HCSGD entry for CAV1

1. General information

Official gene symbolCAV1
Entrez ID857
Gene full namecaveolin 1, caveolae protein, 22kDa
Other gene symbolsBSCL3 CGL3 MSTP085 VIP21
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000122Negative regulation of transcription from RNA polymerase II promoterIEA ISSbiological_process
GO:0000139Golgi membraneIDA IEA TAScellular_component
GO:0000165MAPK cascadeIEAbiological_process
GO:0000188Inactivation of MAPK activityIEA ISSbiological_process
GO:0001525AngiogenesisIEAbiological_process
GO:0001570VasculogenesisIEA ISSbiological_process
GO:0001666Response to hypoxiaIEA ISSbiological_process
GO:0001937Negative regulation of endothelial cell proliferationIEA ISSbiological_process
GO:0001960Negative regulation of cytokine-mediated signaling pathwayIEAbiological_process
GO:0002080Acrosomal membraneIEAcellular_component
GO:0002931Response to ischemiaIEAbiological_process
GO:0003057Regulation of the force of heart contraction by chemical signalIEAbiological_process
GO:0005102Receptor bindingIPImolecular_function
GO:0005113Patched bindingNASmolecular_function
GO:0005198Structural molecule activityIDAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005622IntracellularIDAcellular_component
GO:0005768EndosomeIDAcellular_component
GO:0005783Endoplasmic reticulumIDA IEAcellular_component
GO:0005811Lipid particleTAScellular_component
GO:0005886Plasma membraneIDA TAScellular_component
GO:0005887Integral component of plasma membraneIEAcellular_component
GO:0005901CaveolaIDA IEA NAScellular_component
GO:0005929CiliumIEAcellular_component
GO:0005938Cell cortexIEAcellular_component
GO:0006641Triglyceride metabolic processIEA ISSbiological_process
GO:0006816Calcium ion transportIEA ISSbiological_process
GO:0006874Cellular calcium ion homeostasisIEA ISSbiological_process
GO:0006940Regulation of smooth muscle contractionIEA ISSbiological_process
GO:0007519Skeletal muscle tissue developmentIEA ISSbiological_process
GO:0007595LactationIEAbiological_process
GO:0007596Blood coagulationTASbiological_process
GO:0008104Protein localizationIEA ISSbiological_process
GO:0009267Cellular response to starvationIEPbiological_process
GO:0010524Positive regulation of calcium ion transport into cytosolIEA ISSbiological_process
GO:0015485Cholesterol bindingTASmolecular_function
GO:0016032Viral processIEAbiological_process
GO:0016050Vesicle organizationIDAbiological_process
GO:0016323Basolateral plasma membraneIDAcellular_component
GO:0016324Apical plasma membraneIDAcellular_component
GO:0016504Peptidase activator activityIEA ISSmolecular_function
GO:0019217Regulation of fatty acid metabolic processIEA ISSbiological_process
GO:0019899Enzyme bindingIPImolecular_function
GO:0019915Lipid storageIEA ISSbiological_process
GO:0030193Regulation of blood coagulationIMPbiological_process
GO:0030301Cholesterol transportTASbiological_process
GO:0030514Negative regulation of BMP signaling pathwayIDAbiological_process
GO:0030666Endocytic vesicle membraneTAScellular_component
GO:0030857Negative regulation of epithelial cell differentiationIEA ISSbiological_process
GO:0030879Mammary gland developmentISSbiological_process
GO:0031295T cell costimulationIDAbiological_process
GO:0031397Negative regulation of protein ubiquitinationIEA IMPbiological_process
GO:0031410Cytoplasmic vesicleIDAcellular_component
GO:0032091Negative regulation of protein bindingIDAbiological_process
GO:0032507Maintenance of protein location in cellISSbiological_process
GO:0032570Response to progesteroneIDAbiological_process
GO:0032947Protein complex scaffoldTASmolecular_function
GO:0033137Negative regulation of peptidyl-serine phosphorylationIDAbiological_process
GO:0033138Positive regulation of peptidyl-serine phosphorylationIDAbiological_process
GO:0033484Nitric oxide homeostasisIEA ISSbiological_process
GO:0042310VasoconstrictionIEAbiological_process
GO:0042524Negative regulation of tyrosine phosphorylation of Stat5 proteinIEAbiological_process
GO:0042632Cholesterol homeostasisIEA ISS TASbiological_process
GO:0043234Protein complexIEAcellular_component
GO:0043409Negative regulation of MAPK cascadeISSbiological_process
GO:0043627Response to estrogenIDA IEAbiological_process
GO:0044281Small molecule metabolic processTASbiological_process
GO:0045019Negative regulation of nitric oxide biosynthetic processIEA ISSbiological_process
GO:0045121Membrane raftIDAcellular_component
GO:0045907Positive regulation of vasoconstrictionIEA ISSbiological_process
GO:0046209Nitric oxide metabolic processTASbiological_process
GO:0046426Negative regulation of JAK-STAT cascadeISSbiological_process
GO:0048471Perinuclear region of cytoplasmIDA IEA ISScellular_component
