications 355, no. 1 (2007): 67–71. http://dx.doi.org/10.1016/j.bbrc.2007.01.135.

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Bourez, Sophie, Soazig Le Lay, Carine Van den Daelen, et al. "Accumulation of Polychlorinated Biphenyls in Adipocytes: Selective Targeting to Lipid Droplets and Role of Caveolin-1." PLoS ONE 7, no. 2 (2012): e31834. http://dx.doi.org/10.1371/journal.pone.0031834.

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Watson, Robert T., Megumi Furukawa, Shian-Huey Chiang, et al. "The Exocytotic Trafficking of TC10 Occurs through both Classical and Nonclassical Secretory Transport Pathways in 3T3L1 Adipocytes." Molecular and Cellular Biology 23, no. 3 (2003): 961–74. http://dx.doi.org/10.1128/mcb.23.3.961-974.2003.

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ABSTRACT To examine the structural determinants necessary for TC10 trafficking, localization, and function in adipocytes, we generated a series of point mutations in the carboxyl-terminal targeting domain of TC10. Wild-type TC10 (TC10/WT) localized to secretory membrane compartments and caveolin-positive lipid raft microdomains at the plasma membrane. Expression of a TC10/C206S point mutant resulted in a trafficking and localization pattern that was indistinguishable from that of TC10/WT. In contrast, although TC10/C209S or the double TC10/C206,209S mutant was plasma membrane localized, it was

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Le Lay, S., N. Briand, C. Blouin, et al. "PO31 - Le modèle de souris lipoatrophique déficiente en caveoline-1 révèle une activité autophagique dans les adipocytes." Diabetes & Metabolism 37, no. 1 (2011): A31. http://dx.doi.org/10.1016/s1262-3636(11)70609-7.

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