PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17803693-1 2008 OBJECTIVE: Caveolin-1 (CAV-1) plays important roles in many aspects of cellular biology, including vesicular transport, cholesterol homeostasis and signal transduction. Cholesterol 120-131 caveolin 1 Homo sapiens 11-21 18045854-4 2008 In this study, we demonstrate a role for caveolin in the trafficking of Kv1.5 to lipid raft microdomains where cholesterol modulates channel function. Cholesterol 111-122 caveolin 1 Homo sapiens 41-49 18045854-9 2008 Together, these results show that caveolin modulates channel function by regulating trafficking to cholesterol-rich membrane microdomains. Cholesterol 99-110 caveolin 1 Homo sapiens 34-42 17803693-1 2008 OBJECTIVE: Caveolin-1 (CAV-1) plays important roles in many aspects of cellular biology, including vesicular transport, cholesterol homeostasis and signal transduction. Cholesterol 120-131 caveolin 1 Homo sapiens 23-28 18296864-1 2008 Caveolin-1 is a principal component of caveolae, invaginations of the plasma membrane that are enriched in cholesterol and sphingolipids. Cholesterol 107-118 caveolin 1 Homo sapiens 0-10 17936759-5 2007 Caveolin-1, specifically localized in cholesterol-enriched lipid rafts, appears to regulate constitutive and agonist-stimulated cell surface levels of 5-HT7 receptors via a clathrin-independent mechanism. Cholesterol 38-49 caveolin 1 Homo sapiens 0-10 17690101-1 2007 Autocrine motility factor (AMF) is internalized via a receptor-mediated, dynamin-dependent, cholesterol-sensitive raft pathway to the smooth endoplasmic reticulum that is negatively regulated by caveolin-1. Cholesterol 92-103 caveolin 1 Homo sapiens 195-205 17545472-8 2007 Depletion of plasma membrane cholesterol with methyl-beta-cyclodextrin (MbetaCD) disrupted lipid rafts and abolished co-localization of ATP synthase with caveolin-1, which resulted in a marked reduction in shear stress-induced ATP release. Cholesterol 29-40 caveolin 1 Homo sapiens 154-164 17626904-4 2007 Furthermore, depletion of cholesterol by methyl-beta-cyclodextrin (MCD) or siRNA knockdown of caveolin-1 efficiently blocked CD40 internalization, suggesting that caveolae-rafts pathway regulates CD40 internalization. Cholesterol 26-37 caveolin 1 Homo sapiens 94-104 17392516-8 2007 We propose that cholesterol depletion stimulates the coupling of transcytotic and caveolin-1 signaling pathways, consequently prompting the membranes to shuttle from endosomes to the plasma membrane. Cholesterol 16-27 caveolin 1 Homo sapiens 82-92 17580960-2 2007 Therefore, the interaction between caveolin-1 and sterol carrier protein-2 (SCP-2), a protein that binds and transfers both cholesterol and signaling lipids (e.g., phosphatidylinositides and sphingolipids), was examined by yeast two-hybrid, in vitro binding and fluorescence resonance energy transfer (FRET) analyses. Cholesterol 124-135 caveolin 1 Homo sapiens 35-45 17591975-8 2007 Therefore, human immunodeficiency virus protease inhibitor ritonavir significantly inhibits cholesterol efflux from macrophages, which may be mediated by mitochondrial dysfunction, oxidative stress, ERK1/2 activation, and down-regulation of scavenger receptor B1 and caveolin-1. Cholesterol 92-103 caveolin 1 Homo sapiens 267-277 17498653-5 2007 Cholesterol depletion attenuated integrin-dependent caveolin-1 phosphorylation, Src activation and Csk association with beta1 integrin. Cholesterol 0-11 caveolin 1 Homo sapiens 52-62 17584047-7 2007 Caveolae and its structural protein caveolin-1 are abundant in ECs and could be contributors to cholesterol trafficking as well. Cholesterol 96-107 caveolin 1 Homo sapiens 36-46 16825579-8 2006 Depletion of VSM cholesterol by beta-cyclodextrin resulted in a loss of membrane caveolin-1, a marker of cholesterol-enriched lipid raft, and inhibited the SPC-induced Ca(2+) sensitization and translocation of Rho-kinase from cytosol to the cell membrane. Cholesterol 17-28 caveolin 1 Homo sapiens 81-91 17391247-4 2007 The aim of this study was to determine the role of caveolin and caveolin-associated cholesterol rich microdomains in mechanically stimulated 5-HT release from BON cells. Cholesterol 84-95 caveolin 1 Homo sapiens 64-72 17121865-8 2007 Restoration of caveolae by coincubation of cyclodextrin with cholesterol rescued both RhoA activation and RhoA/cav-1 association in response to strain. Cholesterol 61-72 caveolin 1 Homo sapiens 111-116 17022989-4 2006 Confocal and fluorescence microscopy investigation shows that the caveolin-1 peptides bind to the more fluid cholesterol-poor phase. Cholesterol 109-120 caveolin 1 Homo sapiens 66-76 16996794-1 2006 Caveolae and its structural protein caveolin-1 (Cav-1) are abundant in vascular endothelial cells (ECs) and have been suggested to contribute to cell signaling and cholesterol trafficking. Cholesterol 164-175 caveolin 1 Homo sapiens 36-46 16996794-1 2006 Caveolae and its structural protein caveolin-1 (Cav-1) are abundant in vascular endothelial cells (ECs) and have been suggested to contribute to cell signaling and cholesterol trafficking. Cholesterol 164-175 caveolin 1 Homo sapiens 48-53 16996794-5 2006 Further, cholesterol exposure increased the level of ATPS-beta, along with Cav-1 and cholesterol in caveolae. Cholesterol 9-20 caveolin 1 Homo sapiens 75-80 16825579-8 2006 Depletion of VSM cholesterol by beta-cyclodextrin resulted in a loss of membrane caveolin-1, a marker of cholesterol-enriched lipid raft, and inhibited the SPC-induced Ca(2+) sensitization and translocation of Rho-kinase from cytosol to the cell membrane. Cholesterol 105-116 caveolin 1 Homo sapiens 81-91 15863835-5 2005 Although ceramide rapidly depleted lipid raft cholesterol, the levels of the cholesterol binding protein caveolin-1 (Cav-1) decreased by 25% only after 8 h. Importantly, replenishing the cells with cholesterol rapidly reversed the loss of Cav-1 from the CEMs. Cholesterol 77-88 caveolin 1 Homo sapiens 105-115 16734766-8 2006 Potentiation of the response by cholesterol depletion was maintained in caveolin-1 deficient Caco-2 colonocytes as well as in sphingomyelinase-treated Intestine 407 cells, indicating that cholesterol-rich microdomains are not crucially involved. Cholesterol 32-43 caveolin 1 Homo sapiens 72-82 16734766-8 2006 Potentiation of the response by cholesterol depletion was maintained in caveolin-1 deficient Caco-2 colonocytes as well as in sphingomyelinase-treated Intestine 407 cells, indicating that cholesterol-rich microdomains are not crucially involved. Cholesterol 188-199 caveolin 1 Homo sapiens 72-82 16123345-2 2005 In the present study, we examined potential contributory roles of membrane-associated, cholesterol-enriched lipid rafts/caveolae and their constituent proteins (e.g., caveolin-1 [Cav-1]) as potential sites for IL-1beta-induced nitric oxide (NO) release in the isolated beta-cell. Cholesterol 87-98 caveolin 1 Homo sapiens 167-177 16123345-2 2005 In the present study, we examined potential contributory roles of membrane-associated, cholesterol-enriched lipid rafts/caveolae and their constituent proteins (e.g., caveolin-1 [Cav-1]) as potential sites for IL-1beta-induced nitric oxide (NO) release in the isolated beta-cell. Cholesterol 87-98 caveolin 1 Homo sapiens 179-185 15863835-0 2005 Ceramide displaces cholesterol from lipid rafts and decreases the association of the cholesterol binding protein caveolin-1. Cholesterol 85-96 caveolin 1 Homo sapiens 113-123 15907796-1 2005 The goal of this study was to investigate the cellular localization and the interaction between caveolin-1 and ABCA1 in cholesterol-loaded aortic endothelial cells after HDL incubation. Cholesterol 120-131 caveolin 1 Homo sapiens 96-106 15907796-7 2005 The studies provide evidence for a direct interaction between ABCA1 and HDL, ABCA1 and caveolin-1, but not HDL and caveolin-1, indicating that ABCA1 may act as a structural platform between HDL and caveolin-1 on the cell surface during cellular cholesterol efflux. Cholesterol 245-256 caveolin 1 Homo sapiens 87-97 15863835-5 2005 Although ceramide rapidly depleted lipid raft cholesterol, the levels of the cholesterol binding protein caveolin-1 (Cav-1) decreased by 25% only after 8 h. Importantly, replenishing the cells with cholesterol rapidly reversed the loss of Cav-1 from the CEMs. Cholesterol 77-88 caveolin 1 Homo sapiens 117-122 15863835-5 2005 Although ceramide rapidly depleted lipid raft cholesterol, the levels of the cholesterol binding protein caveolin-1 (Cav-1) decreased by 25% only after 8 h. Importantly, replenishing the cells with cholesterol rapidly reversed the loss of Cav-1 from the CEMs. Cholesterol 77-88 caveolin 1 Homo sapiens 105-115 15863835-5 2005 Although ceramide rapidly depleted lipid raft cholesterol, the levels of the cholesterol binding protein caveolin-1 (Cav-1) decreased by 25% only after 8 h. Importantly, replenishing the cells with cholesterol rapidly reversed the loss of Cav-1 from the CEMs. Cholesterol 77-88 caveolin 1 Homo sapiens 117-122 15531587-0 2005 KLF11-mediated repression antagonizes Sp1/sterol-responsive element-binding protein-induced transcriptional activation of caveolin-1 in response to cholesterol signaling. Cholesterol 148-159 caveolin 1 Homo sapiens 122-132 15531587-4 2005 Through a combination of RNA interference, chromatin immunoprecipitation assays, electrophoretic mobility shift assays, and reporter assays, we demonstrate that in the presence of cholesterol, KLF11 acts as a dominant repressor of the caveolin-1 gene. Cholesterol 180-191 caveolin 1 Homo sapiens 235-245 15240128-2 2004 In this report, we demonstrate for the first time that after overexpressing caveolin-1, the plasma membrane cholesterol level was decreased by about 12% and 30% for doxorubicin-sensitive and doxorubicin-resistant Hs578T breast cancer cells, respectively. Cholesterol 108-119 caveolin 1 Homo sapiens 76-86 15576483-4 2004 Caveolin-1 drives the formation of plasma membrane caveolae and anchors them to the actin cytoskeleton, modulates cell interaction with the extracellular matrix, pulls together and regulates signaling molecules, and transports cholesterol. Cholesterol 227-238 caveolin 1 Homo sapiens 0-10 15388640-2 2004 In this study, we show that oxidized PAPC (OxPAPC), which accumulates in atherosclerotic lesions, paradoxically depletes endothelial cholesterol, causing caveolin-1 internalization from the plasma membrane to the endoplasmic reticulum and Golgi, and activates sterol regulatory element-binding protein (SREBP). Cholesterol 133-144 caveolin 1 Homo sapiens 