GO:0048554Positive regulation of metalloenzyme activityIEA ISSbiological_process
GO:0050900Leukocyte migrationTASbiological_process
GO:0050998Nitric-oxide synthase bindingIPImolecular_function
GO:0050999Regulation of nitric-oxide synthase activityTASbiological_process
GO:0051001Negative regulation of nitric-oxide synthase activityIEAbiological_process
GO:0051260Protein homooligomerizationIEA ISSbiological_process
GO:0051480Cytosolic calcium ion homeostasisIDAbiological_process
GO:0051592Response to calcium ionIEA ISSbiological_process
GO:0051899Membrane depolarizationIEA ISSbiological_process
GO:0052547Regulation of peptidase activityISSbiological_process
GO:0055074Calcium ion homeostasisISSbiological_process
GO:0060056Mammary gland involutionIEA ISSbiological_process
GO:0070836Caveola assemblyIEA IMPbiological_process
GO:0071455Cellular response to hyperoxiaIMPbiological_process
GO:0072584Caveolin-mediated endocytosisIDAbiological_process
GO:0090090Negative regulation of canonical Wnt signaling pathwayIEA ISSbiological_process
GO:0090263Positive regulation of canonical Wnt signaling pathwayIMPbiological_process
GO:0097190Apoptotic signaling pathwayIMPbiological_process
GO:2000286Receptor internalization involved in canonical Wnt signaling pathwayIMPbiological_process
GO:2000811Negative regulation of anoikisIEA IMPbiological_process
GO:2001238Positive regulation of extrinsic apoptotic signaling pathwayIMPbiological_process
GO:2001244Positive regulation of intrinsic apoptotic signaling pathwayIMPbiological_process
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.99064053040.00095401390.99999024730.0581263889

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Down-0.3623720314
GSE13712_SHEARDown-0.0573314717
GSE13712_STATICDown-0.0648293875
GSE19018Down-0.0271316238
GSE19899_A1Down-1.6045127602
GSE19899_A2Down-1.6320745516
PubMed_21979375_A1Down-3.3408967963
PubMed_21979375_A2Down-1.7995712085
GSE35957Down-0.0629060076
GSE36640Up0.2167407925
GSE54402Down-1.0317384466
GSE9593Up0.3473631675
GSE43922Down-1.3236120143
GSE24585Down-0.4006449032
GSE37065Down-0.0840076193
GSE28863_A1Down-0.6292315903
GSE28863_A2Up0.1538849034
GSE28863_A3Down-0.4708010515
GSE28863_A4Down-0.0906964179
GSE48662Down-0.5554758729

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Not regulated by compounds

  • Drugs

Not regulated by drugs

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-103a-3pMIMAT0000101MIRT006428Luciferase reporter assay//MicroarrayFunctional MTI21654750
hsa-miR-34c-5pMIMAT0000686MIRT000752MicroarrayFunctional MTI (Weak)19461653
hsa-miR-34b-5pMIMAT0000685MIRT000753MicroarrayFunctional MTI (Weak)19461653
hsa-miR-124-3pMIMAT0000422MIRT002719MicroarrayFunctional MTI (Weak)15685193
hsa-miR-124-3pMIMAT0000422MIRT002719Proteomics;MicroarrayFunctional MTI (Weak)18668037
hsa-miR-7-5pMIMAT0000252MIRT025929MicroarrayFunctional MTI (Weak)19073608
hsa-miR-26b-5pMIMAT0000083MIRT030024MicroarrayFunctional MTI (Weak)19088304
hsa-miR-199a-5pMIMAT0000231MIRT035548Luciferase reporter assayFunctional MTI23459460
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  • mirRecord
No target information from mirRecord

6. Text-mining results about the gene

Gene occurances in abstracts of cellular senescence-associated articles: 48 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

27048255Background/Aims: We demonstrated the role of caveolin-1 involved in high glucose (HG)-induced glomerular mesangial cells (GMCs) senescence
27048255The expressions of caveolin-1 and P53 proteins were determined by Western blot
27048255The caveolin-1 is involved in HG-induced mesangial cell senescence, and blocking caveolin-1 significantly reduced cell senescence
26696133In addition, the levels of some senescence-associated proteins, such as phosphorylated ERK1/2, caveolin-1, p53, p16(ink4a), and p21(waf1), were elevated in PPKO-treated cells
26687460Although sham-injected IVDs showed increased CAV1 expression compared with noninjected IVDs, which may indicate increased cell senescence, these findings were not supported by immunohistochemistry, biomolecular analysis of genes related to apoptosis, biochemical and histopathological results
25815136Extracellular matrices may interact with caveolin-1, the lipid raft on cell membrane to regulate quiescence
25799323Oxidative stress induces caveolin 1 degradation and impairs caveolae functions in skeletal muscle cells
25799323Caveolin 1 is the major component of caveolae, small membrane invaginations involved in signaling and endocytic trafficking
25799323The expression level of caveolin 1 was significantly decreased as early as 10 min after 500 muM H2O2 treatment
