AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation ScienceHealth Care
CaveolinsCaveolin 2Caveolin 3Caveolin 1CaveolaeMembrane MicrodomainsMembrane ProteinsSignal TransductionCell MembraneMice, KnockoutRespiratory TherapyRespiratory Therapy Department, HospitalAdenosineRespiratory Care UnitsCavesReceptor, Adenosine A2ARalstonia pickettiiRhabdomyosarcomaSatellite Cells, Skeletal MuscleReceptors, Dopamine D4Receptors, Dopamine D2Receptors, DopamineGlial Fibrillary Acidic ProteinBrain IschemiaInfarction, Middle Cerebral ArteryIschemic Attack, TransientCerebral InfarctionApoptosisAnnexin A5Cell Line, TumorP-GlycoproteinOvarian NeoplasmsBlotting, WesternNotochordEncyclopedias as TopicMolecular Sequence Data
Caveolins
The main structural proteins of CAVEOLAE. Several distinct genes for caveolins have been identified.
Caveolin 2
Caveolin 2 is a binding partner of CAVEOLIN 1. It undergoes tyrosine phosphorylation by C-SRC PROTEIN PP60 and plays a regulatory role in CAVEOLAE formation.
Caveolin 3
A caveolin that is expressed exclusively in MUSCLE CELLS and is sufficient to form CAVEOLAE in SARCOLEMMA. Mutations in caveolin 3 are associated with multiple muscle diseases including DISTAL MYOPATHY and LIMB-GIRDLE MUSCULAR DYSTROPHY.
Caveolin 1
A tyrosine phosphoprotein that plays an essential role in CAVEOLAE formation. It binds CHOLESTEROL and is involved in LIPIDS transport, membrane traffic, and SIGNAL TRANSDUCTION.
Caveolae
Endocytic/exocytic CELL MEMBRANE STRUCTURES rich in glycosphingolipids, cholesterol, and lipid-anchored membrane proteins that function in ENDOCYTOSIS (potocytosis), transcytosis, and SIGNAL TRANSDUCTION. Caveolae assume various shapes from open pits to closed vesicles. Caveolar coats are composed of CAVEOLINS.
Membrane Microdomains
Detergent-insoluble CELL MEMBRANE components. They are enriched in SPHINGOLIPIDS and CHOLESTEROL and clustered with glycosyl-phosphatidylinositol (GPI)-anchored proteins.
Membrane Proteins
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Signal Transduction
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Cell Membrane
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Mice, Knockout
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Respiratory Therapy
Care of patients with deficiencies and abnormalities associated with the cardiopulmonary system. It includes the therapeutic use of medical gases and their administrative apparatus, environmental control systems, humidification, aerosols, ventilatory support, bronchopulmonary drainage and exercise, respiratory rehabilitation, assistance with cardiopulmonary resuscitation, and maintenance of natural, artificial, and mechanical airways.
Respiratory Therapy Department, Hospital
Hospital department which is responsible for the administration of diagnostic pulmonary function tests and of procedures to restore optimum pulmonary ventilation.
Adenosine
A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter.
Respiratory Care Units
The hospital unit in which patients with respiratory conditions requiring special attention receive intensive medical care and surveillance.
Caves
Geological formations consisting of underground enclosures with access from the surface.
Receptor, Adenosine A2A
A subclass of adenosine A2 receptors found in LEUKOCYTES, the SPLEEN, the THYMUS and a variety of other tissues. It is generally considered to be a receptor for ADENOSINE that couples to the GS, STIMULATORY G-PROTEIN.
Ralstonia pickettii
The type species in the genus RALSTONIA. It is often found in the hospital ward as a contaminant of antiseptic and disinfectant solutions.
Rhabdomyosarcoma
A malignant solid tumor arising from mesenchymal tissues which normally differentiate to form striated muscle. It can occur in a wide variety of sites. It is divided into four distinct types: pleomorphic, predominantly in male adults; alveolar (RHABDOMYOSARCOMA, ALVEOLAR), mainly in adolescents and young adults; embryonal (RHABDOMYOSARCOMA, EMBRYONAL), predominantly in infants and children; and botryoidal, also in young children. It is one of the most frequently occurring soft tissue sarcomas and the most common in children under 15. (From Dorland, 27th ed; Holland et al., Cancer Medicine, 3d ed, p2186; DeVita Jr et al., Cancer: Principles & Practice of Oncology, 3d ed, pp1647-9)
Satellite Cells, Skeletal Muscle
Elongated, spindle-shaped, quiescent myoblasts lying in close contact with adult skeletal muscle. They are thought to play a role in muscle repair and regeneration.
Receptors, Dopamine D4
A subtype of dopamine D2 receptors that has high affinity for the antipsychotic CLOZAPINE.
Receptors, Dopamine D2
A subfamily of G-PROTEIN-COUPLED RECEPTORS that bind the neurotransmitter DOPAMINE and modulate its effects. D2-class receptor genes contain INTRONS, and the receptors inhibit ADENYLYL CYCLASES.
Receptors, Dopamine
Cell-surface proteins that bind dopamine with high affinity and trigger intracellular changes influencing the behavior of cells.
Glial Fibrillary Acidic Protein
An intermediate filament protein found only in glial cells or cells of glial origin. MW 51,000.
Brain Ischemia
Localized reduction of blood flow to brain tissue due to arterial obstruction or systemic hypoperfusion. This frequently occurs in conjunction with brain hypoxia (HYPOXIA, BRAIN). Prolonged ischemia is associated with BRAIN INFARCTION.
Infarction, Middle Cerebral Artery
NECROSIS occurring in the MIDDLE CEREBRAL ARTERY distribution system which brings blood to the entire lateral aspects of each CEREBRAL HEMISPHERE. Clinical signs include impaired cognition; APHASIA; AGRAPHIA; weak and numbness in the face and arms, contralaterally or bilaterally depending on the infarction.
Ischemic Attack, Transient
Brief reversible episodes of focal, nonconvulsive ischemic dysfunction of the brain having a duration of less than 24 hours, and usually less than one hour, caused by transient thrombotic or embolic blood vessel occlusion or stenosis. Events may be classified by arterial distribution, temporal pattern, or etiology (e.g., embolic vs. thrombotic). (From Adams et al., Principles of Neurology, 6th ed, pp814-6)
Cerebral Infarction
The formation of an area of NECROSIS in the CEREBRUM caused by an insufficiency of arterial or venous blood flow. Infarcts of the cerebrum are generally classified by hemisphere (i.e., left vs. right), lobe (e.g., frontal lobe infarction), arterial distribution (e.g., INFARCTION, ANTERIOR CEREBRAL ARTERY), and etiology (e.g., embolic infarction).
Apoptosis
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
Annexin A5
A protein of the annexin family isolated from human PLACENTA and other tissues. It inhibits cytosolic PHOSPHOLIPASE A2, and displays anticoagulant activity.
Cell Line, Tumor
A cell line derived from cultured tumor cells.
P-Glycoprotein
A 170-kDa transmembrane glycoprotein from the superfamily of ATP-BINDING CASSETTE TRANSPORTERS. It serves as an ATP-dependent efflux pump for a variety of chemicals, including many ANTINEOPLASTIC AGENTS. Overexpression of this glycoprotein is associated with multidrug resistance (see DRUG RESISTANCE, MULTIPLE).
Ovarian Neoplasms
Tumors or cancer of the OVARY. These neoplasms can be benign or malignant. They are classified according to the tissue of origin, such as the surface EPITHELIUM, the stromal endocrine cells, and the totipotent GERM CELLS.
Blotting, Western
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Notochord
A cartilaginous rod of mesodermal cells at the dorsal midline of all CHORDATE embryos. In lower vertebrates, notochord is the backbone of support. In the higher vertebrates, notochord is a transient structure, and segments of the vertebral column will develop around it. Notochord is also a source of midline signals that pattern surrounding tissues including the NEURAL TUBE development.
Encyclopedias as Topic
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The dually acylated NH2-terminal domain of gi1alpha is sufficient to target a green fluorescent protein reporter to caveolin-enriched plasma membrane domains. Palmitoylation of caveolin-1 is required for the recognition of dually acylated g-protein alpha subunits in vivo. (1/923)

Here we investigate the molecular mechanisms that govern the targeting of G-protein alpha subunits to the plasma membrane. For this purpose, we used Gi1alpha as a model dually acylated G-protein. We fused full-length Gi1alpha or its extreme NH2-terminal domain (residues 1-32 or 1-122) to green fluorescent protein (GFP) and analyzed the subcellular localization of these fusion proteins. We show that the first 32 amino acids of Gi1alpha are sufficient to target GFP to caveolin-enriched domains of the plasma membrane in vivo, as demonstrated by co-fractionation and co-immunoprecipitation with caveolin-1. Interestingly, when dual acylation of this 32-amino acid domain was blocked by specific point mutations (G2A or C3S), the resulting GFP fusion proteins were localized to the cytoplasm and excluded from caveolin-rich regions. The myristoylated but nonpalmitoylated (C3S) chimera only partially partitioned into caveolin-containing fractions. However, both nonacylated GFP fusions (G2A and C3S) no longer co-immunoprecipitated with caveolin-1. Taken together, these results indicate that lipid modification of the NH2-terminal of Gi1alpha is essential for targeting to its correct destination and interaction with caveolin-1. Also, a caveolin-1 mutant lacking all three palmitoylation sites (C133S, C143S, and C156S) was unable to co-immunoprecipitate these dually acylated GFP-G-protein fusions. Thus, dual acylation of the NH2-terminal domain of Gi1alpha and palmitoylation of caveolin-1 are both required to stabilize and perhaps regulate this reciprocal interaction at the plasma membrane in vivo. Our results provide the first demonstration of a functional role for caveolin-1 palmitoylation in its interaction with signaling molecules.  (+info)