154-164 15388640-7 2004 Furthermore, cholesterol loading of ECs by either the cholesterol-cyclodextrin complex or caveolin-1 overexpression inhibited OxPAPC induction of IL-8. Cholesterol 13-24 caveolin 1 Homo sapiens 90-100 15539932-1 2004 Caveolin-1 is the principal structural protein of caveolae, sphingolipid and cholesterol-rich invaginations of the plasma membrane involved in vesicular trafficking and signal transduction. Cholesterol 77-88 caveolin 1 Homo sapiens 0-10 15240128-4 2004 By measuring fluorescence and flow cytometry using the fluorescence dyes 1,6-diphenyl-1,3,5-hexatriene and Merocyanine 540, we found that overexpressing caveolin-1 resulted in a similar increase in membrane fluidity and loosening of lipid packing density as cholesterol depletion by 1 mM methyl-beta-cyclodextrin (MbetaCD) or 2-hydroxypropyl-beta-cyclodextrin (HbetaCD). Cholesterol 258-269 caveolin 1 Homo sapiens 153-163 15240128-6 2004 Our data demonstrate for the first time that the reduction of the plasma membrane cholesterol level induced by overexpressing caveolin-1 may indirectly inhibit P-gp transport activity by increasing plasma membrane fluidity. Cholesterol 82-93 caveolin 1 Homo sapiens 126-136 14992595-2 2004 This was measured after immunoprecipitation of caveolin-1 from cells labeled with tritiated cholesterol or the photoactivable cholesterol analogue FCBP [Fielding et al. Cholesterol 92-103 caveolin 1 Homo sapiens 47-57 15213113-7 2004 In contrast, extracting or changing membrane-bound cholesterol by means of drugs that modify lipid rafts (MBCD, filipin III, or mevalonate plus lovastatin plus MBCD) inhibited the entry of Dr-positive IH11128 both into cells that expressed VIP21/caveolin (HeLa and Caco-2/Cav-1 cells) and into those that did not (parental Caco-2 cells). Cholesterol 51-62 caveolin 1 Homo sapiens 240-271 15213113-7 2004 In contrast, extracting or changing membrane-bound cholesterol by means of drugs that modify lipid rafts (MBCD, filipin III, or mevalonate plus lovastatin plus MBCD) inhibited the entry of Dr-positive IH11128 both into cells that expressed VIP21/caveolin (HeLa and Caco-2/Cav-1 cells) and into those that did not (parental Caco-2 cells). Cholesterol 51-62 caveolin 1 Homo sapiens 272-277 15001554-1 2004 Caveolin-1, a putative mediator of intracellular cholesterol transport, is generally assumed to be integrated into the cytoplasmic leaflets of all cellular membranes. Cholesterol 49-60 caveolin 1 Homo sapiens 0-10 14729661-0 2004 Expression of caveolin-1 enhances cholesterol efflux in hepatic cells. Cholesterol 34-45 caveolin 1 Homo sapiens 14-24 14729661-11 2004 We conclude that overexpression of caveolin-1 in hepatic cells stimulates cholesterol efflux by enhancing transfer of cholesterol to cholesterol-rich domains in the plasma membrane. Cholesterol 74-85 caveolin 1 Homo sapiens 35-45 14729661-11 2004 We conclude that overexpression of caveolin-1 in hepatic cells stimulates cholesterol efflux by enhancing transfer of cholesterol to cholesterol-rich domains in the plasma membrane. Cholesterol 118-129 caveolin 1 Homo sapiens 35-45 14729661-11 2004 We conclude that overexpression of caveolin-1 in hepatic cells stimulates cholesterol efflux by enhancing transfer of cholesterol to cholesterol-rich domains in the plasma membrane. Cholesterol 118-129 caveolin 1 Homo sapiens 35-45 15143558-0 2004 [High cholesterol level upregulate the expression of caveolin-1]. Cholesterol 6-17 caveolin 1 Homo sapiens 53-63 15143558-3 2004 In the initial stage of hypercholesterolemia model, the expression of caveolin-1 increased as the time of high cholesterol level added, but in the later period it was decreased slightly. Cholesterol 29-40 caveolin 1 Homo sapiens 70-80 14670987-5 2004 We demonstrate for the first time by biochemical methods the existence of sphingolipid-cholesterol-enriched domains in human and dog thyroid follicular cells that contain caveolin, flotillin-2, and the insulin receptor. Cholesterol 87-98 caveolin 1 Homo sapiens 171-179 15032325-8 2004 In the gut, caveolin-1-rich lipid particles can act as donor particles to facilitate (protein-mediated) intestinal uptake of cholesterol and phospholipids. Cholesterol 125-136 caveolin 1 Homo sapiens 12-22 12657603-14 2003 Specific proteins, such as caveolin-1, must recruit cholesterol and induce clustering. Cholesterol 52-63 caveolin 1 Homo sapiens 27-37 14707126-2 2004 CD147-caveolin-1 complex formation was temperature and cholesterol dependent, reminiscent of associations seen within caveolae/lipid rafts. Cholesterol 55-66 caveolin 1 Homo sapiens 6-16 12639973-0 2003 Visualizing caveolin-1 and HDL in cholesterol-loaded aortic endothelial cells. Cholesterol 34-45 caveolin 1 Homo sapiens 12-30 12639973-3 2003 The goal of the present study was to investigate the location and distribution of caveolin-1, the main structural protein component of caveolae, in cholesterol-loaded aortic endothelial cells after HDL incubation. Cholesterol 148-159 caveolin 1 Homo sapiens 82-92 11883949-6 2002 While caveolin has been associated with cholesterol transport, signal transduction, and transcytosis, this study provides evidence that caveolin is also a SNARE accessory protein. Cholesterol 40-51 caveolin 1 Homo sapiens 6-14 12482878-5 2003 Cholesterol depletion by beta-cyclodextrin results in the loss of caveola structure in myeloma cells, as shown by transmission electron microscopy, and loss of caveolin-1 function. Cholesterol 0-11 caveolin 1 Homo sapiens 160-170 12482878-9 2003 Therefore, cholesterol depletion by beta-cyclodextrin abrogates both interleukin-6- and insulin-like growth factor-I-triggered multiple myeloma cell survival via negative regulation of caveolin-1. Cholesterol 11-22 caveolin 1 Homo sapiens 185-195 12269838-0 2002 Stabilization of caveolin-1 by cellular cholesterol and scavenger receptor class B type I. Caveolae are 50-100 nm plasma membrane invaginations, which function in cell signaling, in transcytosis, and in regulating cellular cholesterol homeostasis. Cholesterol 40-51 caveolin 1 Homo sapiens 17-27 12269838-0 2002 Stabilization of caveolin-1 by cellular cholesterol and scavenger receptor class B type I. Caveolae are 50-100 nm plasma membrane invaginations, which function in cell signaling, in transcytosis, and in regulating cellular cholesterol homeostasis. Cholesterol 223-234 caveolin 1 Homo sapiens 17-27 12269838-8 2002 When cells were loaded with cholesterol, we observed the dramatic stabilization of caveolin-1 with significant clustering of caveolin-1 at the cell surface. Cholesterol 28-39 caveolin 1 Homo sapiens 83-93 12269838-8 2002 When cells were loaded with cholesterol, we observed the dramatic stabilization of caveolin-1 with significant clustering of caveolin-1 at the cell surface. Cholesterol 28-39 caveolin 1 Homo sapiens 125-135 12269838-9 2002 In addition, a palmitoylation-deficient caveolin-1 mutant was still responsive to cholesterol-induced stabilization, indicating that palmitoylation of caveolin-1 is not required for the cholesterol-induced stabilization of caveolin-1. Cholesterol 82-93 caveolin 1 Homo sapiens 40-50 12269838-10 2002 These results suggest an important role for cholesterol and SR-BI in the regulation of caveolin functioning, especially in cell types such as endothelial cells and macrophages, which can be dramatically affected by changes in their cholesterol content during the development of atherosclerosis. Cholesterol 44-55 caveolin 1 Homo sapiens 87-95 12269838-10 2002 These results suggest an important role for cholesterol and SR-BI in the regulation of caveolin functioning, especially in cell types such as endothelial cells and macrophages, which can be dramatically affected by changes in their cholesterol content during the development of atherosclerosis. Cholesterol 232-243 caveolin 1 Homo sapiens 87-95 11880282-8 2002 Experiments with methyl-beta-cyclodextrin, filipin, and antisense caveolin-1 demonstrate that sequestration of the receptors is dependent on cholesterol and caveolin-1. Cholesterol 141-152 caveolin 1 Homo sapiens 66-76 11907140-2 2002 In this article, cholesterol transport to caveolin-1 and caveolin-2 containing compartments, such as the trans-Golgi network (TGN) and plasma membrane caveolae, was examined in normal (NPC+/+), NPC heterozygous (NPC+/-), and NPC homozygous (NPC-/-) human fibroblasts. Cholesterol 17-28 caveolin 1 Homo sapiens 42-52 11907140-7 2002 These studies demonstrate that NPC1 regulates cholesterol transport to caveolin-1 and caveolin-2 containing compartments such as the TGN and plasma membrane caveolae. Cholesterol 46-57 caveolin 1 Homo sapiens 71-81 11827555-5 2002 Expression of caveolin-1 increases the amount of cholesterol recovered in the lipid raft fraction but does not affect the relative proportions of the various phospholipid classes. Cholesterol 49-60 caveolin 1 Homo sapiens 14-24 11888297-4 2002 Caveolae are most likely generated through the subsequent interaction of these caveolin homo-oligomers with one another, with sphingolipids, and with cholesterol. Cholesterol 150-161 caveolin 1 Homo sapiens 79-87 11673056-1 2001 Caveolin-1 traffics cholesterol between the endoplasmic reticulum and cell surface caveolae in a non-vesicle chaperone complex which contains heat shock protein 56, cyclophilin 40, and cyclophilin A. Cholesterol 20-31 caveolin 1 Homo sapiens 0-10 11689206-2 2001 We have examined the interaction of recombinant His-tagged caveolin-1 with cholesterol and 7-keto cholesterol, the most abundant non-enzymatically formed oxysterol found in oxidised LDL and atheromatous plaque. Cholesterol 75-86 caveolin 1 Homo sapiens 59-69 11683884-3 2001 The caveola protein, caveolin-1, binds to cholesterol and is involved in intracellular cholesterol trafficking. Cholesterol 42-53 caveolin 1 Homo sapiens 21-31 11683884-3 2001 The caveola protein, caveolin-1, binds to cholesterol and is involved in intracellular cholesterol trafficking. Cholesterol 87-98 caveolin 1 Homo sapiens 21-31 11551402-4 2001 The relationship between caveolin and MDR may be linked to the function of caveolin-1 in mediating cholesterol efflux, a pathway that we hypothesized to facilitate the delivery of drugs from intracellular compartments to plasma membrane resident drug transporters. Cholesterol 99-110 caveolin 1 Homo sapiens 75-85 11529503-2 2001 The objective of this study was to analyse cholesterol esterification and the expression of MDR1 (multidrug resistance), ACAT (acyl-CoA:cholesterol acyltransferase) and caveolin-1 genes in atherosclerotic and healthy