25799323This reduction was not observed in the presence of a proteasome inhibitor, suggesting that caveolin 1 was rapidly degraded by the proteasome
25799323In spite of caveolin 1 decrease, caveolae were still able to assemble at the plasma membrane
25799323Altogether, our results indicate that H2O2 decreased caveolin 1 expression and impaired caveolae functions
25565110HF-Cas-fed rats had increased caveolin-1 and down-regulated Sirt1 leading to activations of PPARgamma and p53/p21; whereas, rats fed HF-SPI suppressed caveolin-1and activated Sirt1 to de-acetylate PPARgamma and p53 in bone
25512378Oxidative stress-induced inhibition of Sirt1 by caveolin-1 promotes p53-dependent premature senescence and stimulates the secretion of interleukin 6 (IL-6)
25512378We found that caveolin-1, a structural protein component of caveolar membranes, is a direct binding partner of Sirt1, as shown by the binding of the scaffolding domain of caveolin-1 (amino acids 82-101) to the caveolin-binding domain of Sirt1 (amino acids 310-317)
25512378Our data show that oxidative stress promotes the sequestration of Sirt1 into caveolar membranes and the interaction of Sirt1 with caveolin-1, which lead to inhibition of Sirt1 activity
25512378Reactive oxygen species stimulation promotes acetylation of p53 and premature senescence in wild-type but not caveolin-1 null mouse embryonic fibroblasts (MEFs)
25512378Either down-regulation of Sirt1 expression or re-expression of caveolin-1 in caveolin-1 null MEFs restores reactive oxygen species-induced acetylation of p53 and premature senescence
25512378In addition, overexpression of caveolin-1 induces stress induced premature senescence in p53 wild-type but not p53 knockout MEFs
25512378Phosphorylation of caveolin-1 on tyrosine 14 promotes the sequestration of Sirt1 into caveolar membranes and activates p53/senescence signaling
25512378Therefore, by inhibiting Sirt1, caveolin-1 links free radicals to the activation of the p53/senescence pathway and the protumorigenic properties of IL-6
25490147HF-Cas-fed rats had increased caveolin-1 and down-regulated Sirt1, leading to activations of peroxisome proliferator-activated receptor gamma (PPARgamma) and p53/p21, whereas rats fed HF-SPI suppressed caveolin-1 and activated Sirt1 to deacetylate PPARgamma and p53 in bone
25407919In confirmation, EC isolated from the aortas of CAV-1(-/-) mice failed to induce this anti-inflammatory senescent cell population upon expression of ARHGAP18, whereas EC from wild-type mice showed a significant increase
25002533In this study, we show that KSR1 interacts with caveolin-1 and is responsible for MEK and ERK redistribution to caveolin-1-rich fractions
25002533The interaction between KSR1 and caveolin-1 is essential for optimal activation of ERK as a KSR1 mutant unable to interact with caveolin-1 does not efficiently mediate growth factor-induced ERK activation at the early stages of pathway activation
25002533These data show that caveolin-1 is necessary for optimal KSR1-dependent ERK activation by growth factors and oncogenic Ras
24742020Role of caveolin-1 in asthma and chronic inflammatory respiratory diseases
24742020Caveolin-1 (Cav-1) is the major protein present in invaginations of the plasma membrane of cells known as caveolae
24742020Cav-1 is expressed in numerous resident and inflammatory cells implicated in the pathogenesis of asthma and chronic inflammatory respiratory diseases including chronic obstructive pulmonary disease
24742020A remarkable repertoire of functions has been identified for Cav-1 and these extend to, and have relevance to, asthma and chronic inflammatory respiratory diseases
24742020Important processes influenced by Cav-1 include inflammation, fibrosis, smooth muscle contractility, regulation of apoptosis and cell senescence as well as epithelial barrier function and homeostasis
24742020A better understanding of Cav-1 may be useful in developing new therapies for chronic inflammatory respiratory diseases
24719353Soy protein isolate down-regulates caveolin-1 expression to suppress osteoblastic cell senescence pathways
24719353In cell culture studies, membranous caveolin-1 and nuclear p53 expression was greater in replicative senescent ST2 cell cultures than in earlier passaged cells
24719353SPI-fed rat serum significantly down-regulated both caveolin-1 and p53 in senescent and nonsenescent cells
24719353Replicative senescent ST2 cells exhibited a strong association among caveolin-1, p53, and mouse double minute 2 homologue (mdm2), which was inhibited by SPI-fed rat serum
24719353Overexpression of caveolin-1 in ST2 cells resulted in increased expression of p53 and p21, whereas, knockdown of caveolin-1 using shRNA led to increases in mdm2 and eliminated SPI-fed rat serum's effects on p53 and p21 expression