The Npc1 mutation causes an altered expression of caveolin-1, annexin II and protein kinases and phosphorylation of caveolin-1 and annexin II in murine livers. (2/923)

We have previously demonstrated (1) an increased expression of caveolin-1 in murine heterozygous and homozygous Niemann-Pick type C (NPC) livers, and (2) an increased concentration of unesterified cholesterol in a detergent insoluble caveolae-enriched fraction from homozygous livers. To define further the relationship between caveolin-1 function and the cholesterol trafficking defect in NPC, we examined the expression and distribution of additional caveolar and signal transduction proteins. The expression of annexin II was significantly increased in homozygous liver homogenates and the Triton X-100 insoluble floating fraction (TIFF). Phosphoamino acid analysis of caveolin-1 and annexin II from the homozygous TIFF demonstrated an increase in serine and tyrosine phosphorylation, respectively. To determine the basis for increased phosphorylation of these proteins, the expression and distribution of several protein kinases was examined. The expression of PKCalpha, PKCzeta and pp60-src (protein kinases) were significantly increased in both heterozygous and homozygous liver homogenates, while PKCdelta was increased only in homozygous livers. Of the protein kinases analyzed, only CK IIalpha was significantly enriched in the heterozygous TIFF. Finally, the concentration of diacylglycerol in the homozygous TIFF was significantly increased and this elevation may modulate PKC distribution and function. These results provide additional evidence for involvement of a caveolin-1 containing cellular fraction in the pathophysiology of NPC and also suggest that the Npc1 gene product may directly or indirectly, regulate the expression and distribution of signaling molecules.  (+info)

Hypercholesterolemia decreases nitric oxide production by promoting the interaction of caveolin and endothelial nitric oxide synthase. (3/923)

Hypercholesterolemia is a central pathogenic factor of endothelial dysfunction caused in part by an impairment of endothelial nitric oxide (NO) production through mechanisms that remain poorly characterized. The activity of the endothelial isoform of NO synthase (eNOS) was recently shown to be modulated by its reciprocal interactions with the stimulatory Ca2+-calmodulin complex and the inhibitory protein caveolin. We examined whether hypercholesterolemia may reduce NO production through alteration of this regulatory equilibrium. Bovine aortic endothelial cells were cultured in the presence of serum obtained from normocholesterolemic (NC) or hypercholesterolemic (HC) human volunteers. Exposure of endothelial cells to the HC serum upregulated caveolin abundance without any measurable effect on eNOS protein levels. This effect of HC serum was associated with an impairment of basal NO release paralleled by an increase in inhibitory caveolin-eNOS complex formation. Similar treatment with HC serum significantly attenuated the NO production stimulated by the calcium ionophore A23187. Accordingly, higher calmodulin levels were required to disrupt the enhanced caveolin-eNOS heterocomplex from HC serum-treated cells. Finally, cell exposure to the low-density lipoprotein (LDL) fraction alone dose-dependently reproduced the inhibition of basal and stimulated NO release, as well as the upregulation of caveolin expression and its heterocomplex formation with eNOS, which were unaffected by cotreatment with antioxidants. Together, our data establish a new mechanism for the cholesterol-induced impairment of NO production through the modulation of caveolin abundance in endothelial cells, a mechanism that may participate in the pathogenesis of endothelial dysfunction and the proatherogenic effects of hypercholesterolemia.  (+info)

Regulation of G protein-coupled receptor kinases by caveolin. (4/923)

G protein-coupled receptor kinases (GRKs) have been principally characterized by their ability to phosphorylate and desensitize G protein-coupled receptors. However, recent studies suggest that GRKs may have more diverse protein/protein interactions in cells. Based on the identification of a consensus caveolin binding motif within the pleckstrin homology domain of GRK2, we tested the direct binding of purified full-length GRK2 to various glutathione S-transferase-caveolin-1 fusion proteins, and we discovered a specific interaction of GRK2 with the caveolin scaffolding domain. Interestingly, analysis of GRK1 and GRK5, which lack a pleckstrin homology domain, revealed in vitro binding properties similar to those of GRK2. Maltose-binding protein caveolin and glutathione S-transferase-GRK fusion proteins were used to map overlapping regions in the N termini of both GRK2 and GRK5 that appear to mediate conserved GRK/caveolin interactions. In vivo association of GRK2 and caveolin was suggested by co-fractionation of GRK2 with caveolin in A431 and NIH-3T3 cells and was further supported by co-immunoprecipitation of GRK2 and caveolin in COS-1 cells. Functional significance for the GRK/caveolin interaction was demonstrated by the potent inhibition of GRK-mediated phosphorylation of both receptor and peptide substrates by caveolin-1 and -3 scaffolding domain peptides. These data reveal a novel mode for the regulation of GRKs that is likely to play an important role in their cellular function.  (+info)

Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines. (5/923)

We identified CAVEOLIN-1 as a candidate for a tumour suppressor gene mapping to human chromosome 7q31.1. A number of studies suggest that caveolin could function as a tumour suppressor. Expression of caveolin, and in turn the number of caveolae within a cell, are inversely correlated with the transforming ability of numerous oncoproteins, including H-ras, v-abl, and bcr-abl, and caveolin is a major transformation-dependent substrate of v-src. Heterologous expression of caveolin has been shown to abrogate anchorage-independent growth and induce apoptosis in transformed fibroblasts and also to suppress anchorage-independent growth in human mammary carcinoma cells. We have analysed the status and expression of the human CAVEOLIN-1 gene in primary tumours and tumour-derived cell lines. We found no evidence for mutation of CAVEOLIN-1 in human cancers. Additionally, we found that while the first two exons of CAVEOLIN-1 are associated with a CpG island, this is not methylated in either primary tumours or in tumour-derived cell lines in which Caveolin-1 expression is low or undetectable. The level of expression of Caveolin-1 does not correlate with loss of heterozygosity at the CAVEOLIN-1 locus in these same cell lines. Contrary to other published studies, we have shown that CAVEOLIN-1 is not expressed in normal breast ductal epithelial cells in vivo. CAVEOLIN-1 is however highly expressed in breast myoepithelial cells and its expression is retained in tumours derived from breast myoepithelium. Together our data refute a role for CAVEOLIN-1 as a breast tumour suppressor gene in vivo.  (+info)

A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling. (6/923)

The assembly of signaling molecules surrounding the integrin family of adhesion receptors remains poorly understood. Recently, the membrane protein caveolin was found in complexes with beta1 integrins. Caveolin binds cholesterol and several signaling molecules potentially linked to integrin function, e.g., Src family kinases, although caveolin has not been directly implicated in integrin-dependent adhesion. Here we report that depletion of caveolin by antisense methodology in kidney 293 cells disrupts the association of Src kinases with beta1 integrins resulting in loss of focal adhesion sites, ligand-induced focal adhesion kinase (FAK) phosphorylation, and adhesion. The nonintegrin urokinase receptor (uPAR) associates with and stabilizes beta1 integrin/caveolin complexes. Depletion of caveolin in uPAR-expressing 293 cells also disrupts uPAR/integrin complexes and uPAR-dependent adhesion. Further, beta1 integrin/caveolin complexes could be disassociated by uPAR-binding peptides in both uPAR-transfected 293 cells and human vascular smooth muscle cells. Disruption of complexes by peptides in intact smooth muscle cells blocks the association of Src family kinases with beta1 integrins and markedly impairs their migration on fibronectin. We conclude that ligand-induced signaling necessary for normal beta1 integrin function requires caveolin and is regulated by uPAR. Caveolin and uPAR may operate within adhesion sites to organize kinase-rich lipid domains in proximity to integrins, promoting efficient signal transduction.  (+info)

Visualization of caveolin-1, a caveolar marker protein, in living cells using green fluorescent protein (GFP) chimeras. The subcellular distribution of caveolin-1 is modulated by cell-cell contact. (7/923)