vascular walls, in SMCs obtained from atherosclerotic lesions and saphenous veins. Cholesterol 43-54 caveolin 1 Homo sapiens 169-179 11294831-7 2001 In response to cell surface cholesterol oxidation, BENE redistributed to the dilated vesicular structures that concentrate most of the caveolin-1 originally on the cell surface. Cholesterol 28-39 caveolin 1 Homo sapiens 135-145 11278313-1 2001 Caveolin-1 is a palmitoylated protein involved in assembly of signaling molecules in plasma membrane subdomains termed caveolae and in intracellular cholesterol transport. Cholesterol 149-160 caveolin 1 Homo sapiens 0-10 11339822-7 2001 In addition, depletion of cellular cholesterol by mevalonate and methyl-beta-cyclodextrin leads to the shift of PGI2 synthase and caveolin-1 to higher density fractions of the gradient. Cholesterol 35-46 caveolin 1 Homo sapiens 130-140 11102446-3 2001 Caveolae are cholesterol-rich membrane microdomains that, along with their marker protein caveolin-1 (Cav-1), have been implicated in the compartmentalization and regulation of certain signaling events. Cholesterol 13-24 caveolin 1 Homo sapiens 90-100 11102446-3 2001 Caveolae are cholesterol-rich membrane microdomains that, along with their marker protein caveolin-1 (Cav-1), have been implicated in the compartmentalization and regulation of certain signaling events. Cholesterol 13-24 caveolin 1 Homo sapiens 102-107 11136695-2 2001 Increased uptake of cholesterol by endothelial cells (ECs) upregulates the abundance of the structural protein caveolin-1 and impairs NO release through the stabilization of the inhibitory heterocomplex between caveolin-1 and endothelial NO synthase (eNOS). Cholesterol 20-31 caveolin 1 Homo sapiens 111-121 11136695-2 2001 Increased uptake of cholesterol by endothelial cells (ECs) upregulates the abundance of the structural protein caveolin-1 and impairs NO release through the stabilization of the inhibitory heterocomplex between caveolin-1 and endothelial NO synthase (eNOS). Cholesterol 20-31 caveolin 1 Homo sapiens 211-221 11108728-0 2000 Involvement of caveolin-1 in cholesterol enrichment of high density lipoprotein during its assembly by apolipoprotein and THP-1 cells. Cholesterol 29-40 caveolin 1 Homo sapiens 15-25 11073854-9 2000 Finally, we determined the binding of [(3)H]-labeled free cholesterol and recombinant H-Ras to Cav-1 fusion proteins in vitro. Cholesterol 58-69 caveolin 1 Homo sapiens 95-100 11073854-10 2000 Both cholesterol and Ras bound to full-length GST-Cav-1, scaffolding domain (61-101), and C-terminal (135-178) Cav-1 fusion peptides. Cholesterol 5-16 caveolin 1 Homo sapiens 50-55 11073854-10 2000 Both cholesterol and Ras bound to full-length GST-Cav-1, scaffolding domain (61-101), and C-terminal (135-178) Cav-1 fusion peptides. Cholesterol 5-16 caveolin 1 Homo sapiens 111-116 11073854-11 2000 Addition of cholesterol enhanced Ras binding to the full-length and scaffolding domain of Cav-1 but not to the C-terminal Cav-1. Cholesterol 12-23 caveolin 1 Homo sapiens 90-95 11073854-12 2000 These findings strongly suggest a role for Cav-1 in cholesterol trafficking and cholesterol-mediated intracellular signaling, which may mediate EC activation by LDL. Cholesterol 52-63 caveolin 1 Homo sapiens 43-48 11073854-12 2000 These findings strongly suggest a role for Cav-1 in cholesterol trafficking and cholesterol-mediated intracellular signaling, which may mediate EC activation by LDL. Cholesterol 80-91 caveolin 1 Homo sapiens 43-48 11108728-7 2000 When the cells were treated with the antisense DNA of caveolin-1 and differentiated, both caveolin-1 synthesis and cholesterol incorporation into the HDL were reduced in parallel to generate the cholesterol-poor HDL. Cholesterol 115-126 caveolin 1 Homo sapiens 54-64 11108728-7 2000 When the cells were treated with the antisense DNA of caveolin-1 and differentiated, both caveolin-1 synthesis and cholesterol incorporation into the HDL were reduced in parallel to generate the cholesterol-poor HDL. Cholesterol 195-206 caveolin 1 Homo sapiens 54-64 11108728-8 2000 We concluded that caveolin-1 is involved in enrichment with cholesterol of the HDL generated by the apolipoprotein-cell interaction. Cholesterol 60-71 caveolin 1 Homo sapiens 18-28 10833523-0 2000 Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. Cholesterol 45-56 caveolin 1 Homo sapiens 18-28 10833523-0 2000 Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. Cholesterol 118-129 caveolin 1 Homo sapiens 18-28 10833523-3 2000 In the present study, we hypothesized that palmitoylation of caveolin-1 is necessary for binding of cholesterol, formation of a caveolin-chaperone transport complex, and rapid, direct transport of cholesterol to caveolae. Cholesterol 100-111 caveolin 1 Homo sapiens 61-71 10833523-3 2000 In the present study, we hypothesized that palmitoylation of caveolin-1 is necessary for binding of cholesterol, formation of a caveolin-chaperone transport complex, and rapid, direct transport of cholesterol to caveolae. Cholesterol 197-208 caveolin 1 Homo sapiens 61-71 10833523-7 2000 Wild type caveolin-1 and mutant 133 assembled into complete transport complexes and rapidly (10-20 min) transported cholesterol to caveolae. Cholesterol 116-127 caveolin 1 Homo sapiens 10-20 10833523-10 2000 We conclude that palmitoylation of caveolin-1 at positions 143 and 156 is required for cholesterol binding and transport complex formation. Cholesterol 87-98 caveolin 1 Homo sapiens 35-45 9183542-4 1997 Specialized plasma membrane invaginations, caveolae, were implicated in cholesterol efflux, and the abundant caveolar protein, caveolin-1 which belongs to a newly discovered caveolin family of proteins, was shown to be a cholesterol-binding membrane protein. Cholesterol 221-232 caveolin 1 Homo sapiens 127-137 10629215-1 2000 Caveolin-1 is an integral membrane protein of caveolae that is thought to play an important role in both the traffic of cholesterol to caveolae and modulating the activity of multiple signaling molecules at this site. Cholesterol 120-131 caveolin 1 Homo sapiens 0-10 9183542-4 1997 Specialized plasma membrane invaginations, caveolae, were implicated in cholesterol efflux, and the abundant caveolar protein, caveolin-1 which belongs to a newly discovered caveolin family of proteins, was shown to be a cholesterol-binding membrane protein. Cholesterol 221-232 caveolin 1 Homo sapiens 127-135 8791446-2 1996 Highlights include the identification of new caveolin family members, the characterization of VIP21-caveolin as a cholesterol-binding oligomeric protein, and evidence for functional interactions between caveolins and heterotrimeric G proteins. Cholesterol 114-125 caveolin 1 Homo sapiens 94-99 8690074-0 1996 Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol. Cholesterol 90-101 caveolin 1 Homo sapiens 19-24 22500212-3 2012 These interactions indicate that cholesterol/caveolin-1 plays a role in NSP4 transport to the cell surface, which is essential to its enterotoxic activity. Cholesterol 33-44 caveolin 1 Homo sapiens 45-55 33811938-5 2021 AdhAQP1-transduced hepatocytes show that the canalicularly-expressed hAQP1 not only enhances osmotic membrane water permeability but also induces the transport activities of BSEP/ABCB11 and MRP2/ABCC2 by redistribution in canalicular cholesterol-rich microdomains likely through interactions with the cholesterol-binding protein caveolin-1. Cholesterol 234-245 caveolin 1 Homo sapiens 329-339 33811938-5 2021 AdhAQP1-transduced hepatocytes show that the canalicularly-expressed hAQP1 not only enhances osmotic membrane water permeability but also induces the transport activities of BSEP/ABCB11 and MRP2/ABCC2 by redistribution in canalicular cholesterol-rich microdomains likely through interactions with the cholesterol-binding protein caveolin-1. Cholesterol 301-312 caveolin 1 Homo sapiens 329-339 22500212-6 2012 Direct fluorescence-binding assays were employed to determine binding affinities of the NSP4-caveolin-1 peptides and cholesterol. Cholesterol 117-128 caveolin 1 Homo sapiens 93-103 34359618-9 2021 Addition of labelled-TF resulted in the accumulation within caveolin-1-containing cholesterol-rich regions and was also accompanied with the increased assimilation of cell-surface fVIIa. Cholesterol 82-93 caveolin 1 Homo sapiens 60-70 34545870-3 2021 The molecular mechanisms underlying the interactions of cav-1 with complex membranes, leading to modulation of membrane topology and the formation of cholesterol-rich domains, remain elusive. Cholesterol 150-161 caveolin 1 Homo sapiens 56-61 34122329-0 2021 Crosstalk Between LXR and Caveolin-1 Signaling Supports Cholesterol Efflux and Anti-Inflammatory Pathways in Macrophages. Cholesterol 56-67 caveolin 1 Homo sapiens 26-36 34436568-1 2022 Caveolin-1 (Cav-1) is a structural protein component of caveolae, which are invaginations of the plasma membrane involved in various cellular processes, including endocytosis, extracellular matrix organization, cholesterol distribution, cell migration, and signaling. Cholesterol 211-222 caveolin 1 Homo sapiens 0-10 34436568-1 2022 Caveolin-1 (Cav-1) is a structural protein component of caveolae, which are invaginations of the plasma membrane involved in various cellular processes, including endocytosis, extracellular matrix organization, cholesterol distribution, cell migration, and signaling. Cholesterol 211-222 caveolin 1 Homo sapiens 12-17 34210318-1 2021 BACKGROUND: Caveolin-1 (CAV-1) is a cholesterol-dependent essential component located in caveolae. Cholesterol 36-47 caveolin 1 Homo sapiens 12-22 34210318-1 2021 BACKGROUND: Caveolin-1 (CAV-1) is a cholesterol-dependent essential component located in caveolae. Cholesterol 36-47 caveolin 1 Homo sapiens 24-29 34210318-8 2021 RESULTS: There was a significant interaction between CAV-1 rs3807992 and healthy DP on high-density cholesterol (HDL) (P-interaction = 0.03), TC/HDL (P-interaction = 0.03) and high sensitivity C-reactive protein (hs-CRP) (P-interaction = 0.04); in A-allele carriers, higher following a healthy DP was related to a higher level of HDL and lower TC/HDL and hs-CRP. Cholesterol 100-111 caveolin 1 Homo sapiens 53-58 34122329-6 2021 Although the role of Cav-1 in cellular cholesterol homeostasis and vascular inflammation has been reported, the connection between LXR transcriptional activity and Cav-1 expression and function in macrophages has not been investigated. Cholesterol 39-50 caveolin 1 Homo sapiens 21-26 34122329-8 2021 As a result, Cav-1 participates in LXR-dependent cholesterol efflux