24719353In contrast, manipulation of caveolin-1 expression did not affect the actions of E2 or isoflavones on p53 expression in either ST2 or OB6 cells
24719353These results suggest that caveolin-1 is a mediator of nonestrogenic SPI effects on bone cells
24719353Soy protein isolate down-regulates caveolin-1 expression to suppress osteoblastic cell senescence pathways
24024133HDFs that undergo replicative senescence display typical morphological features, express senescence-associated beta-galactosidase, and increased levels of the tumor suppressor genes, p16, p21, and caveolin-1
23941874Mechanistically, we found that diabetes-induced oxidative stress upregulated caveolin-1 (Cav-1) and PTRF expression, which in turn sequestered Mdm2 away from p53
23941874Intriguingly, we confirmed that the targeted depletion of Cav-1 or PTRF using siRNA- or Vivo-Morpholino antisense-based gene therapy markedly inhibited diabetes/oxidative stress-induced premature senescence and also accelerated tissue repair in this disease state
23899671The less-often-traveled surface of stem cells: caveolin-1 and caveolae in stem cells, tissue repair and regeneration
23899671These activities are of relevance to stem cell biology, and in this review evidence for caveolin-1 involvement in stem cell biology is summarized
23899671Altered stem and progenitor cell populations in caveolin-1 null mice suggest that caveolin-1 can regulate stem cell proliferation, and in vitro studies with isolated stem cells suggest that caveolin-1 regulates stem cell differentiation
23899671The available evidence leads us to hypothesize that caveolin-1 expression may stabilize the differentiated and undifferentiated stem cell phenotype, and transient downregulation of caveolin-1 expression may be required for transition between the two
23899671We also review here the temporal changes in caveolin-1 expression reported during tissue repair
23899671Delayed muscle regeneration in transgenic mice overexpressing caveolin-1 as well as compromised cardiac, brain and liver tissue repair and delayed wound healing in caveolin-1 null mice suggest that caveolin-1 plays an important role in tissue repair, but that this role may be negative or positive depending on the tissue type and the nature of the repair process
23899671Finally, we also discuss how caveolin-1 quiescence-inducing activities and effects on mitochondrial antioxidant levels may influence stem cell aging
23637463Finally, we show that overexpression of caveolin-1 in colon cancer cells inhibits oxidant-induced activation of Nrf2-dependent signaling, promotes premature senescence, and inhibits their transformed phenotype
23637463Thus, by inhibiting Nrf2-mediated signaling, caveolin-1 links free radicals to the activation of the p53/senescence pathway
22362388Idiopathic pulmonary fibrosis is associated with a decreased expression of caveolin-1 (cav-1), yet its role remains unclear
22129993Finally, TFAM-deficient fibroblasts also showed a loss of caveolin-1 (Cav-1), a known breast cancer stromal biomarker
22129993Loss of stromal fibroblast Cav-1 is associated with early tumor recurrence, metastasis, and treatment failure, resulting in poor clinical outcome in breast cancer patients
22100852Recently, great progress has been made toward understanding of the role of caveolin-1 in stress-induced premature senescence
22100852In this review, we discuss the cellular mechanisms and functions of caveolin-1 in the context of SIPS and their relevance to the biology of aging
22037549Caveolin-1 inhibiting miR-133a was reduced and caveolin-1, a negative regulator of eNOS activity, was elevated in senescent HAEC
21445100Our data suggest that the role of PTRF in cellular senescence is dependent on its targeting to caveolae and its interaction with caveolin-1, which appeared to be regulated by the phosphorylation of PTRF
20937408Bleomycin treatment of A549 human lung cancer cells results in association of MGr1-Ag and caveolin-1 in lipid rafts
20937408We have previously shown that upregulation of caveolin-1, the main structural component of caveolae, plays a key role in this process
20937408We show that MGr1-Ag becomes partly localised in lipid rafts following bleomycin treatment, and that MGr1-Ag and caveolin-1 occur in a common protein complex in vivo using co-immunoprecipitation studies
20937408Our results reveal MGr1-Ag as a novel lipid raft protein; its increased association with caveolin-1 in bleomycin-induced cell cycle arrest and subsequent cellular senescence might contribute to the success of chemotherapy