Caveolin-1, a suspected tumor suppressor, is a principal protein component of caveolae in vivo. Recently, we have shown that NIH 3T3 cells harboring anti-sense caveolin-1 exhibit a loss of contact inhibition and anchorage-independent growth. These observations may be related to the ability of caveolin-1 expression to positively regulate contact inhibition. In order to understand the postulated role of caveolin-1 in contact inhibition, it will be necessary to follow the distribution of caveolins in living cells in response to a variety of stimuli, such as cell density. Here, we visualize the distribution of caveolin-1 in living normal NIH 3T3 cells by creating GFP-fusion proteins. In many respects, the behavior of these GFP-caveolin-1 fusion proteins is indistinguishable from endogenous caveolin-1. These GFP-caveolin-1 fusion proteins co-fractionated with endogenous caveolin-1 using an established protocol that separates caveolae-derived membranes from the bulk of cellular membranes and cytosolic proteins, and co-localized with endogenous caveolin-2 in vivo as seen by immunofluorescence microscopy. We show here that as NIH 3T3 cells become confluent, the distribution of GFP-caveolin-1 and endogenous caveolin-1 shifts to areas of cell-cell contact, coincident with contact inhibition. However, unlike endogenous caveolin-1, the levels of GFP-caveolin-1 expression are unaffected by changes in cell density, serum starvation, or growth factor stimulation. These results are consistent with the idea that the levels of endogenous caveolin-1 are modulated by either transcriptional or translational control, and that this modulation is separable from density-dependent regulation of the distribution of caveolin-1. These studies provide a new living-model system for elucidating the dynamic mechanisms underlying the density-dependent regulation of the distribution of caveolin-1 and how this relates to contact inhibition.  (+info)

Tyrosine-phosphorylated caveolin-1: immunolocalization and molecular characterization. (8/923)

Caveolin-1 was discovered as a major substrate for v-Src, but the effect of its tyrosine phosphorylation has not been known. We generated a specific antibody (PY14) to caveolin-1 phosphorylated at tyrosine 14 and studied the significance of the modification. By Western blotting of lysates of v-Src-expressing cells, PY14 recognized not only a 22-kDa band (the position of nonphosphorylated caveolin-1) but bands at 23-24 and 25 kDa. Bands of slower mobility were diminished by dephosphorylation and were also observed for mutant caveolin-1 lacking tyrosine 14. By immunofluorescence microscopy, PY14 did not label normal cells but detected large dots in v-Src-expressing cells. Immunoelectron microscopy revealed that the dots corresponded to aggregated caveolae and/or vesicles of various sizes; besides, the label was observed in intramembrane particle-free areas in the plasma membrane, which appeared to have been formed by fusion of flattened caveolae. A positive reaction with PY14 was found in normal cells after vanadate or pervanadate treatment; it occurred mainly at 22 kDa by Western blotting and was not seen as large dots by immunofluorescence microscopy. Detergent solubility, oligomerization, and association with caveolin-2 were observed similarly for caveolin-1 in normal and v-Src-expressing cells. The results indicate that phosphorylation of caveolin-1 in v-Src-expressing cells occurs at multiple residues and induces flattening, aggregation, and fusion of caveolae and/or caveolae-derived vesicles.  (+info)