and the control of inflammatory responses. Cholesterol 49-60 caveolin 1 Homo sapiens 13-18 34122329-9 2021 Together, our data show modulation of the LXR-Cav-1 axis could be exploited to control exacerbated inflammation and cholesterol overload in the macrophage during the pathogenesis of lipid and immune disorders, such as atherosclerosis. Cholesterol 116-127 caveolin 1 Homo sapiens 46-51 33996409-1 2021 As one of the most important components of caveolae, caveolin-1 is involved in caveolae-mediated endocytosis and transcytosis pathways, and also plays a role in regulating the cell membrane cholesterol homeostasis and mediating signal transduction. Cholesterol 190-201 caveolin 1 Homo sapiens 53-63 35467110-6 2022 The most interesting aspect of caveolin-1 membrane binding is the interplay of cholesterol clustering and membrane curvature. Cholesterol 79-90 caveolin 1 Homo sapiens 31-41 35467110-7 2022 Although cholesterol has been reported to cluster in the vicinity of caveolin-1 by several approaches, simulations show that the clustering is maximal in membrane leaflet opposing the surface-bound caveolin-1. Cholesterol 9-20 caveolin 1 Homo sapiens 69-79 35467110-7 2022 Although cholesterol has been reported to cluster in the vicinity of caveolin-1 by several approaches, simulations show that the clustering is maximal in membrane leaflet opposing the surface-bound caveolin-1. Cholesterol 9-20 caveolin 1 Homo sapiens 198-208 35545719-4 2022 We show that TFEB favors ECM adhesion turnover by promoting the transcription of genes that drive the synthesis of cholesterol, which promotes the aggregation of caveolin-1, and the caveolin-dependent endocytosis of integrin beta1. Cholesterol 115-126 caveolin 1 Homo sapiens 162-172 35534471-4 2022 We show a negative correlation between CAV1 tumoral protein levels - a major protein of cholesterol-rich membrane domains - and Trastuzumab-drug conjugate TDM1 tumor uptake. Cholesterol 88-99 caveolin 1 Homo sapiens 39-43 35419431-7 2022 Recent literature has provided new insight, with two membrane lipids, phosphatidylinositol 4,5-bisphosphate (PIP2) and cholesterol, noted to (1) stabilize Kir2 channels in a preferred open or closed state, respectively, and (2) confer, in association with the cytoskeleton, caveolin-1 (Cav1) and syntrophin, hemodynamic sensitivity. Cholesterol 119-130 caveolin 1 Homo sapiens 274-284 35419431-7 2022 Recent literature has provided new insight, with two membrane lipids, phosphatidylinositol 4,5-bisphosphate (PIP2) and cholesterol, noted to (1) stabilize Kir2 channels in a preferred open or closed state, respectively, and (2) confer, in association with the cytoskeleton, caveolin-1 (Cav1) and syntrophin, hemodynamic sensitivity. Cholesterol 119-130 caveolin 1 Homo sapiens 286-290 33533890-10 2021 Lastly, cholesterol depletion reduced the interaction of Kv7.4 with caveolin-1 and dynein while increasing the overall membrane expression of Kv7.4, although it attenuated the Kv7.4 current in oocytes and interfered with the action of ciliobrevin D and channel activators in arterial segments. Cholesterol 8-19 caveolin 1 Homo sapiens 68-78 33279502-2 2021 Previous studies indicate that caveolin-1 exhibits a pathogenic capacity in atherosclerosis via the regulation of membrane trafficking, cholesterol metabolism and cellular signal transduction. Cholesterol 136-147 caveolin 1 Homo sapiens 31-41 32997514-9 2020 Furthermore, through studies in caveolin-1 knockdown cells, as well as subcellular distribution studies in cell lines with different alpha isoforms, we found that Na/K-ATPase, Src and caveolin-1 worked together for the cholesterol regulation. Cholesterol 219-230 caveolin 1 Homo sapiens 32-42 32997514-9 2020 Furthermore, through studies in caveolin-1 knockdown cells, as well as subcellular distribution studies in cell lines with different alpha isoforms, we found that Na/K-ATPase, Src and caveolin-1 worked together for the cholesterol regulation. Cholesterol 219-230 caveolin 1 Homo sapiens 184-194 32878944-7 2020 Consistently, the depletion of cholesterol from the plasma membrane induced the PACSIN2-localized tubules with caveolin-1 at their tips, suggesting that cholesterol inhibited the membrane tubulation by PACSIN2. Cholesterol 31-42 caveolin 1 Homo sapiens 111-121 32997514-10 2020 Taken together, these new findings reveal that the putative Src binding domain and the intact Na/K-ATPase/Src/caveolin-1 complex is indispensable for the isoform-specific regulation of Na/K-ATPase by cholesterol. Cholesterol 200-211 caveolin 1 Homo sapiens 110-120 33053168-3 2020 We show that caveolin-1 (Cav1) centrally regulates exosome biogenesis and exosomal protein cargo sorting through the control of cholesterol content at the endosomal compartment/MVBs. Cholesterol 128-139 caveolin 1 Homo sapiens 13-23 33053168-3 2020 We show that caveolin-1 (Cav1) centrally regulates exosome biogenesis and exosomal protein cargo sorting through the control of cholesterol content at the endosomal compartment/MVBs. Cholesterol 128-139 caveolin 1 Homo sapiens 25-29 33053168-6 2020 Cav1 acts as a cholesterol rheostat in MVBs, determining sorting of ECM components into specific exosome pools and thus ECM deposition. Cholesterol 15-26 caveolin 1 Homo sapiens 0-4 33123955-2 2020 Some of these clinical characteristics have been associated with caveolin-1, a caveolae structural protein, responsible for insulin activation, storage and degradation of cholesterol, and so on. Cholesterol 171-182 caveolin 1 Homo sapiens 65-75 32878944-7 2020 Consistently, the depletion of cholesterol from the plasma membrane induced the PACSIN2-localized tubules with caveolin-1 at their tips, suggesting that cholesterol inhibited the membrane tubulation by PACSIN2. Cholesterol 153-164 caveolin 1 Homo sapiens 111-121 33090411-1 2020 OBJECTIVE: Caveolin-1 plays critical roles in regulating signal transduction and cholesterol trafficking in cells. Cholesterol 81-92 caveolin 1 Homo sapiens 11-21 32855410-3 2020 Mechanistic studies of the underlying tumor supportive onco-metabolism reveal coordinated activities through which Cav-1 enables rewiring of cancer cell lipid metabolism towards a program of 1) exogenous sphingolipid scavenging independent of cholesterol, 2) increased cancer cell catabolism of sphingomyelins to ceramide derivatives and 3) altered ceramide metabolism that results in increased glycosphingolipid synthesis and efflux of Cav-1-sphingolipid particles containing mitochondrial proteins and lipids. Cholesterol 243-254 caveolin 1 Homo sapiens 115-120 32986849-8 2021 On the other hand, oxLDLs may affect cholesterol plasma membrane content/distribution thus influencing caveolae architecture, Cav-1 localization and the associated signaling. Cholesterol 37-48 caveolin 1 Homo sapiens 126-131 32476424-1 2020 The caveolin-1 (cav-1) protein is an integral component of caveolae and has been reported to co-localize with cholesterol and sphingomyelin-rich curved membrane domains. Cholesterol 110-121 caveolin 1 Homo sapiens 4-14 32476424-1 2020 The caveolin-1 (cav-1) protein is an integral component of caveolae and has been reported to co-localize with cholesterol and sphingomyelin-rich curved membrane domains. Cholesterol 110-121 caveolin 1 Homo sapiens 16-21 32476424-3 2020 We considered a palmitoylated-cav-1 construct interacting with phospholipid/cholesterol membranes with asymmetrically distributed sphingomyelin, varying between 5-15% in total. Cholesterol 76-87 caveolin 1 Homo sapiens 30-35 32476424-5 2020 Both cholesterol and sphingomyelin are observed to cluster in cav-1 bound membranes, mainly in the extracellular leaflet. Cholesterol 5-16 caveolin 1 Homo sapiens 62-67 32109845-6 2020 The reverse cholesterol transport is related to caveolae and caveolin proteins, and CAV-1 is directly connected to cholesterol transport. Cholesterol 12-23 caveolin 1 Homo sapiens 61-69 32109845-0 2020 Caveolin proteins electrochemical oxidation and interaction with cholesterol. Cholesterol 65-76 caveolin 1 Homo sapiens 0-8 32109845-6 2020 The reverse cholesterol transport is related to caveolae and caveolin proteins, and CAV-1 is directly connected to cholesterol transport. Cholesterol 115-126 caveolin 1 Homo sapiens 84-89 32109845-7 2020 The influence of cholesterol on the three caveolin proteins electrochemical behaviour was evaluated. Cholesterol 17-28 caveolin 1 Homo sapiens 42-50 32109845-8 2020 In the absence and in the presence of cholesterol, significant differences in the CAV-1 oxidation peak current were observed. Cholesterol 38-49 caveolin 1 Homo sapiens 82-87 32357558-3 2020 Caveolae/caveolin-1 is tightly associated with a wide range of biological processes, including cholesterol homeostasis, cell mechano-sensing, tumorigenesis, and signal transduction. Cholesterol 95-106 caveolin 1 Homo sapiens 9-19 32428234-11 2020 Conclusions: Regulation of aqueous humor outflow via the caveolin-1/endothelial NO synthase/NO pathway is a newly defined function of ABCA1 that is different from its traditional role in mediating cholesterol efflux. Cholesterol 197-208 caveolin 1 Homo sapiens 57-67 30290209-4 2018 Further, we show that CD133 in these cells is localized in the lipid-rafts (characterized by Cav-1-cholesterol association). Cholesterol 99-110 caveolin 1 Homo sapiens 93-98 32082483-3 2020 Caveolin-1 (CAV1), an integral membrane protein, is the principal component of caveolae in membranes and is involved in multiple cellular functions such as endocytosis, cholesterol homeostasis, signal transduction, and mechanoprotection. Cholesterol 169-180 caveolin 1 Homo sapiens 0-10 32082483-3 2020 Caveolin-1 (CAV1), an integral membrane protein, is the principal component of caveolae in membranes and is involved in multiple cellular functions such as endocytosis, cholesterol homeostasis, signal transduction, and mechanoprotection. Cholesterol 169-180 caveolin 1 Homo sapiens 12-16 31727739-9 2019 Paradoxically, the amount of free cholesterol increased on the surface of LDs in ACAT1/2-overexpressing adipocytes, accompanied by increased LD localization of caveolin-1. Cholesterol 34-45 caveolin 1 Homo sapiens 160-170 31646333-3 2019 Caveolin-1 (Cav-1), a constituent protein of caveolae, is involved in not only the formation of the caveolae, vesicular transport, maintaining cholesterol homeostasis directly, but also many cellular physiological and pathological processes including growth, regulation of mitochondrial antioxidant level, apoptosis and carcinomas by interacting with a lot of signaling molecules through