20374325We aimed to ascertain whether angiogenic growth factors (AGFs) can inhibit interleukin (IL)-1beta-induced senescence in human chondrocytes by downregulation of caveolin-1
20374325After 72-h incubation, we observed the expression of caveolin-1 in human chondrocytes by immunohistochemistry, and analysed the protein levels of caveolin-1 by Western blot
20374325RESULTS: Treatment with AGFs inhibited IL-1beta-induced overexpression of caveolin-1 in human OA chondrocytes
20374325Treatment with AGFs all down-regulated protein levels of IL-1beta-accelerated expression of caveolin-1 in chondrocytes
20374325The specific inhibitors for MAPK/extracellular signal-regulated kinase and PI3-K cancelled the AGF-induced downregulation of overexpression of caveolin-1
20362703Here, we demonstrate that FGFR3 signaling is also capable of inducing premature senescence in chondrocytes, manifested as reversible, ERK-dependent growth arrest accompanied by alteration of cellular shape, loss of the extracellular matrix, upregulation of senescence markers (alpha-GLUCOSIDASE, FIBRONECTIN, CAVEOLIN 1, LAMIN A, SM22alpha and TIMP 1), and induction of senescence-associated beta-GALACTOSIDASE activity
20187241A potential clue to the vulnerability of these neurons is an increasing reliance with age upon L-type Ca(2+) channels with a pore-forming Cav1
20157570Recently, we reported that the development of cigarette smoking-induced pulmonary emphysema was inhibited in caveolin-1 null mice, which do not express caveolin-1
20157570We demonstrated that lack of caveolin-1 expression in lung fibroblasts dramatically inhibited premature senescence induced by oxidants contained in cigarette smoke
20157570Mechanistically, we uncovered that premature senescence of lung fibroblasts induced by oxidative stress occurred through activation of an ataxia telangiectasia-mutated (ATM)/p53-depedent pathway following sequestration of the catalytic subunit of protein phosphatase 2A (PP2A-C), an inhibitor of ATM, by caveolin-1 into caveolar membranes
20157570We propose caveolin-1 as a key player of a novel signaling pathway that links cigarette smoke to premature senescence of lung fibroblasts and development of pulmonary emphysema
20137501Consistent with these findings, caveolin-1 expression, caveolin-1/eNOS interaction and ADMA accumulation were also decreased
20096033Salmonella invasion increased in nonphagocytotic senescent host cells in which caveolin-1 was also increased
20096033When caveolae structures were disrupted by methyl-beta-cyclodextrin or siRNA of caveolin-1 in the senescent cells, Salmonellae invasion was reduced markedly compared to that in nonsenescent cells
20096033In contrast, the over-expression of caveolin-1 led to increased Salmonellae invasion in nonsenescent cells
20096033Moreover, in aged mice, caveolin-1 was found to be highly expressed in Peyer's patch and spleen, which are targets for infection by Salmonellae
20096033These results suggest that high levels of caveolae and caveolin-1 in senescent host cells might be related to the increased susceptibility of elderly individuals to microbial infections
20072934Mapping of oxidative stress response elements of the caveolin-1 promoter
20072934We have shown that oxidative stress induces cellular senescence through activation of the caveolin-1 promoter and upregulation of caveolin-1 protein expression
20072934Here, we describe how reactive oxygen species activate the caveolin-1 promoter and how the signaling may be assayed
20072934These approaches provide insight into the functional role of caveolin-1 and potentially allow the identification of novel ROS-regulated genes that are part of the signaling machinery regulating cellular senescence/aging
19820694Inhibition of thioredoxin reductase 1 by caveolin 1 promotes stress-induced premature senescence
19820694We show that caveolin 1, the structural protein component of caveolae, is a TrxR1-binding protein by demonstrating that the scaffolding domain of caveolin 1 (amino acids 82-101) binds directly to the caveolin-binding motif (CBM) of TrxR1 (amino acids 454-463)
19820694We also show that overexpression of caveolin 1 inhibits TrxR activity, whereas a lack of caveolin 1 activates TrxR, both in vitro and in vivo
19820694A TrxR1 mutant lacking the CBM, which fails to localize to caveolae and bind to caveolin 1, is constitutively active and inhibits oxidative-stress-mediated activation of the p53/p21(Waf1/Cip1) pathway and induction of premature senescence
19820694Finally, we show that caveolin 1 expression inhibits TrxR1-mediated cell transformation
19820694Thus, caveolin 1 links free radicals to activation of the p53/p21(Waf1/Cip1) pathway and induction of cellular senescence by acting as an endogenous inhibitor of TrxR1