Caveolins in Cancer Pathogenesis, Prevention and TherapyCaveolins in Cancer Pathogenesis, Prevention and Therapy
www.MOLUNA.de Caveolins in Cancer Pathogenesis, Prevention and Therapy [4196990] - Caveolins play an important role in the pathogenesis of multiple cancers. This volume focuses mainly on the importance of Caveolin-1 in breast, prostate, lung, skin, colon, pancreatic and brain cancers. It also studies the role of Caveolin-3 in breast cancer.Caveolins are important structural proteins of Caveolae, small invaginations of the
https://www.moluna.de/buch/4196990-caveolins+in+cancer+pathogenesis%2C+prevention+and+therapy/
Expression of caveolins in RMS tumours. Double immunost | Open-iExpression of caveolins in RMS tumours. Double immunost | Open-i
Expression of caveolins in RMS tumours. Double immunostain showing that in skeletal muscle Cav-1 and Cav-3 mark satellite cells and the plasmalemma of myofibres
https://openi.nlm.nih.gov/detailedresult.php?img=PMC4373424_jcmm0015-2553-f2&req=4
Download Caveolins In Cancer Pathogenesis, Prevention And TherapyDownload Caveolins In Cancer Pathogenesis, Prevention And Therapy
This download caveolins was been, and received on the treatment by Sir Henry Irving in 1875. Harold was in 1876, The Cup in 1881( at the Lyceum), The Promise of May( at the Globe) in 1882, Becket in 1884, with The Foresters in 1892. The download is one from which I give, not right of secure single-player of the purchase and of of rendering for the analysis.
http://oughtsix.com/ebooks/download-caveolins-in-cancer-pathogenesis%2C-prevention-and-therapy.html
Caveolin-1 as a potential new therapeutic target in multiple myelomaCaveolin-1 as a potential new therapeutic target in multiple myeloma
Caveolae are specialized flask-shaped lipid rafts enriched in cholesterol, sphingolipids, and structural marker proteins termed caveolins. Caveolins are highly conserved hairpin loop-shaped, oligomeric proteins of 22-24 kDa. Besides the plasma cell membrane, caveolins are also present in mitochondri …
https://pubmed.ncbi.nlm.nih.gov/16473666/?dopt=Abstract
Quartett - Caveolin 1 1-CA286-05 Caveolins are a family of int...Quartett - Caveolin 1 1-CA286-05 Caveolins are a family of int...
opamine D3 receptor, Caveolin1, Caveolin 1, 3 dopamine receptor, D, Dopamine receptor D3, DRD, ETM1, FET1, Cav-1, ETM1, CAV 1, CAV1, CAV1_HUMAN.
https://www.quartett.com/Antikoerper/Caveolin-1/
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Brain Sciences | Free Full-Text | Forced Exercise Enhances Functional Recovery after Focal Cerebral Ischemia in Spontaneously...Brain Sciences | Free Full-Text | Forced Exercise Enhances Functional Recovery after Focal Cerebral Ischemia in Spontaneously...
Caveolin is the principal protein of caveolae and has been implicated in the pathogenesis of cerebral ischemia. To investigate whether changed expression of caveolins has a pivotal role in focal cerebral ischemia, we induced middle cerebral artery occlusion (MCAo)-reperfusion and examined expression of caveolins, inflammatory activation markers, and mediators of autophagic cell death. We also treated MCAo rats with forced exercise to determine its effects on neurological outcome. Particularly, spontaneously hypertensive rats (SHR) and normotensive Wistar-Kyoto (WKY) rats were used to compare the effects of hypertension on focal cerebral ischemia. All MCAo groups showed neurological deficiencies, motor dysfunction, and disruption of balancing ability; however, these pathological changes were more severe in SHR than WKY rats. Expression of caveolins was decreased in MCAo brain tissue, whereas the levels of iNOS and glial fibrillary acidic protein (GFAP) increased. Additionally, LC3-II and beclin-1 levels
https://www.mdpi.com/2076-3425/2/4/483
Role of caveolae in the airway<...Role of caveolae in the airway<...
TY - CHAP. T1 - Role of caveolae in the airway. AU - Pabelick, Christina M. AU - Singh, Brij B.. AU - Prakash, Y.s.. PY - 2013/11/1. Y1 - 2013/11/1. N2 - Caveolae are flask-shaped invaginations of the plasma membrane that are rich in lipids and serve as microdomains to facilitate interactions between proteins at the membrane as well as intracellular components, thus modulating signal transduction, protein and lipid transport, and other processes. Constituent caveolar proteins such as caveolins and cavins also have scaffolding domains that anchor and regulate protein function. There is now evidence that caveolae and their constituent proteins are present in airway smooth muscle in a variety of species. Caveolae in airway cells contain or interact with molecules such as receptors, ion channels, and regulatory proteins that are key to the roles of airway epithelium and smooth muscle in regulating airway structure and function. Furthermore, caveolar protein expression and regulation appear to be ...
https://mayoclinic.pure.elsevier.com/en/publications/role-of-caveolae-in-the-airway
Abstract 176: Administration of a Caveolin-1 Mimetic Peptide Rescues the Cardiac and Pulmonary Abnormalities Observed in Cav-1...Abstract 176: Administration of a Caveolin-1 Mimetic Peptide Rescues the Cardiac and Pulmonary Abnormalities Observed in Cav-1...
Introduction: Caveolins (Cav), the principal structural proteins of the caveolar domain, have been implicated in the development of cardiac hypertrophy, pulmonary hypertension (PH) and lung remodeling. Mice with homozygous deletion of the Cav-1 gene display cardiac hypertrophy and pulmonary abnormalities characterized by thickened alveolar septa, hypercellularity and PH. In vivo administration of a cell-permeable Cav-1 mimetic peptide was previously shown to prevent the development of monocrotaline-induced pulmonary artery medial hypertrophy, PH and right ventricular hypertrophy in rats. Whether administration of such a Cav-1 peptide could rescue the cardio-pulmonary defects observed in Cav-1 KO mice remains unknown.. Methods and Results: Three week-old wild-type and Cav-1 KO mice were randomly assigned to receive a daily intraperitoneal injection of either saline, penetratin alone (AP, 2.5 mg/kg/d) or a peptide consisting of the Cav-1 scaffolding domain coupled to penetratin (AP-Cav, 2.5 ...
http://circ.ahajournals.org/content/116/Suppl_16/II_13.2
Caveolae-associated protein 1Caveolae-associated protein 1
This gene encodes a protein that enables the dissociation of paused ternary polymerase I transcription complexes from the 3 end of pre-rRNA transcripts. This protein regulates rRNA transcription by promoting the dissociation of transcription complexes and the reinitiation of polymerase I on nascent rRNA transcripts. This protein also localizes to caveolae at the plasma membrane and is thought to play a critical role in the formation of caveolae and the stabilization of caveolins. This protein translocates from caveolae to the cytoplasm after insulin stimulation. Caveolae contain truncated forms of this protein and may be the site of phosphorylation-dependent proteolysis. This protein is also thought to modify lipid metabolism and insulin-regulated gene expression. Mutations in this gene result in a disorder characterized by generalized lipodystrophy and muscular dystrophy. [provided by RefSeq, Nov 2009 ...
https://pharos.nih.gov/idg/targets/Q6NZI2
Interaction with Caveolin-1 Modulates G Protein Coupling of Mouse beta(3)-AdrenoceptorInteraction with Caveolin-1 Modulates G Protein Coupling of Mouse beta(3)-Adrenoceptor
Caveolins act as scaffold proteins in multiprotein complexes and have been implicated in signaling by G protein-coupled receptors. Studies using knock-out mice suggest that beta(3)-adrenoceptor (beta(3)-AR) signaling is dependent on caveolin-1; however, it is not known whether caveolin-1 is associated with the beta(3)-AR or solely with downstream signaling proteins. We have addressed this question by examining the impact of membrane rafts and caveolin-1 on the differential signaling of mouse beta(3a)- and beta(3b)-AR isoforms that diverge at the distal C terminus. Only the beta(3b)-AR promotes pertussis toxin (PTX)-sensitive cAMP accumulation. When cells expressing the beta(3a)-AR were treated with filipin III to disrupt membrane rafts or transfected with caveolin-1 siRNA, the cyclic AMP response to the beta(3)-AR agonist CL316243 became PTX-sensitive, suggesting G alpha(i/o) coupling. The beta(3a)-AR C terminus, S (P-384) under bar PLNR (P-389) under bar DG (Y-392) under bar EGARP (P-398) under ...
http://su.diva-portal.org/smash/record.jsf?pid=diva2:555303
Caveolin-3Caveolin-3
This gene encodes a caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites. [provided by RefSeq, Jul 2008 ...
https://pharos.nih.gov/idg/targets/P56539
Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2
Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other epithelial tissues. We have recently shown that there is an association between this glycerol channel and phospholipase D2 (PLD2) in caveolin-rich membrane microdomains. While …
https://pubmed.ncbi.nlm.nih.gov/21276418/
Gentaur Molecular :Prospecbio \ Mouse Anti Human Caveolin-1 CAV1 \ ant-027Gentaur Molecular :Prospecbio \ Mouse Anti Human Caveolin-1 CAV1 \ ant-027
Gentaur molecular products has all kinds of products like :search , Prospecbio \ Mouse Anti Human Caveolin-1 CAV1 \ ant-027 for more molecular products just contact us
http://www.antibody-antibodies.com/product_det.php?id=2790468&supplier=search&name=Mouse%20Anti%20Human%20Caveolin_1%20CAV1
Laboratory of Virology - Charles UniversityLaboratory of Virology - Charles University
Virus tracking in living NMuMG epithelial cells expressing GFP-fused caveolin-1. (a) Caveolar endocytosis, fission and fusion events, and internal vesicle membrane dynamics are shown not to be affected in a stable cell line. (b) Detail of an infected cell (in a surface confocal section) with a virion bypassing a caveolin-rich domain. (c) In-depth confocal section with a virion(s) captured in a caveolin-rich vesicle at the nuclear periphery. (d and e) Uptake of virions through caveolin membrane domains at the cell surface. Mouse NMuMG epithelial cells expressing GFP-tagged caveolin-1 were infected with Alexa 594-prestained virus (MOI of 10e3 virus particles per cell) and scanned in an open, mediumcontaining chamber with a deltaT of 6 s. Bars, 5 um (a to c) and 2 um (d and e). Liebl et al., J Virol 2006. ...
http://prfdec.natur.cuni.cz/molbio/virology/gallery.htm
Caveolin-2 is targeted to lipid droplets, a new membrane domain in the cell<...Caveolin-2 is targeted to lipid droplets, a new membrane domain in the cell<...