caveolin scaffolding domain. Cholesterol 143-154 caveolin 1 Homo sapiens 0-10 31646333-3 2019 Caveolin-1 (Cav-1), a constituent protein of caveolae, is involved in not only the formation of the caveolae, vesicular transport, maintaining cholesterol homeostasis directly, but also many cellular physiological and pathological processes including growth, regulation of mitochondrial antioxidant level, apoptosis and carcinomas by interacting with a lot of signaling molecules through caveolin scaffolding domain. Cholesterol 143-154 caveolin 1 Homo sapiens 12-17 30742851-1 2019 Caveolin-1 is the main structural and functional component of caveolin, and it is involved in the regulation of cholesterol transport, endocytosis, and signal transduction. Cholesterol 112-123 caveolin 1 Homo sapiens 0-10 30742851-1 2019 Caveolin-1 is the main structural and functional component of caveolin, and it is involved in the regulation of cholesterol transport, endocytosis, and signal transduction. Cholesterol 112-123 caveolin 1 Homo sapiens 62-70 30673589-2 2019 Caveolin-1 (Cav-1) is a major protein of caveolae, which participates in various cellular functions, such as vesicle trafficking, cholesterol homeostasis, tumor progression, etc. Cholesterol 130-141 caveolin 1 Homo sapiens 0-10 30673589-2 2019 Caveolin-1 (Cav-1) is a major protein of caveolae, which participates in various cellular functions, such as vesicle trafficking, cholesterol homeostasis, tumor progression, etc. Cholesterol 130-141 caveolin 1 Homo sapiens 12-17 30463973-4 2019 The caveolin chaperone complex (CCC) is a cytoplasmic complex formed by caveolin-1 and the chaperones FKBP52, Cy40, and CyA and is responsible for the cholesterol traffic inside the cell. Cholesterol 151-162 caveolin 1 Homo sapiens 72-82 30579563-1 2019 Caveolin-1 (cav-1) is an important player in cell signaling and endocytosis that has been shown to colocalize with cholesterol-rich membrane domains. Cholesterol 115-126 caveolin 1 Homo sapiens 0-10 30579563-1 2019 Caveolin-1 (cav-1) is an important player in cell signaling and endocytosis that has been shown to colocalize with cholesterol-rich membrane domains. Cholesterol 115-126 caveolin 1 Homo sapiens 12-17 30579563-2 2019 Experimental studies with varying cav-1 constructs have suggested that it can induce both cholesterol clustering and membrane curvature. Cholesterol 90-101 caveolin 1 Homo sapiens 34-39 30579563-3 2019 Here, we probe the molecular origin of membrane curvature and cholesterol clustering by cav-1 by using coarse-grain molecular dynamics simulations. Cholesterol 62-73 caveolin 1 Homo sapiens 88-93 30579563-5 2019 Our results suggest that cav-1 is able to induce cholesterol clustering in the membrane leaflet to which it is bound as well as the opposing leaflet. Cholesterol 49-60 caveolin 1 Homo sapiens 25-30 30579563-6 2019 A positive membrane curvature is observed upon cav-1 binding in cholesterol-containing bilayers. Cholesterol 64-75 caveolin 1 Homo sapiens 47-52 30579563-7 2019 Interestingly, we observe an interplay between cholesterol clustering and membrane curvature such that cav-1 is able to induce higher membrane curvature in cholesterol-rich membranes. Cholesterol 47-58 caveolin 1 Homo sapiens 103-108 30579563-7 2019 Interestingly, we observe an interplay between cholesterol clustering and membrane curvature such that cav-1 is able to induce higher membrane curvature in cholesterol-rich membranes. Cholesterol 156-167 caveolin 1 Homo sapiens 103-108 30579563-9 2019 Further, we address the importance of the secondary structure of cav-1 domains and show that it could play an important role in membrane curvature and cholesterol clustering. Cholesterol 151-162 caveolin 1 Homo sapiens 65-70 29615119-6 2018 Findings from this study will contribute to the understanding of how cholesterol/CAV-1/caveolae regulates aspects of the cell membrane important to cell adhesion, substrate sensing, and microenvironment interaction. Cholesterol 69-80 caveolin 1 Homo sapiens 81-86 29615119-11 2018 RESULTS: Cholesterol supplementation to MSCs increased membrane cholesterol, and resulted in decreased membrane fluidity and localization of elevated numbers of caveolae and CAV-1 to the cell membrane. Cholesterol 9-20 caveolin 1 Homo sapiens 174-179 29615119-13 2018 Conversely, knockdown of CAV-1 expression or cholesterol depletion on MSCs caused a parallel decrease in caveolae content and an increase in membrane fluidity due to decreased delivery of cholesterol to the cell membrane. Cholesterol 188-199 caveolin 1 Homo sapiens 25-30 29615119-15 2018 CONCLUSIONS: Our results demonstrate that perturbations in cholesterol/CAV-1 levels significantly affect the membrane properties of MSCs. Cholesterol 59-70 caveolin 1 Homo sapiens 71-76 29091885-11 2018 The cholesterol supplementation enhanced the clonogenic potential and upregulated the expression of caveolin-1 and LRP6. Cholesterol 4-15 caveolin 1 Homo sapiens 100-110 28919480-5 2017 In the present study we found that reducing PM cholesterol results in the internalization of Orai1 channels, which can be prevented by overexpressing caveolin 1 (Cav1). Cholesterol 47-58 caveolin 1 Homo sapiens 150-160 28919480-5 2017 In the present study we found that reducing PM cholesterol results in the internalization of Orai1 channels, which can be prevented by overexpressing caveolin 1 (Cav1). Cholesterol 47-58 caveolin 1 Homo sapiens 162-166 28919480-7 2017 The effects of reducing cholesterol were not limited to an increased rate of Orai1 internalization, but also, affects the lateral movement of Orai1, inducing movement in a linear pattern (unobstructed diffusion) opposite to basal cholesterol conditions were most of Orai1 channels moves in a confined space, as assessed by Fluorescence Correlation Spectroscopy, Cav1 overexpression inhibited these alterations maintaining Orai1 into a confined and partially confined movement. Cholesterol 24-35 caveolin 1 Homo sapiens 362-366 28835336-9 2017 In vivo and in vitro, increased mu-calpain activity resulted in proteolysis of the membrane cholesterol trafficking protein caveolin-1. Cholesterol 92-103 caveolin 1 Homo sapiens 124-134 28637901-4 2017 We show that Cav1-knockout CD8 T cells have a reduction in membrane cholesterol and sphingomyelin, and upon TCR triggering they exhibit altered morphology and polarity, with reduced effector function compared with Cav1 wild-type CD8 T cells. Cholesterol 68-79 caveolin 1 Homo sapiens 13-17 27832597-8 2017 Interestingly, caveolin-1 (Cav-1), a cholesterol binding and scaffolding protein, regulates neuronal signal transduction and promotes neuroplasticity. Cholesterol 37-48 caveolin 1 Homo sapiens 15-25 28903310-2 2017 Caveolin-1 functions as a scaffolding protein to organize and concentrate signaling molecules within the caveolae, which may be associated with its unique physicochemical properties including oligomerization, acquisition of detergent insolubility, and association with cholesterol. Cholesterol 269-280 caveolin 1 Homo sapiens 0-10 27832597-8 2017 Interestingly, caveolin-1 (Cav-1), a cholesterol binding and scaffolding protein, regulates neuronal signal transduction and promotes neuroplasticity. Cholesterol 37-48 caveolin 1 Homo sapiens 27-32 27852311-1 2016 Caveolin-1 (CAV1) is an oncogenic membrane protein associated with endocytosis, extracellular matrix organisation, cholesterol distribution, cell migration and signaling. Cholesterol 115-126 caveolin 1 Homo sapiens 0-10 28053625-8 2016 A reduced proportion of caveolin-1 found in DRM fractions indicated a cholesterol extraction-induced disruption of lipid raft integrity. Cholesterol 70-81 caveolin 1 Homo sapiens 24-34 27852311-1 2016 Caveolin-1 (CAV1) is an oncogenic membrane protein associated with endocytosis, extracellular matrix organisation, cholesterol distribution, cell migration and signaling. Cholesterol 115-126 caveolin 1 Homo sapiens 12-16 27038819-7 2016 The simulations also provide new insights into the effects of caveolin-1 on the morphology of caveolae and the possible interacting site of cholesterol on caveolin-1. Cholesterol 140-151 caveolin 1 Homo sapiens 155-165 27168348-1 2016 Caveolins (Cav-1, -2 and -3) and Cavins (Cavin-1, -2, -3 and -4) are two protein families controlling the biogenesis and function of caveolae, plasma membrane omega-like invaginations representing the primary site of important cellular processes like endocytosis, cholesterol homeostasis and signal transduction. Cholesterol 264-275 caveolin 1 Homo sapiens 11-27 29714927-1 2016 Mesenchymal stem cells(MSCs)have the property of osteogenic induction.As a result,using the property of MSCs to treat the fractures and bone defects has become a new treatment modality with the development of cell and tissue engineering technology.Caveolae is a flask-shaped membrane microdomain in cell membrane,which composed primarily of cholesterol,sphingolipids and proteins.Caveolin-1is one of the main protein component.Caveolae is the integrator of cell signals,and many signal molecules gather here to bind with caveolin-1protein to regulate cell proliferation,differentiation and other life activities.This paper presents a review about Caveolae/Caveolin-1biologic effects on cell differentiation of MSCs. Cholesterol 341-352 caveolin 1 Homo sapiens 380-390 29714927-1 2016 Mesenchymal stem cells(MSCs)have the property of osteogenic induction.As a result,using the property of MSCs to treat the fractures and bone defects has become a new treatment modality with the development of cell and tissue engineering technology.Caveolae is a flask-shaped membrane microdomain in cell membrane,which composed primarily of cholesterol,sphingolipids and proteins.Caveolin-1is one of the main protein component.Caveolae is the integrator of cell signals,and many signal molecules gather here to bind with caveolin-1protein to regulate cell proliferation,differentiation and other life activities.This paper presents a review about Caveolae/Caveolin-1biologic effects on cell differentiation of MSCs. Cholesterol 341-352 caveolin 1 Homo sapiens 521-531 29714927-1 2016 Mesenchymal stem cells(MSCs)have the property of osteogenic induction.As a result,using the property of MSCs to treat the fractures and bone defects has become a new treatment modality with the development of cell and tissue engineering technology.Caveolae is a flask-shaped membrane microdomain in cell membrane,which composed primarily of cholesterol,sphingolipids and proteins.Caveolin-1is one of the main protein component.Caveolae is the integrator