19626662To understand the mechanism underlying the senescence, we investigated the activity of phosphatidylcholine-specific phospholipase C (PC-PLC) and levels of integrin beta4, caveolin-1 and ROS with BMSC senescence
19626662The activity of PC-PLC and levels of integrin beta4, caveolin-1 and ROS increased greatly during cell senescence
19626662Moreover, D609 suppressed the elevated levels of integrin beta4, caveolin-1 and ROS
19626662The data suggest that PC-PLC is involved in senescence of BMSCs, and its function is associated with integrin beta4, caveolin-1 and ROS
19318577We show that caveolin-1 is a novel binding protein for Mdm2
19318577We also show that reintroduction of caveolin-1 in oncogenic Ras (Ras(G12V))-transformed fibroblasts, which express residual levels of caveolin-1, is sufficient to promote cellular senescence
19318577Moreover, caveolin-1 expression in MEFs is required for senescent fibroblast-induced stimulation of cell growth and tumorigenesis of both Ras(G12V)-transformed fibroblasts and MDA-MB-231 breast cancer epithelial cells both in vitro and in vivo
19318577Thus, our results propose caveolin-1 as a key mediator of the antagonistic pleiotropic properties of cellular senescence
19011671EC exhibited higher expression levels of markers of oxidative stress (lipid peroxydation level and caveolin-1 mRNA), inflammation (angiopoietin-like 2 mRNA), hypoxia (vascular endothelial growth factor (VEGF)-A mRNA), and cell damage (p53 mRNA)
18848576We instead found that selective COX-2 inhibitors regulate caveolin-1 expression at transcriptional levels, which was closely associated with the inhibitors' effect on the senescence
18681962We hypothesised that stress-induced premature senescence (SIPS) occurs within the IVD and here we have investigated the expression and production of caveolin-1, a protein that has been shown previously to be upregulated in SIPS
18681962METHODS: Caveolin-1 gene expression in human nucleus pulposus (NP) cells was assessed by conventional and quantitative real-time polymerase chain reaction (PCR), and caveolin-1 protein expression was examined within human IVDs using immunohistochemistry
18681962The correlation between caveolin-1 and p16INK4a (biomarker of cellular senescence) gene expression was investigated using quantitative real-time PCR
18681962NP cells from degenerate discs exhibited elevated levels of caveolin-1 which did not relate to increasing chronological age
18681962A negative correlation was observed between gene expression for caveolin-1 and donor age, and no correlation was found between caveolin-1 protein expression and age
18681962A positive correlation was identified between gene expression of caveolin-1 and p16INK4a
18681962CONCLUSION: Our findings are consistent with a role for caveolin-1 in degenerative rather than age-induced changes in the NP
18681962Its expression in IVD tissue and its association with the senescent phenotype suggest that caveolin-1 and SIPS may play a prominent role in the pathogenesis of IVD degeneration
18385095Expression of the senescence-associated transmembrane protein caveolin-1 was investigated by Northern and Western blot analyses
18385095Quercetin caused a significant dose-dependent reduction of caveolin-1 mRNA 48 hours after treatment with hydrogen peroxide
18385095After 96 hours of incubation, caveolin-1 protein levels were also reduced
18385095The authors suggest that this increase in antioxidative capacity is--among other mechanisms, such as the intracellular redox state--also mediated by inhibiting the upregulation of caveolin-1
17662641Downregulation of caveolin-1 affects bleomycin-induced growth arrest and cellular senescence in A549 cells
17662641Bleomycin is an anti-cancer drug that induces both apoptosis and senescence, two processes thought to involve caveolin-1
17662641Here we investigate the role of caveolin-1 in bleomycin-induced senescence
17662641As predicted, we find that caveolin-1 amount increases in response to bleomycin-treatment and that modulation of caveolin-1 affects p21 and p53 levels, cell cycling, and senescence (SA-beta-galactosidase activity)
17662641Interestingly, senescence-associated cell cycle arrest via p53 and p21 and SA-beta-galactosidase activity is reduced in young A549 cells when short hairpin RNA specific for caveolin-1 was applied before bleomycin-treatment
17662641Our results support the hypothesis that downregulation of caveolin-1 expression affects bleomycin-induced cell cycle arrest and subsequent cellular senescence that is driven by p53 and p21
17108117We have previously shown that up-regulation of caveolin-1 was required for oxidative stress-induced premature senescence in fibroblasts