TY - JOUR. T1 - Caveolin-2 is targeted to lipid droplets, a new membrane domain in the cell. AU - Fujimoto, Toyoshi. AU - Kogo, Hiroshi. AU - Ishiguro, Kimiko. AU - Tauchi, Kumi. AU - Nomura, Ryuji. PY - 2001/3/5. Y1 - 2001/3/5. N2 - Caveolin-1 and -2 constitute a framework of caveolae in nonmuscle cells. In the present study, we showed that caveolin-2, especially its β isoform, is targeted to the surface of lipid droplets (LD) by immunofluorescence and immunoelectron microscopy, and by subcellular fractionation. Brefeldin A treatment induced further accumulation of caveolin-2 along with caveolin-1 in LD. Analysis of mouse caveolin-2 deletion mutants revealed that the central hydrophobic domain (residues 87-119) and the NH2-terminal (residues 70-86) and COOH-terminal (residues 120-150) hydrophilic domains are all necessary for the localization in LD. The NH2- and COOH-terminal domains appeared to be related to membrane binding and exit from ER, respectively, implying that caveolin-2 is ...
https://pure.fujita-hu.ac.jp/en/publications/caveolin-2-is-targeted-to-lipid-droplets-a-new-membrane-domain-in
Gaining Respectability | Circulation ResearchGaining Respectability | Circulation Research
Shibata and colleagues have shown previously that the application of peptides derived from the Gαs sequence in inside-out macropatches enhanced isoproterenol-evoked sodium current (INa), attributable to an apparent increase in the number of functional channels.5,6⇓ In this issue of Circulation Research, Shibata and colleagues (Yarbrough et al8) report that the source of these new channels could be caveolae. Using antibodies directed against caveolin-3, the muscle-specific isoform of caveolin, these investigators were able to block the direct effect of isoproterenol on the Na+ channel (ie, the PKA-independent, Gαs membrane-delimited pathway). Importantly, this effect seems specific, given that antibodies directed against other caveolin isoforms did not affect isoproterenol activation of Na+ channel activity. Moreover, Yarbrough et al8 also documented, in cardiac myocytes, the apparent preferential enrichment into caveolar microdomains of Na+ channels and Gαs. Although these data led the ...
http://circres.ahajournals.org/content/90/4/369.long
Caveolin-2 (phospho Y19)抗体[EPR2220(3)]|Anti-Caveolin-2 (phospho Y19)抗体[EPR2220(3)]Caveolin-2 (phospho Y19)抗体[EPR2220(3)]|Anti-Caveolin-2 (phospho Y19)抗体[EPR2220(3)]
Caveolin-2兔单克隆抗体[EPR2220(3)](ab124883)可与人样本反应并经WB, Flow Cyt实验严格验证。中国75%以上现货，所有产品均提供质保服务，可通过电话、电邮或微信获得本地专属技术支持。
http://www.abcam.cn/caveolin-2-phospho-y19-antibody-epr22203-ab124883.html
ROLES FOR A NOVEL CAVIN-1/SOCS3 INTERACTION IN REGULATING PRO-INFLAMMATORY IL-6 SIGNALLING AND CAVEOLA STABILITY | HeartROLES FOR A NOVEL CAVIN-1/SOCS3 INTERACTION IN REGULATING PRO-INFLAMMATORY IL-6 SIGNALLING AND CAVEOLA STABILITY | Heart
Caveolae are plasma membrane microdomains that localise receptors and signalling intermediates within an environment where they can efficiently trigger downstream events. While present in most cells types, they are particularly abundant in vascular smooth muscle cells and endothelial cells (ECs), where they regulate low density lipoprotein trans-cytosis, NO production and inflammation. Cavin-1 is a protein required for caveolae maturation, such that its deletion results in no detectable caveolae and the down-regulation of caveolin scaffolding proteins. However, the cellular processes regulating cavin-1 function are poorly understood. Proteomic screening and biochemical experiments have identified cavin-1 as a novel interacting protein of the cytokine-inducible E3 ubiquitin ligase component suppressor of cytokine signalling-3 (SOCS3), a key inhibitor of IL-6-mediated pro-inflammatory signalling in ECs. We hypothesise d that the SOCS3/cavin-1 interaction may be important in controlling caveola ...
http://heart.bmj.com/content/100/Suppl_4/A6.1
Recent Publication: Keratinocyte Proliferation and Differentiation - CC: Report | communication. information. engagement.Recent Publication: Keratinocyte Proliferation and Differentiation - CC: Report | communication. information. engagement.
Phospholipase D2 (PLD2) has been found localized in low-density caveolin-rich membrane microdomains. Our previous study suggested that PLD2 and aquaporin 3 (AQP3) interact in these domains to inhibit keratinocyte proliferation and promote differentiation by cooperating to produce phosphatidylglycerol. To examine the effect of membrane microdomain localization on the PLD2/AQP3 signaling module and keratinocyte proliferation and differentiation, we treated mouse keratinocytes with 3 µM cell-permeable caveolin-1 scaffolding domain peptide or a negative control peptide and stimulated cell differentiation using a moderately elevated extracellular calcium concentration (125 uM) to maximally promote differentiation and phosphatidylglycerol production. Cell proliferation, differentiation, total PLD activity, phosphatidylglycerol levels, and AQP3 activity were monitored. The caveolin-1 scaffolding domain peptide itself had no effect on phosphatidylglycerol levels or keratinocyte proliferation or ...
https://ccreport.augusta.edu/2013/12/02/keratinocyte-proliferation-and-differentiation/
Circulating cardiovascular disease risk factors and signaling in endothelial cell caveolae<...Circulating cardiovascular disease risk factors and signaling in endothelial cell caveolae<...
TY - JOUR. T1 - Circulating cardiovascular disease risk factors and signaling in endothelial cell caveolae. AU - Mineo, Chieko. AU - Shaul, Philip W.. PY - 2006/4/1. Y1 - 2006/4/1. N2 - Caveolae are a subset of lipid rafts that are prevalent on the plasma membrane of endothelial cells. They compartmentalize signal transduction molecules which regulate multiple endothelial functions including the production of nitric oxide (NO) by the caveolae resident enzyme endothelial NO synthase (eNOS). Recent studies have demonstrated that circulating factors known to modify cardiovascular disease risk regulate signaling in endothelial cell caveolae. In particular, high density lipoprotein (HDL) maintains the lipid environment in caveolae, thereby promoting the retention and function of eNOS in the domain, and it also causes direct activation of eNOS via scavenger receptor type BI (SR-BI)-induced kinase signaling. Estrogen binding to estrogen receptors (ER) in caveolae also activates eNOS, and this occurs ...
https://utsouthwestern.pure.elsevier.com/en/publications/circulating-cardiovascular-disease-risk-factors-and-signaling-in-
Caveolae Conducting Calcium | Science SignalingCaveolae Conducting Calcium | Science Signaling
Caveolae are specialized membrane domains that function in endocytosis and contain relatively high concentrations of signaling molecules. Isshiki et al. now present evidence that caveolae serve as preferential sites of Ca2+ influx across the plasma membrane when intracellular stores of Ca2+ are depleted. The authors fused the calcium sensor yellow chameleon 3.1 to the COOH-terminal end of caveolin-1 to target the sensor to caveolae. Then, they compared Ca2+ signals at the caveolae to those from unmodified yellow chameleon in the cytoplasm or from another fusion protein that targeted the sensor to the plasma membrane. When Ca2+ was depleted from the endoplasmic reticulum of fetal bovine endothelial cells by exposure of the cells to adenosine triphosphate (ATP) and thapsigargin, Ca2+ entry into the cells occurred preferentially at caveolae, apparently through store-operated channels of the TRP (transient receptor potential) family. The authors propose that caveolae may function as preassembled, ...
https://stke.sciencemag.org/content/2002/158/tw414
CAVIN2 - Caveolae-associated protein 2 - Homo sapiens (Human) - CAVIN2 gene & proteinCAVIN2 - Caveolae-associated protein 2 - Homo sapiens (Human) - CAVIN2 gene & protein
Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (PubMed:19525939). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity).
http://www.uniprot.org/uniprot/O95810
Cav2 - Caveolin-2 - Mus musculus (Mouse) - Cav2 gene & proteinCav2 - Caveolin-2 - Mus musculus (Mouse) - Cav2 gene & protein
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).
http://www.uniprot.org/uniprot/Q9WVC3
Caveolin-1 says NO to permeability | JCBCaveolin-1 says NO to permeability | JCB
Proteins and other substances can cross the endothelial layer that lines a blood vessel via two routes. Caveolin-1 is essential for both, Siddiqui et al. show.. Researchers already knew that caveolin-1 was necessary for transcellular protein trafficking, in which macromolecules such as albumin enter an endothelial cell from the bloodstream and exit on the tissue side. Caveolae swallow these molecular travelers and bundle them into vesicles that wend through the cell. In an alternative pathway, known as the paracellular route, molecules slip between the cells of the endothelial layer, passing through the adherens junctions that fasten adjacent cells together. Previous work showed that adherens junctions become permeable in mice lacking caveolin-1, suggesting that the protein helps seal the junctions.. Siddiqui et al. dissected the molecular chain of events that connects caveolin-1 to adherens junction integrity. Loss of caveolin-1 activated the enzyme eNOS, which spawns nitric oxide (NO) that ...
http://jcb.rupress.org/content/193/5/800.2
Plus itPlus it
Caveolae are specialised forms of lipid rafts in the plasma membrane of most cells. They form dynamic assemblies of sphingolipids and cholesterol containing scaffolding domains with different affinities for proteins resulting in a variety of functions [1]. The constitutive Cav-1 protein is distributed ubiquitously, while Cav-2 is usually associated with Cav-1 [3, 28]. Although Cav-3 is thought to be muscle specific and is expressed in striated muscles [3, 28, 29], we and others have found that Cav-3 is not expressed within human ASM [6, 30]. Recent studies have established that ASM caveolae contain a number of proteins important to [Ca2+]i regulation (e.g. agonist receptors, Ca2+ influx channels, and force regulatory proteins such as RhoA). In canine ASM, it has been established that caveolar-enriched membrane fractions express Cav-1, L-type Ca2+ channels and plasma membrane Ca2+ ATPase, but not SR proteins such as IP3R or RyR channels [31].. In ASM of different species, in addition to Ca2+ ...
http://erj.ersjournals.com/content/40/2/470
Molecular Vision: Apoptosis of lens epithelial cells induced by high concentration of glucose is associated with a decrease in...Molecular Vision: Apoptosis of lens epithelial cells induced by high concentration of glucose is associated with a decrease in...