of cell signals,and many signal molecules gather here to bind with caveolin-1protein to regulate cell proliferation,differentiation and other life activities.This paper presents a review about Caveolae/Caveolin-1biologic effects on cell differentiation of MSCs. Cholesterol 341-352 caveolin 1 Homo sapiens 656-666 26918609-8 2016 Perturbation of lipid rafts with the cholesterol-chelating agent MbetaCD also shifts Cav1, c-Src and EGFR out of the rafts and activates signaling pathways. Cholesterol 37-48 caveolin 1 Homo sapiens 85-89 26775739-4 2016 Using far UV circular dichroism spectroscopy it was shown that cholesterol attenuated the helicity of caveolin-1, and that mutation of P110 to alanine caused a significant increase in the alpha-helicity of the protein. Cholesterol 63-74 caveolin 1 Homo sapiens 102-112 27346864-6 2016 Dysregulation of flot-1 and cav-1 by DJ-1 deficiency caused an alteration in the cellular cholesterol level, membrane fluidity, and alteration in lipid rafts-dependent endocytosis. Cholesterol 90-101 caveolin 1 Homo sapiens 28-33 27011179-0 2016 Caveolae and Caveolin-1 Integrate Reverse Cholesterol Transport and Inflammation in Atherosclerosis. Cholesterol 42-53 caveolin 1 Homo sapiens 13-23 27011179-3 2016 Caveolae and caveolin-1 are in the center stage of cholesterol transportation and inflammation in macrophages. Cholesterol 51-62 caveolin 1 Homo sapiens 13-23 27011179-4 2016 Here, we propose that reverse cholesterol transport and inflammation in atherosclerosis can be integrated by caveolae and caveolin-1. Cholesterol 30-41 caveolin 1 Homo sapiens 122-132 26354438-2 2015 The novel nicotinic acetylcholine receptor (nAChR) mutation alphaC418W, the first lipid-exposed mutation identified in a patient that causes slow channel congenital myasthenia syndrome was shown to be cholesterol-sensitive and to accumulate in microdomains rich in the membrane raft marker protein caveolin-1. Cholesterol 201-212 caveolin 1 Homo sapiens 298-308 26409042-1 2015 Caveolin-1 (Cav-1), the homo-oligomeric coat protein of cholesterol-rich caveolae signalosomes, regulates signaling proteins including endothelial nitric oxide synthase (eNOS). Cholesterol 56-67 caveolin 1 Homo sapiens 0-10 26409042-1 2015 Caveolin-1 (Cav-1), the homo-oligomeric coat protein of cholesterol-rich caveolae signalosomes, regulates signaling proteins including endothelial nitric oxide synthase (eNOS). Cholesterol 56-67 caveolin 1 Homo sapiens 12-17 26354438-6 2015 In addition, our results in HEK 293 cells show an interdependence between CAV-1 and alphaC418W that could confer end plates rich in alphaC418W nAChRs to a susceptibility to changes in cholesterol levels that could cause adverse drug reactions to cholesterol-lowering drugs such as statins. Cholesterol 184-195 caveolin 1 Homo sapiens 74-79 26354438-6 2015 In addition, our results in HEK 293 cells show an interdependence between CAV-1 and alphaC418W that could confer end plates rich in alphaC418W nAChRs to a susceptibility to changes in cholesterol levels that could cause adverse drug reactions to cholesterol-lowering drugs such as statins. Cholesterol 246-257 caveolin 1 Homo sapiens 74-79 26354438-7 2015 The current work suggests that the interplay between cholesterol and CAV-1 provides the molecular basis for modulating the function and dynamics of the cholesterol-sensitive alphaC418W nAChR. Cholesterol 152-163 caveolin 1 Homo sapiens 69-74 26304117-1 2015 The generation of caveolae involves insertion of the cholesterol-binding integral membrane protein caveolin-1 (Cav1) into the membrane, however, the precise molecular mechanisms are as yet unknown. Cholesterol 53-64 caveolin 1 Homo sapiens 99-109 26304117-1 2015 The generation of caveolae involves insertion of the cholesterol-binding integral membrane protein caveolin-1 (Cav1) into the membrane, however, the precise molecular mechanisms are as yet unknown. Cholesterol 53-64 caveolin 1 Homo sapiens 111-115 25924234-5 2015 In vitro cholesterol treatment of PC-3 cells stimulated migration and increased IQGAP1 and caveolin-1 protein level and localization to a detergent-resistant fraction. Cholesterol 9-20 caveolin 1 Homo sapiens 91-101 24998359-0 2014 Interactions of caveolin-1 scaffolding and intramembrane regions containing a CRAC motif with cholesterol in lipid bilayers. Cholesterol 94-105 caveolin 1 Homo sapiens 16-26 24998359-1 2014 Caveolin-1 is a major structural protein of caveolae and specifically binds cholesterol (Chol). Cholesterol 76-87 caveolin 1 Homo sapiens 0-10 24998359-1 2014 Caveolin-1 is a major structural protein of caveolae and specifically binds cholesterol (Chol). Cholesterol 89-93 caveolin 1 Homo sapiens 0-10 24998359-2 2014 The caveolin scaffolding domain is thought to be involved in caveolin-Chol interaction through the sequence V94-T-K-Y-W-F-Y-R101, a motif that matches a cholesterol recognition amino-acid consensus (CRAC). Cholesterol 70-74 caveolin 1 Homo sapiens 4-12 24998359-2 2014 The caveolin scaffolding domain is thought to be involved in caveolin-Chol interaction through the sequence V94-T-K-Y-W-F-Y-R101, a motif that matches a cholesterol recognition amino-acid consensus (CRAC). Cholesterol 153-164 caveolin 1 Homo sapiens 4-12 25017566-2 2014 Caveolin-1 plays a key role in carcinogenesis through its diverse roles in membrane trafficking, cholesterol transport and cellular signal transduction. Cholesterol 97-108 caveolin 1 Homo sapiens 0-10 25038242-0 2014 Silencing of Kir2 channels by caveolin-1: cross-talk with cholesterol. Cholesterol 58-69 caveolin 1 Homo sapiens 30-40 25038242-2 2014 Furthermore, it has been proposed that cholesterol-induced regulation of ion channels might be attributed to partitioning into caveolae and association with caveolin-1 (Cav-1). Cholesterol 39-50 caveolin 1 Homo sapiens 157-167 25038242-2 2014 Furthermore, it has been proposed that cholesterol-induced regulation of ion channels might be attributed to partitioning into caveolae and association with caveolin-1 (Cav-1). Cholesterol 39-50 caveolin 1 Homo sapiens 169-174 25038242-9 2014 Moreover, a single point mutation of Kir2.1, L222I that abrogates the sensitivity of the channels to cholesterol also abolishes their sensitivity to Cav-1 suggesting that the two modulators regulate Kir2 channels via a common mechanism. Cholesterol 101-112 caveolin 1 Homo sapiens 149-154 24576892-0 2014 Caveolin-1 interacts with ATP binding cassette transporter G1 (ABCG1) and regulates ABCG1-mediated cholesterol efflux. Cholesterol 99-110 caveolin 1 Homo sapiens 0-10 24576892-4 2014 Knockdown of CAV1 expression using siRNAs significantly reduced ABCG1-mediated cholesterol efflux without detectable effect on ABCA1-mediated cholesterol efflux. Cholesterol 79-90 caveolin 1 Homo sapiens 13-17 24576892-5 2014 Disruption of the putative CAV1 binding site in ABCG1, through replacement of tyrosine residues at positions 487 and 489 or at positions 494 and 495 with alanine (Y487AY489A and Y494AY495A), impaired the interaction of ABCG1 with CAV1 and significantly decreased ABCG1-mediated cholesterol efflux. Cholesterol 278-289 caveolin 1 Homo sapiens 27-31 24576892-9 2014 Finally, we found that CAV1 co-immunoprecipitated with ABCG1 and regulated cholesterol efflux to reconstituted HDL in THP-1-derived macrophages upon the liver X receptor agonist treatment. Cholesterol 75-86 caveolin 1 Homo sapiens 23-27 24576892-10 2014 These findings indicate that CAV1 interacts with ABCG1 and regulates ABCG1-mediated cholesterol efflux. Cholesterol 84-95 caveolin 1 Homo sapiens 29-33 25285302-7 2014 Together, this report presents novel results demonstrating that the NPC1 and caveolin-1 proteins interact to modulate efflux of LDL-derived cholesterol from late endocytic compartments. Cholesterol 140-151 caveolin 1 Homo sapiens 77-87 24643062-12 2014 Furthermore, when cellular cholesterol was depleted by methyl-beta cyclodextrin treatment after DENV entrance, lipid rafts were disrupted, NS3 protein level was reduced, besides Cav-1 and NS3 were displaced to fractions 9 and 10 in sucrose gradient analysis, and we observed a dramatically reduction of DENV particles release. Cholesterol 27-38 caveolin 1 Homo sapiens 178-183 24530906-3 2014 Treatment with the cholesterol biosynthesis inhibitor, zaragozic acid A, shifted the distribution of the LDL receptor to clathrin containing fractions, whereas treatment with cholesterol or LDL shifted the receptor distribution towards caveolin-1 containing fractions. Cholesterol 175-186 caveolin 1 Homo sapiens 236-246 24738074-1 2014 Caveolae/lipid rafts are membrane-rich cholesterol domains endowed with several functions in signal transduction and caveolin-1 (Cav-1) has been reported to be implicated in regulating multiple cancer-associated processes, ranging from tumor growth to multidrug resistance and angiogenesis. Cholesterol 39-50 caveolin 1 Homo sapiens 117-127 24120917-5 2014 With DHA treatment, caveolin-1, a marker for rafts, and EGFR were colocalized with LAMP-1, a lysosomal marker, in a cholesterol-dependent manner, indicating that DHA induces raft fusion with lysosomes. Cholesterol 116-127 caveolin 1 Homo sapiens 20-30 24738074-1 2014 Caveolae/lipid rafts are membrane-rich cholesterol domains endowed with several functions in signal transduction and caveolin-1 (Cav-1) has been reported to be implicated in regulating multiple cancer-associated processes, ranging from tumor growth to multidrug resistance and angiogenesis. Cholesterol 39-50 caveolin 1 Homo sapiens 129-134 24801727-0 2014 Caveolin-1 and ATP binding cassette transporter A1 and G1-mediated cholesterol efflux. Cholesterol 67-78 caveolin 1 Homo sapiens 0-10 24801727-4 2014 Recently, caveolin-1 (CAV1), a scaffolding protein that organizes and concentrates certain caveolin-interacting signaling molecules and receptors within caveolae membranes, has been shown to regulate ABCA1 and ABCG1-mediated cholesterol efflux probably via interacting with them. Cholesterol 225-236 caveolin 1 Homo sapiens 10-20 24801727-4 2014 Recently, caveolin-1 (CAV1), a scaffolding protein that organizes and concentrates certain caveolin-interacting signaling molecules and receptors within caveolae membranes, has been shown to regulate ABCA1 and ABCG1-mediated cholesterol efflux probably via interacting with them. Cholesterol 225-236 caveolin 1 Homo sapiens 22-26 24801727-4 2014 Recently, caveolin-1 (CAV1), a scaffolding protein that organizes and concentrates certain caveolin-interacting signaling molecules and receptors within caveolae membranes, has been shown