17108117However, the molecular mechanisms underlying caveolin-1 up-regulation in senescent cells remain unknown
17108117Here, we show that subcytotoxic oxidative stress generated by hydrogen peroxide application promotes premature senescence and stimulates the activity of a (-1,296) caveolin-1 promoter reporter gene construct in fibroblasts
17108117Functional deletion analysis mapped the oxidative stress response elements of the mouse caveolin-1 promoter to the sequences -244/-222 and -124/-101
17108117The hydrogen peroxide-mediated activation of both Cav-1 (-244/-222) and Cav-1 (-124/-101) was prevented by the antioxidant quercetin
17108117Finally, we show that oxidative stress induces p38-mediated up-regulation of caveolin-1 and premature senescence in normal human mammary epithelial cells but not in MCF-7 breast cancer cells, which do not express caveolin-1 and undergo apoptosis
17108117This study delineates for the first time the molecular mechanisms that modulate caveolin-1 gene transcription upon oxidative stress and brings new insights into the redox control of cellular senescence in both normal and cancer cells
16523241Interestingly dephosphorylation at Tyr577 of FAK by PP2 treatment, Src-family kinase inhibitor, induced the apoptosis by staurosporine in senescent cells but dephosphorylation at Tyr397 by downregulation of caveolin-1 was not affected
16508959Catabolic stress induces features of chondrocyte senescence through overexpression of caveolin 1: possible involvement of caveolin 1-induced down-regulation of articular chondrocytes in the pathogenesis of osteoarthritis
16508959Recently, it was suggested that caveolin 1, a 21-24-kd membrane protein, participates in premature cellular senescence
16508959Caveolin 1 is the principal structural component of caveolae, vesicular invaginations of the plasma membrane
16508959This study was undertaken to investigate whether the catabolic factors oxidative stress and interleukin-1beta (IL-1beta) induce features of premature senescence of articular chondrocytes through up-regulation of caveolin 1 expression
16508959METHODS: Caveolin 1 expression was investigated in human OA cartilage by real-time polymerase chain reaction and in rat OA cartilage by immunohistologic analysis
16508959We studied whether IL-1beta and H2O2 induce caveolin 1 expression in OA chondrocytes and analyzed the relationship between cellular senescent phenotypes and caveolin 1 expression in human chondrocytes
16508959RESULTS: In human and rat OA articular cartilage, caveolin 1 positivity was associated with cartilage degeneration
16508959Both IL-1beta and H2O2 up-regulated caveolin 1 messenger RNA and protein levels, and both treatments induced marked expression of senescent phenotypes: altered cellular morphology, cell growth arrest, telomere erosion, and specific senescence-associated beta-galactosidase activity
16508959In contrast, down-regulation of caveolin 1 with antisense oligonucleotide significantly inhibited the features of chondrocyte senescence induced by catabolic factors
16508959CONCLUSION: Our findings suggest that IL-1beta and oxidative stress induce features of premature senescence in OA chondrocytes, mediated, at least in part, by stress-induced caveolin 1 expression
16508959This indicates that caveolin 1 plays a role in the pathogenesis of OA via promotion of chondrocyte down-regulation
15811424Increased caveolin-1, a cause for the declined adipogenic potential of senescent human mesenchymal stem cells
15811424In senescent hMSCs, we also found a significant increase of caveolin-1 expression, previously reported as a cause for the attenuated response to growth factors in senescent HDFs
15811424When we overexpressed caveolin-1 in young hMSC, not only insulin signaling but also adipogenic differentiation was significantly suppressed with down-regulated PPARgamma2
15811424These data indicate that loss of adipogenic differentiation potential in senescent hMSC is mediated by the over-expression of caveolin-1
15610768The level of caveolin-1 is strictly regulated to maintain cellular integrity, leading to cellular transformation if depleted, and to the senescent phenotype if overexpressed
15610768In case of senescent cells, the functional and physiological responses to the mitogenic stimuli can be restored and the morphological shape can be resumed by simple adjustment of caveolin-1 status
15610768Therefore, it is suggested that prime modulator molecules, represented by caveolin-1, play a key role in determining the senescent phenotype, either as a physiological response or altered morphology
15263006Morphological adjustment of senescent cells by modulating caveolin-1 status