Caveolae, the sphingomy-cholesterol enriched microdomains, form a stable lipid matrix that act as an ordered support for receptor-mediated signaling events. It has been proposed that caveola composition changes in response to adverse extracellular conditions [35,36]. Consistent with this hypothesis, we found in the current study that HG treatment led to a decrease in the number of caveolae on the surface of LECs. We also found reduced levels of caveolin-1 mRNA and protein in HG-treated LECs, indicating that caveolin-1 expression was down-regulated at the transcription level. Although it has been proposed that caveolin-1 functions as a message center that compartmentalizes anti- and pro-apoptotic signaling molecules on the cell surface to regulate apoptosis [17], its role in regulating apoptosis remains controversial. In the current study, we found the levels of caveolin-1 reduced and apoptosis rate increased in HG-treated LECs, indicating that caveolin-1 may inhibit apoptosis. However, ...
http://www.molvis.org/molvis/v15/a214/
where to get vector overexpressing caveolin-1?: post #1where to get vector overexpressing caveolin-1?: post #1
where to get vector overexpressing caveolin-1? - posted in Molecular Cloning: Trying to overexpress caveolin-1 in human cancer cells...are there readymade products out there which already has cav-1 attached to a dependable promoter? If so, where should I look? Thanks in advance!
http://www.protocol-online.org/forums/topic/25607-where-to-get-vector-overexpressing-caveolin-1/
Caveolin-2 peptide (ab4929) | AbcamCaveolin-2 peptide (ab4929) | Abcam
Buy our Caveolin-2 peptide. Ab4929 is a blocking peptide and has been validated in BL. Abcam provides free protocols, tips and expert support for WB and a 12…
http://www.abcam.com/caveolin-2-peptide-ab4929.html
Only a fraction of flotillins was normally noticed in the raft fractions, while the rest was observed in much more dense...Only a fraction of flotillins was normally noticed in the raft fractions, while the rest was observed in much more dense...
Nevertheless, soon after 10 times of culturing, in the course of which adhesion constructions fully maturate, we noticed a coprecipitation of c-catenin also
http://www.sgkinhibitor.com/2016/02/23/only-a-fraction-of-flotillins-was-normally-noticed-in-the-raft-fractions-while-the-rest-was-observed-in-much-more-dense-fractions/
Cavin3 MGI Mouse Gene Detail - MGI:1923422 - caveolae associated 3Cavin3 MGI Mouse Gene Detail - MGI:1923422 - caveolae associated 3
View mouse Cavin3 Chr7:105480083-105482300 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
http://www.informatics.jax.org/marker/MGI:1923422
Addgene: CAV1-mEGFPAddgene: CAV1-mEGFP
Plasmid CAV1-mEGFP from Dr. Ari Heleniuss lab contains the insert caveolin-1 and is published in Traffic. 2010 Mar . 11(3):361-82. This plasmid is available through Addgene.
https://www.addgene.org/27704/
Hormonal control of reversible translocation of perilipin B to the plasma membrane in primary human adipocytesHormonal control of reversible translocation of perilipin B to the plasma membrane in primary human adipocytes
The primary function of adipose tissue is to store energy in the form of triacylglycerol, which is hydrolyzed to fatty acids to supply other tissues with energy. While insulin promotes the storage of triacylglycerol, catecholamines stimulate its hydrolysis. The development of type II diabetes is strongly associated with obesity, indicating a role of triacylglycerol metabolism in the pathogenesis of diabetes. Caveolae are plasma membrane invaginations found in most cells but are highly abundant in adipocytes. Insulin receptors are localized in caveolae and their function depends on intact caveolae structures. In the present thesis work, mass spectrometry-based methodology allowed identification of a number of new proteins and their posttranslational modifications in caveolae of human adipocytes. Variable N-terminal acetylation and phosphorylation of caveolin-1α and caveolin-1β were identified, which might regulate the function of caveolae. The transcription regulator protein PTRF was identified ...
http://liu.diva-portal.org/smash/record.jsf?pid=diva2:223384
JCI - WelcomeJCI - Welcome
Caveolin-3, the muscle-specific isoform of caveolins, plays important roles in signal transduction. Dominant-negative mutations of the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy 1C (LGMD1C) with loss of caveolin-3. However, identification of the precise molecular mechanism leading to muscular atrophy in caveolin-3-deficient muscle has remained elusive. Myostatin, a member of the muscle-specific TGF-β superfamily, negatively regulates skeletal muscle volume. Here we report that caveolin-3 inhibited myostatin signaling by suppressing activation of its type I receptor; this was followed by hypophosphorylation of an intracellular effector, Mad homolog 2 (Smad2), and decreased downstream transcriptional activity. Loss of caveolin-3 in P104L mutant caveolin-3 transgenic mice caused muscular atrophy with increase in phosphorylated Smad2 (p-Smad2) as well as p21 (also known as Cdkn1a), a myostatin target gene. Introduction of the myostatin prodomain, an inhibitor of ...
https://www.jci.org/tags/32?content=articles&page=38
The cell. 5. Vesicular traffic. Endocytosis. Atlas of plant and animal histology.The cell. 5. Vesicular traffic. Endocytosis. Atlas of plant and animal histology.
Caveolae. Caveolae were described in the fifties of the last century by P. Palade after observing animal tissues at transmission electron microscopy. They are small invaginations (45-80 nm) of the plasma membrane that can be observed in most of the eukaryotic cells. It was suggested that most of the caveolae become vesicles (but see below). Caveolae are abundant in endothelial cells, muscle cells and adipocytes. The membrane of the caveolae contains caveolin, as well as other integral proteins linked to glycosylphosphatidylinositol, many sphingolipids (sphingomyelin and glycosphingolipids), and is enriched in cholesterol. The presence of caveolin in a cell is enought to form caveolae. There are around 100 to 200 caveolin molecules in one caveola and there are different types of caveolin in one caveola. Caveolin 1 is expressed in smooth muscle cells and in most of the non muscle cells, and it is necessary for caveolae formation in these cells. Caveolin 2, which can be expressed in the same cells ...
http://mmegias.webs.uvigo.es/02-english/5-celulas/5-endocitosis.php
CSF1R | PR109A as an Anti-Inflammatory ReceptorCSF1R | PR109A as an Anti-Inflammatory Receptor
Research in cultured cells present that activation of endothelial nitric oxide (Zero) synthase (eNOS) requires the dissociation of the enzyme from it is inhibitory association with caveolin-1 (Cav-1), as well as perhaps it is translocation from plasma membrane caveolae to other cellular compartments. microsomal small percentage. ACh-induced vasodilatation was connected with eNOS translocation towards the cytosolic and Golgi-enriched fractions. After 1.5, 3.0 or 6.0 min of application, 10 m ACh reduced the amount of membrane-bound eNOS by -13 4 %, -60 4 % and -19 17 INCB8761 (PF-4136309) %, respectively; at the same time factors, 100 m ACh decreased microsomal eNOS articles by -38 9 %, -61 16 % and -40 18 %, respectively (= 4-5). In every situations, microsomal Cav-1 articles did not transformation. The close ACh focus dependence as well as the concomitance INCB8761 (PF-4136309) between eNOS subcellular redistribution no release support the idea that eNOS translocation in the plasma membrane is ...
http://gpr109a.info/tag/csf1r/
Low Molecular Weight-Protein Tyrosine Phosphatase and Caveolin-1: Interaction and Isoenzyme-Dependent Regulation | IRIS...Low Molecular Weight-Protein Tyrosine Phosphatase and Caveolin-1: Interaction and Isoenzyme-Dependent Regulation | IRIS...
Abstract: Low molecular weight protein tyrosine phosphatases (LMW-PTPs) are small enzymes that are ubiquitous in many organisms. They are important in biological processes such as cell proliferation, adhesion, migration, and invasiveness. LMW-PTP is expressed in mammalian cells as two isoforms (IF1 and IF2) originating through alternative splicing. We have previously shown that IF2 targets lipid rafts called caveolae and interacts with caveolin-1, their major structural protein. Caveolae are cholesterol- and sphingolipid-rich membrane microdomains that have been implicated in a variety of cellular functions, including signal transduction events. Caveolin-1 contains a scaffolding region that contributes to the binding of the protein to the plasma membrane and mediates protein omo- and etero-oligomerization. Interaction of many signaling molecules with the scaffolding domain sequesters them into caveolae and inhibits or suppresses their activities. Caveolin-interacting proteins usually have a ...
https://flore.unifi.it/handle/2158/315532
Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin. - Zurich Open Repository...Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin. - Zurich Open Repository...
Caveolae are specialized domains present in the plasma membrane (PM) of most mammalian cell types. They function in signalling, membrane regulation, and endocytosis. We found that the Eps-15 homology domain-containing protein 2 (EHD2, an ATPase) associated with the static population of PM caveolae. Recruitment to the PM involved ATP binding, interaction with anionic lipids, and oligomerization into large complexes (60-75S) via interaction of the EH domains with intrinsic NPF/KPF motifs. Hydrolysis of ATP was essential for binding of EHD2 complexes to caveolae. EHD2 was found to undergo dynamic exchange at caveolae, a process that depended on a functional ATPase cycle. Depletion of EHD2 by siRNA or expression of a dominant-negative mutant dramatically increased the fraction of mobile caveolar vesicles coming from the PM. Overexpression of EHD2, in turn, caused confinement of cholera toxin B in caveolae. The confining role of EHD2 relied on its capacity to link caveolae to actin filaments. Thus, ...
https://www.zora.uzh.ch/id/eprint/81279/
SNU Open Repository and Archive: Modulation of cancer cell growth and progression by Caveolin-1 in the tumor microenvironmentSNU Open Repository and Archive: Modulation of cancer cell growth and progression by Caveolin-1 in the tumor microenvironment
Caveolin-1 (Cav-1), a major structural component of cell membrane caveolae, is involved in a variety of intracellular signaling pathways as well as transmembrane transport. Cav-1, as a scaffolding protein, modulates signal transduction associated with cell cycle progression, cellular senescence, cell proliferation and death, lipid homeostasis, etc. Cav-1 is also thought to regulate the expression or activity of oncoproteins, such as Src family kinases, H-Ras, protein kinase C, epidermal growth factor, extracellular signal-regulated kinase, and endothelial nitric oxide synthase. Because of its frequent overexpression or mutation in various tumor tissues and cancer cell lines, Cav-1 has been speculated to play a role as an oncoprotein in cancer development and progression. In contrast, Cav-1 may also function as a tumor suppressor, depending on the type of cancer cells and/or surrounding -stromal cells in the tumor microenvironment as well as the stage of tumors ...