to regulate ABCA1 and ABCG1-mediated cholesterol efflux probably via interacting with them. Cholesterol 225-236 caveolin 1 Homo sapiens 10-18 24801727-5 2014 In the present review, we summarize the current knowledge and views on the regulatory role of CAV1 on the cholesterol homeostasis with emphasis on the association of CAV1 with ABCA1 and ABCG1. Cholesterol 106-117 caveolin 1 Homo sapiens 94-98 24801727-6 2014 We conclude that the dominance of the positive regulation by CAV1 on the ABCA1 and ABCG1-mediated cholesterol efflux is depending on the species, cell types, as well as the levels of CAV1 expression. Cholesterol 98-109 caveolin 1 Homo sapiens 61-65 24801727-6 2014 We conclude that the dominance of the positive regulation by CAV1 on the ABCA1 and ABCG1-mediated cholesterol efflux is depending on the species, cell types, as well as the levels of CAV1 expression. Cholesterol 98-109 caveolin 1 Homo sapiens 183-187 23729330-8 2013 Cav-1-depleted stromal cells exhibited increased levels of intracellular cholesterol, a precursor for androgen biosynthesis, steroidogenic enzymes, and testosterone. Cholesterol 73-84 caveolin 1 Homo sapiens 0-5 23457390-0 2013 Retraction: Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. Cholesterol 57-68 caveolin 1 Homo sapiens 30-40 23457390-0 2013 Retraction: Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. Cholesterol 130-141 caveolin 1 Homo sapiens 30-40 22594670-7 2012 In addition, we show that contents of DRM markers such as flotillin-1, caveolin-1 and GM1 are altered in DRMs upon cholesterol depletion. Cholesterol 115-126 caveolin 1 Homo sapiens 71-81 22740150-5 2013 In the present report, we could show that a caveolin-1 knockdown resulted in an elevation of cellular cholesterol level; it may indicate an important role of caveolin-1 in cholesterol trafficking to the plasma membrane. Cholesterol 102-113 caveolin 1 Homo sapiens 44-54 22740150-5 2013 In the present report, we could show that a caveolin-1 knockdown resulted in an elevation of cellular cholesterol level; it may indicate an important role of caveolin-1 in cholesterol trafficking to the plasma membrane. Cholesterol 102-113 caveolin 1 Homo sapiens 158-168 22740150-5 2013 In the present report, we could show that a caveolin-1 knockdown resulted in an elevation of cellular cholesterol level; it may indicate an important role of caveolin-1 in cholesterol trafficking to the plasma membrane. Cholesterol 172-183 caveolin 1 Homo sapiens 44-54 22740150-5 2013 In the present report, we could show that a caveolin-1 knockdown resulted in an elevation of cellular cholesterol level; it may indicate an important role of caveolin-1 in cholesterol trafficking to the plasma membrane. Cholesterol 172-183 caveolin 1 Homo sapiens 158-168 23267065-0 2013 Retraction for Smart et al., Annexin 2-caveolin 1 complex is a target of ezetimibe and regulates intestinal cholesterol transport. Cholesterol 108-119 caveolin 1 Homo sapiens 39-49 23199331-0 2012 Cholesterol modulates the structure, binding modes, and energetics of caveolin-membrane interactions. Cholesterol 0-11 caveolin 1 Homo sapiens 70-78 23199331-3 2012 Here, we use coarse-grain molecular dynamics simulations to study the interaction of cav-1 peptides with several model bilayer systems mimicking biological scenarios, such as cholesterol-rich domains, cholesterol-depleted domains, and unsaturated lipid domains. Cholesterol 175-186 caveolin 1 Homo sapiens 85-90 23199331-3 2012 Here, we use coarse-grain molecular dynamics simulations to study the interaction of cav-1 peptides with several model bilayer systems mimicking biological scenarios, such as cholesterol-rich domains, cholesterol-depleted domains, and unsaturated lipid domains. Cholesterol 201-212 caveolin 1 Homo sapiens 85-90 23199331-4 2012 We show that cholesterol modulates the depth as well as orientation of cav-1 binding to membranes. Cholesterol 13-24 caveolin 1 Homo sapiens 71-76 23199331-5 2012 Furthermore, the presence of cholesterol stabilizes more open conformations of cav-1, and we speculate that the binding modes and open conformations could be responsible for inducing morphological changes in the bilayer. Cholesterol 29-40 caveolin 1 Homo sapiens 79-84 23199331-8 2012 Our results highlight molecular details of protein-lipid interplay and provide new insights into the effects of cav-1 in tuning the morphology of cholesterol-rich membranes. Cholesterol 146-157 caveolin 1 Homo sapiens 112-117 22807396-1 2012 Caveolin-1 is a scaffolding protein of cholesterol-rich caveolae lipid rafts in the plasma membrane. Cholesterol 39-50 caveolin 1 Homo sapiens 0-10 22807396-2 2012 In addition to regulating cholesterol transport, caveolin-1 has the ability to bind a diverse array of cell signaling molecules and regulate cell signal transduction in caveolae. Cholesterol 26-37 caveolin 1 Homo sapiens 49-59 23027578-2 2012 Caveolin-1 targets to lipid droplets under certain conditions, where they are involved in signaling and cholesterol balance. Cholesterol 104-115 caveolin 1 Homo sapiens 0-10 23185891-2 2012 Caveolin-1, a marker protein of caveolae, functions as scaffolding protein mediating many physiological and pathological processes including caveolae biogenensis, vesicular transport, cholesterol homeostasis, signal transduction and tumorigenesis. Cholesterol 184-195 caveolin 1 Homo sapiens 0-10 23067370-0 2012 Caveolin-1 reduces HIV-1 infectivity by restoration of HIV Nef mediated impairment of cholesterol efflux by apoA-I. Cholesterol 86-97 caveolin 1 Homo sapiens 0-10 23067370-2 2012 We investigated the effect of caveolin-1 (Cav-1) on the cholesterol efflux by apoA-I in HIV infected primary and THP-1 cell-differentiated macrophages as well as astrocyte derived glioblastoma U87 cells. Cholesterol 56-67 caveolin 1 Homo sapiens 30-40 23067370-2 2012 We investigated the effect of caveolin-1 (Cav-1) on the cholesterol efflux by apoA-I in HIV infected primary and THP-1 cell-differentiated macrophages as well as astrocyte derived glioblastoma U87 cells. Cholesterol 56-67 caveolin 1 Homo sapiens 42-47 23067370-3 2012 RESULTS: Our results reveal that Cav-1 restores the Nef -mediated impairment of cholesterol efflux by apoA-I in both cell types. Cholesterol 80-91 caveolin 1 Homo sapiens 33-38 23067370-6 2012 In addition, we examined the cholesterol composition of HIV particles released from Cav-1 treated cells and identified that the cholesterol content is dramatically reduced. Cholesterol 29-40 caveolin 1 Homo sapiens 84-89 23067370-6 2012 In addition, we examined the cholesterol composition of HIV particles released from Cav-1 treated cells and identified that the cholesterol content is dramatically reduced. Cholesterol 128-139 caveolin 1 Homo sapiens 84-89 23067370-8 2012 CONCLUSIONS: These observations suggest that the interplay of Cav-1 with Nef and cholesterol subsequently counters Nef induced impairment of cholesterol efflux by apoA-l. Cholesterol 141-152 caveolin 1 Homo sapiens 62-67 23067370-9 2012 The findings provide a cellular mechanism by which Cav-1 has an ability to restore HIV mediated impairment of cholesterol efflux in macrophages. Cholesterol 110-121 caveolin 1 Homo sapiens 51-56 21801290-4 2011 In this context, we recently showed that CAV1 regulates the poorly understood process controlling mitochondrial cholesterol levels. Cholesterol 112-123 caveolin 1 Homo sapiens 41-45 22474125-2 2012 Caveolin-1 (Cav1), a scaffold protein of membrane caveolae, is transcriptionally regulated by cholesterol via sterol-responsive element-binding protein-1 (SREBP1). Cholesterol 94-105 caveolin 1 Homo sapiens 0-10 22474125-2 2012 Caveolin-1 (Cav1), a scaffold protein of membrane caveolae, is transcriptionally regulated by cholesterol via sterol-responsive element-binding protein-1 (SREBP1). Cholesterol 94-105 caveolin 1 Homo sapiens 12-16 22238363-6 2012 Several studies suggest that caveolin-1 is involved in cholesterol transport within the cell. Cholesterol 55-66 caveolin 1 Homo sapiens 29-39 22238363-7 2012 Strikingly, we find that blocking cholesterol export from lysosomes with progesterone or U18666A or treating cells with low concentrations of cyclodextrin also caused caveolin-1 to accumulate on late endosome/lysosomal membranes. Cholesterol 34-45 caveolin 1 Homo sapiens 167-177 22238363-10 2012 We conclude that caveolin-1 normally traffics to and from the cytoplasmic surface of lysosomes during intracellular cholesterol trafficking. Cholesterol 116-127 caveolin 1 Homo sapiens 17-27 22411316-3 2012 Caveolin-1 also has lipid binding properties and mediates aspects of cholesterol and fatty acid metabolism and can elicit biological responses in a paracrine manner when secreted. Cholesterol 69-80 caveolin 1 Homo sapiens 0-10 21958667-1 2012 Caveolin-1 has a segment of hydrophobic amino acids comprising approximately residues 103-122 that are anchored to the membrane with cholesterol-rich domains. Cholesterol 133-144 caveolin 1 Homo sapiens 0-10 21724437-6 2011 In addition, the BK(Ca) K(+) channel, which co-migrates with caveolin-1 in a membrane fraction enriched with cholesterol, was impaired in SLOS cells as reflected by reduced single channel conductance and a 50 mV rightward shift in the channel activation voltage. Cholesterol 109-120 caveolin 1 Homo sapiens 61-71 21801290-6 2011 In this article, we suggest a working hypothesis that addresses the role of CAV1 within the homeostatic network that regulates the influx/efflux of mitochondrial cholesterol. Cholesterol 162-173 caveolin 1 Homo sapiens 76-80 21951852-0 2011 Interaction abolishment between mutant caveolin-1(Delta62-100) and ABCA1 reduces HDL-mediated cellular cholesterol efflux. Cholesterol 103-114 caveolin 1 Homo sapiens 57-61 21951852-1 2011 Our previous study shows that caveolin-1 colocalizes and interacts with ATP-binding cassette transporter A1 (ABCA1), which is intimately involved in cellular cholesterol efflux. Cholesterol 158-169 caveolin 1 Homo sapiens 30-40 21951852-3 2011 We also examined the interaction between mutant caveolin-1 and ABCA1 in HDL-mediated cholesterol efflux. Cholesterol 85-96 caveolin 1 Homo sapiens 48-58 21951852-7 2011 Concomitantly, caveolin-1(Delta62-100) suppressed HDL-mediated cholesterol efflux. Cholesterol 63-74 caveolin 1 Homo sapiens 33-37 21951852-8 2011 The results suggest that the region of caveolin-1 between amino acids 62 and 100 is an oligomerization domain as well as an attachment site for ABCA1 interaction that regulates HDL-mediated cholesterol efflux. Cholesterol 190-201 caveolin 1 