15263006These determinants included integrins, focal adhesion complexes, and small Rho GTPases, and special emphasis was placed on their relationships with caveolin-1 status
15263006Activated Rac1 and Cdc42 directly interacted with caveolin-1 in senescent cells
15263006Interestingly, caveolin-1 knock-out senescent cells, achieved by using small interfering RNA and antisense oligonucleotide, showed disrupted focal adhesion formation and actin stress fibers via the inactivation of FAK, which resulted in morphological adjustment to the young cell-like small spindle shape
15263006Based on the results obtained, we propose that caveolin-1 plays an important role in senescence-associated morphological changes by regulating focal adhesion kinase activity and actin stress fiber formation in the senescent cells
12730243We reduced the level of caveolin-1 in senescent human diploid fibroblasts using its antisense oligonucleotides and small interfering RNA, and this resulted in the restoration of normal growth factor responses such as the increased phosphorylation of Erk, the nuclear translocation of p-Erk, and the subsequent activation of p-Elk upon epidermal growth factor stimulation
12730243Taken together, we conclude that the loss of mitogenic signaling in senescent cells is strongly related to their elevated levels of caveolin-1 and that the functional recovery of senescent cells at least in the terms of growth factor responsiveness and cell cycle entry might be achieved simply by lowering the caveolin level
12134086Expression of caveolin-1 induces premature cellular senescence in primary cultures of murine fibroblasts
12134086Several lines of evidence are consistent with the idea that caveolin-1 functions as a "transformation suppressor" protein
12134086In fact, caveolin-1 mRNA and protein expression are lost or reduced during cell transformation by activated oncogenes
12134086Interestingly, the human caveolin-1 gene is localized to a suspected tumor suppressor locus (7q31
12134086We have previously demonstrated that overexpression of caveolin-1 arrests mouse embryonic fibroblasts in the G(0)/G(1) phase of the cell cycle through activation of a p53/p21-dependent pathway, indicating a role of caveolin-1 in mediating growth arrest
12134086Here, we demonstrate that mouse embryonic fibroblasts transgenically overexpressing caveolin-1 show: 1) a reduced proliferative lifespan; 2) senescence-like cell morphology; and 3) a senescence-associated increase in beta-galactosidase activity
12134086These results indicate for the first time that the expression of caveolin-1 in vivo is sufficient to promote and maintain the senescent phenotype
12134086Interestingly, we show that subcytotoxic level of hydrogen peroxide induces premature senescence in NIH 3T3 cells and increases endogenous caveolin-1 expression
12134086Importantly, quercetin and vitamin E, two antioxidant agents, successfully prevent the premature senescent phenotype and the up-regulation of caveolin-1 induced by hydrogen peroxide
12134086Also, we demonstrate that hydrogen peroxide alone, but not in combination with quercetin, stimulates the caveolin-1 promoter activity
12134086Interestingly, premature senescence induced by hydrogen peroxide is greatly reduced in NIH 3T3 cells harboring antisense caveolin-1
12134086Importantly, induction of premature senescence is recovered when caveolin-1 levels are restored
12134086Taken together, these results clearly indicate a central role for caveolin-1 in promoting cellular senescence and they suggest the hypothesis that premature senescence may represent a tumor suppressor function mediated by caveolin-1 in vivo
11976184In those senescent cells, we found an increased level of caveolin proteins and strong interactions between caveolin-1 and EGFR
11976184When we overexpressed caveolin-1 in young HDF, the activation of Erk-1/2 on EGF stimulation was significantly suppressed
11268002Furthermore, old cells had little caveolar protein exposed to the outer plasma membrane as estimated by using an in vivo biotinylation assay and no detectable caveolin 1 on the cell surface when processed for immunofluoresence and confocal microscopy
10781609In those senescent cells, we found an increased level of caveolin proteins and strong interactions between caveolin-1 and EGF receptor
10781609However, in the case of p53-induced senescence, caveolin-1 was not induced, and EGF stimulation phosphorylated Erk-1/2 as much as young control cells
10781609Finally, we overexpressed caveolin-1 in young human diploid fibroblasts in which the activation of Erk-1/2 upon EGF stimulation was significantly suppressed
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