https://s-space.snu.ac.kr/handle/10371/172545
The Role of Caveolae in PECAM-1 Mechanotransduction :: Temple University Electronic Theses and DissertationsThe Role of Caveolae in PECAM-1 Mechanotransduction :: Temple University Electronic Theses and Dissertations
Altered fluid flow, which is found in branches and curvatures of arteries, results in abnormal forces on the endothelial cells (EC). These forces have been shown to alter EC gene expression and phenotype and to activate several cellular structures including G-proteins, ion channels, adhesion molecules, and caveolae. Recently, PECAM-1 has been implicated as the primary sensor of hemodynamic forces in EC. Shear stress rapidly induces tyrosine phosphorylation of PECAM-1 and the recruitment of SHP-2. These events appear to contribute to shear-activation of ERK1/2. Additionally, PECAM-1 has been shown to form a mechanosensory signaling complex with VE-cadherin, VEGFR2, and βcatenin which plays a role in adhesion molecule expression and regulation of NF-κB. Past work has shown that caveolae membrane domains also serve as mechanotransduction sites that regulate many of these same second messengers. Based on these novel observations, we hypothesize that the PECAM-1 mediated mechanotransduction ...
http://digital.library.temple.edu/cdm/ref/collection/p245801coll10/id/263778/
Caveolin-1 (Cav-1) is a 21?kDa protein enriched in caveolae and continues - Role of adrenergic receptors in human coronary...Caveolin-1 (Cav-1) is a 21?kDa protein enriched in caveolae and continues - Role of adrenergic receptors in human coronary...
Caveolin-1 (Cav-1) is a 21?kDa protein enriched in caveolae and continues to be implicated in oncogenic cell transformation CHC tumorigenesis and metastasis. response to chemotherapy and radiation and tumor growth. We found Cav-1 is definitely overexpressed in human being Personal computer cell lines mouse models and human being pancreatic tumors and is associated with worse tumor grade and clinical results. In Personal computer cell lines disruption/depletion of caveolae/Cav-1 reduces proliferation colony formation and invasion. Radiation and chemotherapy up-regulate Cav-1 manifestation while Cav-1 depletion induces both chemosensitization and radiosensitization through modified apoptotic and DNA restoration signaling. and and transgene (KPC mouse) (Fig. 1B). Cav-1 manifestation was also tested on a cells microarray of 110 individuals with pancreatic malignancy and obtained semi-quantitatively for low versus high CHC manifestation. While Cav-1 is definitely virtually absent in pancreatic ...
http://researchreportone.com/?p=1569
Flotillins: Signals from a RaftFlotillins: Signals from a Raft
Flotillins are highly homologous proteins (known as flotillin-1 and flotillin-2, or reggie-2 and reggie-1, respectively) that localize to membrane rafts (specific cholesterol-rich microdomains in cellular membranes), and are associated with various signaling pathways, cell adhesion, membrane trafficking and axonal growth.. Flotillins are strongly conserved across many species, found in bacteria, plants, fungi and all mammals, and show ubiquitous tissue expression. They are widely used as biomarkers for membrane rafts and show dynamic subcellular distribution. Significantly, flotillins are also frequently overexpressed in cancer.. In Flotillins in Receptor Tyrosine Kinase Signaling and Cancer, Banning et al., provide a timely review that details recent studies offering novel insights into flotillin involvement in receptor tyrosine kinase and mitogen activated protein (MAP) kinase signaling, cancer and metastasis. Further, the authors provide a thorough overview of data that correlates ...
https://blog.mdpi.com/2014/02/21/flotillins-signals-from-a-raft/
November 2015 - HourlyBookNovember 2015 - HourlyBook
1.The upper part of thalamus may be disc shaped, cup-shaped or flask-shaped. 2.Calyx, corolla and androecium arise from around the ovary and not beneath it. 3.Ovary is half-superior/half-inferior. 4.The ovary is placed at the bottom of cup or flask-shaped thalamus. Ovary wall is not fused with the thalamus. 5.Calyx, corolla and androecium often develop from …. Read more ...
https://www.hourlybook.com/2015/11/
Caveolin-1 antibody | acris-antibodies.comCaveolin-1 antibody | acris-antibodies.com
The scaffolding protein CAV1 is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to…
https://www.acris-antibodies.com/target/caveolin-1-antibody.htm
Biogenesis of Caveolae - Research CollectionBiogenesis of Caveolae - Research Collection
Received 6 November 2009. Accepted 1 December 2009. Uncorrected manuscript published online 3 December 2009. Published online 8 January 2010 ...
https://www.research-collection.ethz.ch/handle/20.500.11850/17146
Rab12 localizes to Shiga toxin-induced plasma membrane invaginations and controls toxin transport. | DIAL.pr - BOREALRab12 localizes to Shiga toxin-induced plasma membrane invaginations and controls toxin transport. | DIAL.pr - BOREAL
Several exogenous and endogenous cargo proteins are internalized independently of clathrin, including the bacterial Shiga toxin. The mechanisms underlying early steps of clathrin-independent uptake remain largely unknown. In this study, we have designed a protocol to obtain gradient fractions containing Shiga toxin internalization intermediates. Using stable isotope labeling with amino acids in cell culture (SILAC) and quantitative mass spectrometry, Rab12 was found in association with these very early uptake carriers. The localization of the GTPase on Shiga toxin-induced plasma membrane invaginations was shown by fluorescence microscopy in cells transfected with GFP-Rab12. Furthermore, using a quantitative biochemical assay, it was found that the amount of receptor-binding B-subunit of Shiga toxin reaching the trans-Golgi/TGN membranes was decreased in Rab12-depleted cells, and that cells were partially protected against intoxication by Shiga-like toxin 1 under these conditions. These findings ...
https://dial.uclouvain.be/pr/boreal/object/boreal:180288
Caveolae - WikipediaCaveolae - Wikipedia
In biology, caveolae (Latin for little caves; singular, caveola), which are a special type of lipid raft, are small (50-100 nanometer) invaginations of the plasma membrane in many vertebrate cell types, especially in endothelial cells, adipocytes and embryonic notochord cells. They were originally discovered by E. Yamada in 1955. These flask-shaped structures are rich in proteins as well as lipids such as cholesterol and sphingolipids and have several functions in signal transduction. They are also believed to play a role in mechanoprotection, mechanosensation, endocytosis, oncogenesis, and the uptake of pathogenic bacteria and certain viruses. Formation and maintenance of caveolae was initially thought to be primarily due to caveolin, a 21 kD protein. There are three homologous genes of caveolin expressed in mammalian cells: Cav1, Cav2 and Cav3. These proteins have a common topology: cytoplasmic N-terminus with scaffolding domain, long hairpin transmembrane domain and cytoplasmic C-terminus. ...
https://en.wikipedia.org/wiki/Caveolae
Cholesterol is important in control of EGF receptor kinase activity but EGF receptors are not concentrated in caveolae |...Cholesterol is important in control of EGF receptor kinase activity but EGF receptors are not concentrated in caveolae |...
The plasma membrane is not uniform, but can be divided into different microdomains. Whereas some microdomains, such as clathrin-coated pits, are morphologically identifiable, others can be identified only upon colocalization with domain-specific marker molecules. Caveolae are microdomains originally identified morphologically as small noncoated invaginations of the plasma membrane. The formation of caveolae depends on expression of caveolin and, since the plasma membrane contains different noncoated invaginations, caveolae can be identified only by labeling for caveolin. Some confusion exists with respect to the relationship between caveolae and lipid rafts [see raft nomenclature ( Simons and Toomre, 2000)]. This is partly due to difficulties in isolating pure caveolae and to the various methods used for this purpose. Initially, subcellular fractionation upon Triton X-100 extraction at 4°C was used. Such fractionation allows the isolation of detergent-resistant membranes [DRMs; also called DIGs ...
https://jcs.biologists.org/content/115/6/1331?ijkey=a231e2eba2dddd9bd248cbf67aa1661ebe92ca5b&keytype2=tf_ipsecsha
Adenovirus-Mediated Overexpression of Caveolin-3 Inhibits Rat Cardiomyocyte Hypertrophy | HypertensionAdenovirus-Mediated Overexpression of Caveolin-3 Inhibits Rat Cardiomyocyte Hypertrophy | Hypertension
In this study, we examined cardiomyocyte hypertrophy by several methods. PE and ET increased leucine incorporation and cell area and changed the immunostaining pattern of phalloidin from a dense staining without agonists to fiberlike staining, indicating that myocyte hypertrophy did occur at the protein and structural levels. Moreover, βMHC expression was markedly augmented by PE and ET, suggesting the transformation of myosin. These results indicate that PE and ET induced pathologic hypertrophy in cardiomyocytes. Infection with Ad.Cav-3 prevented all of these changes induced by PE and ET. Thus, caveolin-3 might act as an inhibitor of myocyte hypertrophy. The effects of overexpression of wild-type caveolin-3 were not nonspecific, because infection with Ad.LacZ did not affect myocyte hypertrophy. Overexpression of caveolin-3 in Ad.Cav-3-infected cells was associated with the prevention of both agonist-induced hypertrophy and sarcomeric disorganization seen in Ad.LacZ-infected and control cells ...
http://hyper.ahajournals.org/content/42/2/213
Psych Central - Fatty acids and caveolin-1 are essential in liver regenerationPsych Central - Fatty acids and caveolin-1 are essential in liver regeneration
Lipids are the energy source used during liver regeneration. The research group, led by Dr. Albert Pol and with members from IDIBAPS, Universitat de Barcelona and Queensland University, unveils the essential role of the protein caveolin-1 in a fundamental process for liver cure after injury or transplant. Results also evidence the existence of cellular mechanisms by which excessive accumulation of lipids in the liver is a risk factor for the apparition of hepatic tumours.