Homo sapiens 39-49 22010198-4 2011 The localized ATP release occurred at caveolin-1-rich regions of the cell membrane, and was blocked by caveolin-1 knockdown with siRNA and the depletion of plasma membrane cholesterol with methyl-beta-cyclodexrin, indicating involvement of caveolae in localized ATP release. Cholesterol 172-183 caveolin 1 Homo sapiens 38-48 22336460-7 2011 Western blot result confirmed that cholesterol depletion or CAV-1 siRNA significantly decreased CAV-1 protein expression (-18.6% or -41.2% vs. 10(-8) mol/L E2-BSA alone). Cholesterol 35-46 caveolin 1 Homo sapiens 96-101 21747233-8 2011 In the case of TRPC1-SOC channels, it appears that specific lipid domains, lipid raft domains (LRDs), in the plasma membrane, as well as cholesterol-binding scaffolding proteins such as caveolin-1 (Cav-1), are involved in assembly of the TRPC channel complexes. Cholesterol 137-148 caveolin 1 Homo sapiens 186-196 21753190-1 2011 Caveolae, a class of cholesterol-rich lipid rafts, are smooth invaginations of the plasma membrane whose formation in nonmuscle cells requires caveolin-1 (Cav1). Cholesterol 21-32 caveolin 1 Homo sapiens 143-153 21753190-1 2011 Caveolae, a class of cholesterol-rich lipid rafts, are smooth invaginations of the plasma membrane whose formation in nonmuscle cells requires caveolin-1 (Cav1). Cholesterol 21-32 caveolin 1 Homo sapiens 155-159 21747233-8 2011 In the case of TRPC1-SOC channels, it appears that specific lipid domains, lipid raft domains (LRDs), in the plasma membrane, as well as cholesterol-binding scaffolding proteins such as caveolin-1 (Cav-1), are involved in assembly of the TRPC channel complexes. Cholesterol 137-148 caveolin 1 Homo sapiens 198-203 21631282-1 2011 Caveolin-1 (CAV-1) is a key structural component of caveolae that regulates cholesterol. Cholesterol 76-87 caveolin 1 Homo sapiens 0-10 21631282-1 2011 Caveolin-1 (CAV-1) is a key structural component of caveolae that regulates cholesterol. Cholesterol 76-87 caveolin 1 Homo sapiens 12-17 21631282-2 2011 Employing transgenic techniques to regulate the cholesterol content of pork through CAV-1 is hindered by our lack of knowledge about its regulation. Cholesterol 48-59 caveolin 1 Homo sapiens 84-89 21631282-6 2011 The purpose of this study is to systematically elucidate the transcriptional regulation mechanism of porcine CAV-1 and to contribute to the investigation of the interaction between CAV-1 and cholesterol. Cholesterol 191-202 caveolin 1 Homo sapiens 181-186 20835267-9 2010 In brief, the caveolin-1 system transports cholesterol from intracellular compartments to caveolae. Cholesterol 43-54 caveolin 1 Homo sapiens 14-24 20977883-1 2010 Caveolin-1, a main structural protein constituent of caveolae, plays an important role in the signal transduction, endocytosis, and cholesterol transport. Cholesterol 132-143 caveolin 1 Homo sapiens 0-10 20798376-5 2010 In human aortic ECs, free cholesterol loading promoted the interaction of Cav-1 with eNOS, reducing eNOS activity. Cholesterol 26-37 caveolin 1 Homo sapiens 74-79 20663016-5 2010 These findings correlated with high levels of caveolin-1 and glycosphingolipid GM1, two well-defined markers of cholesterol-enriched domains, at the cell surface. Cholesterol 112-123 caveolin 1 Homo sapiens 46-56 20466611-0 2010 Cholesterol and phytosterols differentially regulate the expression of caveolin 1 and a downstream prostate cell growth-suppressor gene. Cholesterol 0-11 caveolin 1 Homo sapiens 71-81 20944122-0 2010 Caveolin-1 and doxorubicin-induced P-glycoprotein modulate plasma cholesterol membrane accessibility in erythrolymphoblastic cell line. Cholesterol 66-77 caveolin 1 Homo sapiens 0-10 20944122-2 2010 We tested the assumption that anthracycline-induced P-gp and Caveolin-1 have correlated effects on cholesterol distribution in plasma membrane. Cholesterol 99-110 caveolin 1 Homo sapiens 61-71 20466611-1 2010 BACKGROUND: The purpose of our study was to show the distinction between the apoptotic and anti-proliferative signaling of phytosterols and cholesterol-enrichment in prostate cancer cell lines, mediated by the differential transcription of caveolin-1, and N-myc downstream-regulated gene 1 (NDRG1), a pro-apoptotic androgen-regulated tumor suppressor. Cholesterol 140-151 caveolin 1 Homo sapiens 240-250 20466611-9 2010 We demonstrated for the first time that cholesterols concertedly attenuated the expression of caveolin-1 (cav-1) and NDRG1 genes in both prostate cancer cell lines. Cholesterol 40-52 caveolin 1 Homo sapiens 94-104 20466611-9 2010 We demonstrated for the first time that cholesterols concertedly attenuated the expression of caveolin-1 (cav-1) and NDRG1 genes in both prostate cancer cell lines. Cholesterol 40-52 caveolin 1 Homo sapiens 106-111 20466611-11 2010 CONCLUSIONS: Cholesterol and phytosterol treatment differentially regulated the growth of prostate cancer cells and the expression of p53 and cav-1, a gene that regulates androgen-regulated signals. Cholesterol 13-24 caveolin 1 Homo sapiens 142-147 20382259-10 2010 Knockdown of Cav-1 reduced the synergistic effects of cholesterol and inflammation. Cholesterol 54-65 caveolin 1 Homo sapiens 13-18 20382259-12 2010 Cav-1 negatively regulates monocyte adhesion by the co-localization of CAMs in caveolae, which is disturbed by cholesterol. Cholesterol 111-122 caveolin 1 Homo sapiens 0-5 19175685-5 2009 This was achieved through multiple approaches including manipulation of the levels of cholesterol and other lipids at the plasma membrane, alteration of cholesterol trafficking by acting on caveolin 1 expression and phosphorylation. Cholesterol 153-164 caveolin 1 Homo sapiens 190-200 19770838-5 2009 HAART 3-plex significantly reduced the intracellular cholesterol transport molecule caveolin-1, whereas it increased superoxide anion production in THP-1 foam cells as compared with controls. Cholesterol 53-64 caveolin 1 Homo sapiens 84-94 19770838-8 2009 Therefore, HAART drugs significantly inhibit cholesterol efflux from human macrophage-derived foam cells through downregulation of caveolin-1 and increase of oxidative stress. Cholesterol 45-56 caveolin 1 Homo sapiens 131-141 19438814-3 2009 Endocytic uptake of the lipid vesicles was cholesterol dependent in all cell lines tested, including the caveolin-1-deficient human hepatoma 7 cell line. Cholesterol 43-54 caveolin 1 Homo sapiens 105-115 19175685-7 2009 Furthermore, the inhibition of invadopodia formation and ECM degradation after caveolin 1 knock-down was efficiently reverted by simple provision of cholesterol. Cholesterol 149-160 caveolin 1 Homo sapiens 79-89 19175685-10 2009 Also, caveolin 1 exerts its function in invadopodia formation by regulating cholesterol balance at the plasma membrane. Cholesterol 76-87 caveolin 1 Homo sapiens 6-16 19175685-11 2009 These findings support the connection between cholesterol, cancer and caveolin 1, provide further understanding of the role of cholesterol in cancer progression and suggest a mechanistic framework for the proposed anti-cancer activity of statins, tightly related to their blood cholesterol-lowering properties. Cholesterol 46-57 caveolin 1 Homo sapiens 70-80 18992712-4 2009 ShRNA-mediated caveolin knockdown sensitized TRAIL-induced apoptosis and disruption of caveolae structure by the cholesterol-extracting reagent, methyl-beta-cyclodextrin (MCD), enhanced TRAIL-induced apoptosis. Cholesterol 113-124 caveolin 1 Homo sapiens 15-23 19445898-5 2009 Since cholesterol overloading, which fortifies lipid rafts, prevented an increase in Rh2-induced membrane fluidity, caveolin-1 internalization and apoptosis, lipid rafts appear to be essential for Rh2-induced apoptosis. Cholesterol 6-17 caveolin 1 Homo sapiens 116-126 19321006-5 2009 The increased intra-cellular transport of RES was abolished in cells stably expressing CAVM2 (a cholesterol shuttle domain (143-156AA)-defective CAV1 mutant) or CAVRNAi. Cholesterol 96-107 caveolin 1 Homo sapiens 145-149 18353778-1 2008 Caveolin-1 binds cholesterol and caveola formation involves caveolin-1 oligomerization and cholesterol association. Cholesterol 17-28 caveolin 1 Homo sapiens 0-10 18687808-3 2008 This study demonstrated that cholesterol-rich domains mediate the actions of early upstream signaling molecules such as Src and intracellular Ca(2+) in cells stimulated by Ang II, but not by EGF, and that Cav1 has a scaffolding role in the process of mitogen-activated protein kinase activation. Cholesterol 29-40 caveolin 1 Homo sapiens 205-209 18612310-1 2008 Caveolin-1 (CAV1) and caveolin 2 (CAV2) are the principal structural proteins of caveolae, sphingolipid and cholesterol-rich invaginations of the plasma membrane involved in vesicular trafficking and signal transduction. Cholesterol 108-119 caveolin 1 Homo sapiens 0-10 18612310-1 2008 Caveolin-1 (CAV1) and caveolin 2 (CAV2) are the principal structural proteins of caveolae, sphingolipid and cholesterol-rich invaginations of the plasma membrane involved in vesicular trafficking and signal transduction. Cholesterol 108-119 caveolin 1 Homo sapiens 12-16 18635971-2 2008 Caveolin-1 (Cav-1) is a palmitoylated lipid raft protein that plays a key role in signal transduction and cholesterol transport. Cholesterol 106-117 caveolin 1 Homo sapiens 0-10 18635971-2 2008 Caveolin-1 (Cav-1) is a palmitoylated lipid raft protein that plays a key role in signal transduction and cholesterol transport. Cholesterol 106-117 caveolin 1 Homo sapiens 12-17 18353778-1 2008 Caveolin-1 binds cholesterol and caveola formation involves caveolin-1 oligomerization and cholesterol association. Cholesterol 91-102 caveolin 1 Homo sapiens 0-10 18279660-4 2008 Depletion of plasma membrane cholesterol with MbetaCD relocalized raft-resident marker caveolin-1 as well as SARS-CoV receptor ACE2 to a nonraft environment, but did not significantly change the surface expression of ACE2. Cholesterol 29-40 caveolin 1 Homo sapiens 87-97 19763245-7 2008 Cholesterol is also essential for lipid body formation which serves as storage sites for COX-2, eicosanoids and caveolin-1. Cholesterol 0-11 caveolin 1 Homo sapiens 112-122 18166162-8 2008 One subset of raft is enriched with cholesterol-sphingomyeline-ganglioside-cav-1/Src/EGFR (hereafter, "chol-raft") that is involved in normal cell signaling, and when dysregulated promotes cell transformation and tumor progression; another subset of raft is enriched with ceramide-sphingomyeline-ganglioside-FAS/Ezrin (hereafter, "cer-raft") that generally promotes apoptosis. Cholesterol 36-47 caveolin 1 Homo sapiens 75-80