https://psychcentral.com/news/archives/2006-09/i-id-faa091806.html
Caveolar structure and protein sorting are maintained in NIH 3T3 cells independent of glycosphingolipid depletion. - PubMed -...Caveolar structure and protein sorting are maintained in NIH 3T3 cells independent of glycosphingolipid depletion. - PubMed -...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
https://www.ncbi.nlm.nih.gov/pubmed/10620326?dopt=Abstract
The proteoglycan-dystrophin complex in genetic cardiomyopathie...The proteoglycan-dystrophin complex in genetic cardiomyopathie...
The proteoglycan-dystrophin complex in genetic cardiomyopathies--lessons from three siblings with limb-girdle muscular dystrophy-2I (LGMD-2I).:
https://www.mysciencework.com/publication/show/proteoglycan-dystrophin-complex-genetic-cardiomyopathies-lessons-from-three-siblings-limb-girdle-muscular-dystrophy-2i-37985a87
CaveolinCaveolin
... have developed compensation or redundancy for the functions of caveolins. Caveolins have a paradoxical role in the development ... The caveolins are similar in structure. They all form hairpin loops that are inserted into the cell membrane. Both the C- ... The functions of caveolins are still under intensive investigation. They are best known for their role in the formation of 50- ... In molecular biology, caveolins are a family of integral membrane proteins that are the principal components of caveolae ...
https://en.wikipedia.org/wiki/Caveolin
CaveolaeCaveolae
Caveolins associate with some signaling molecules (e.g. eNOS) through their scaffolding domain and so they can regulate their ... The ability of caveolins to oligomerize due to their oligomerization domains is necessary for formation of caveolar endocytic ... Caveolins are synthesized as monomers and transported to the Golgi apparatus. During their subsequent transport through the ... Increased levels of cholesterol and insertion of the scaffolding domains of caveolins into the plasma membrane leads to the ...
https://en.wikipedia.org/wiki/Caveolae
Caveolin 3Caveolin 3
Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin ... Couet J, Sargiacomo M, Lisanti MP (1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding ... Gratton JP, Bernatchez P, Sessa WC (2004). "Caveolae and caveolins in the cardiovascular system". Circ. Res. 94 (11): 1408-17. ...
https://en.wikipedia.org/wiki/Caveolin_3
Epidermal growth factor receptorEpidermal growth factor receptor
Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin ...
https://en.wikipedia.org/wiki/Epidermal_growth_factor_receptor
Caveolin 1Caveolin 1
Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin ... Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". The Journal of Biological Chemistry. 272 ( ...
https://en.wikipedia.org/wiki/Caveolin_1
Romano-Ward syndromeRomano-Ward syndrome
LQT9 is caused by variants in the membrane structural protein, caveolin-3. Caveolins form specific membrane domains called ...
https://en.wikipedia.org/wiki/Romano–Ward_syndrome
FLOT2FLOT2
2006). "Caveolins and flotillin-2 are present in the blood stages of Plasmodium vivax". Parasitol. Res. 99 (2): 153-9. doi: ... "Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in ...
https://en.wikipedia.org/wiki/FLOT2
Caveolin 2Caveolin 2
2000). "Characterization of caveolins from human knee joint catilage: expression of caveolin-1, -2, and -3 in chondrocytes and ... 1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero- ... Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". J. Biol. Chem. UNITED STATES. 272 (46): ... "Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in ...
https://en.wikipedia.org/wiki/Caveolin_2
Lipid raftLipid raft
Caveolins are widely expressed in the brain, micro-vessels of the nervous system, endothelial cells, astrocytes, ... Both types have similar lipid composition (enriched in cholesterol and sphingolipids). Flotillin and caveolins can recruit ...
https://en.wikipedia.org/wiki/Lipid_raft
FLOT1FLOT1
"Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in ...
https://en.wikipedia.org/wiki/FLOT1
Barraquer-Simons syndromeBarraquer-Simons syndrome
Human PTRF mutations may cause secondary deficiency of caveolins, resulting in generalized lipodystrophy in association with in ...
https://en.wikipedia.org/wiki/Barraquer–Simons_syndrome
AmphiregulinAmphiregulin
... expression in prostate cancer cells leads to an increased growth rate and induction of caveolins and amphiregulin". Cancer ...
https://en.wikipedia.org/wiki/Amphiregulin
PTRFPTRF
Cavin3 in caveola formation and has been shown to interact with other membrane associating proteins such as EHD2 and caveolins ...
https://en.wikipedia.org/wiki/PTRF
Frontiers | Caveolae, Caveolins, Cavins, and Endothelial Cell Function: New Insights | PhysiologyFrontiers | Caveolae, Caveolins, Cavins, and Endothelial Cell Function: New Insights | Physiology
Caveolins and the more recently discovered cavins are the major protein components of caveolae. When caveolae were discovered, ... The aim of this review is to focus primarily on molecular and cellular aspects of the role of caveolae, caveolins, and cavins ... The aim of this review is to focus primarily on molecular and cellular aspects of the role of caveolae, caveolins, and cavins ... Caveolins and the more recently discovered cavins are the major protein components of caveolae. When caveolae were discovered, ...
https://www.frontiersin.org/articles/10.3389/fphys.2011.00120/full
Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. |...Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. |...
Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. J ... Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. ... Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. ...
https://connects.catalyst.harvard.edu/Profiles/display/1151671
Volatile Anesthetics Protect Cancer Cells against Tumor Necrosis Factor-related Apoptosis-inducing Ligand-induced Apoptosis via...Volatile Anesthetics Protect Cancer Cells against Tumor Necrosis Factor-related Apoptosis-inducing Ligand-induced Apoptosis via...
Importantly, we have shown that protection in both the neuronal and cardiac system is caveolin-dependent.17 - 20 Caveolins are ... Caveolins, structural proteins found in caveolae, serve as scaffolds and regulators of signaling proteins, including G-proteins ... these data implicate caveolins as an essential component in the temporal and spatial organization of cardiac-protective ... Caveolins. Anesthesiology 9 2011, Vol.115, 499-508. doi:10.1097/ALN.0b013e3182276d42 ...
http://anesthesiology.pubs.asahq.org/article.aspx?articleid=1933562
Actin depolymerization regulates caveolins and cavins a | Open-iActin depolymerization regulates caveolins and cavins a | Open-i
Actin depolymerization regulates caveolins and cavins at the mRNA level in human coronary artery smooth muscle cells.Cells were ... pone.0133931.g002: Actin depolymerization regulates caveolins and cavins at the mRNA level in human coronary artery smooth ... pone.0133931.g002: Actin depolymerization regulates caveolins and cavins at the mRNA level in human coronary artery smooth ... Formation of caveolae requires caveolins and cavins. The make-up of caveolae and their density is considered to reflect cell- ...
https://openi.nlm.nih.gov/detailedresult.php?img=PMC4526231_pone.0133931.g002&req=4
Respiratory Therapy Cave: Olins: Part 3Respiratory Therapy Cave: 'Olins: Part 3
Effect. To a nerve cell, Keepmeawakeolin looks like a coffee molecule which looks like adenosine. It then is allowed to attach to adenosine receptors, thus preventing adenosine from attaching to them. So instead of adenosine slowing you down so you can sleep, Keepmeawakeolin keeps you awake. Adenosine dilates blood vessels in the brain, presumably to keep your brain well oxygenated while you are sleeping and your breathing is more relaxed. Keepmealiveolin mimics this effect, thus causing vasodilation of the vessels in the brain to assure adequate oxygenation while you are not sleeping. A side effect of this is that it may cause a headache, which is where caffeine comes in handy. About three hours after dosing, keepmealiveolin starts to dissolve, opening up just enough adenosine receptors for caffeine to attach. This should be enough, however, to constrict brain vessels, thus ridding you of your headache. Still, once the rest of the keepmealiveoline molecules dissipate, the next dose should be ...
http://respiratorytherapycave.blogspot.com/2015/08/olins-part-3.html
Caveolins and macrophage lipid metabolism<...Caveolins and macrophage lipid metabolism<...
Caveolins and macrophage lipid metabolism. / Gargalovic, Peter; Dory, Ladislav.. In: Journal of Lipid Research, Vol. 44, No. 1 ... Since caveolins have been implicated in the regulation of cellular cholesterol metabolism in several cell types, it is of ... Caveolins and macrophage lipid metabolism. In: Journal of Lipid Research. 2003 ; Vol. 44, No. 1. pp. 11-21. ... Since caveolins have been implicated in the regulation of cellular cholesterol metabolism in several cell types, it is of ...
https://experts.unthsc.edu/en/publications/caveolins-and-macrophage-lipid-metabolism
Caveolins And Caveolae Roles In Signaling And Disease Mechanisms 2012Caveolins And Caveolae Roles In Signaling And Disease Mechanisms 2012
If you did a caveolins and caveolae roles in signaling and disease mechanisms, school No or Cancel. W Confused about those ... Chapter 4s peroxides caveolins and caveolae roles in signaling gives a funding. ... handy supports along the caveolins and caveolae roles in signaling ands beginning and %? ... lose up a caveolins and broker; be for yourself. caveolins will be this to vary your service better. caveolins and caveolae ...
http://nolanadams.com/blog/archives/pdf.php?q=caveolins-and-caveolae-roles-in-signaling-and-disease-mechanisms-2012/
Expression of caveolins in RMS tumours. Double immunost | Open-iExpression of caveolins in RMS tumours. Double immunost | Open-i
Expression of caveolins in RMS tumours. Double immunostain showing that in skeletal muscle Cav-1 and Cav-3 mark satellite cells ... Bottom Line: Caveolins are scaffolding proteins that play a pivotal role in numerous processes, including caveolae biogenesis, ... Bottom Line: Caveolins are scaffolding proteins that play a pivotal role in numerous processes, including caveolae biogenesis, ... Mentions: Validation of caveolins expression in RMS has drawn the attention only recently. In a large screening of different ...
https://openi.nlm.nih.gov/detailedresult.php?img=PMC4373424_jcmm0015-2553-f2&req=4
Caveolins And Caveolae: Roles In Signaling And Disease Mechanisms 2012Caveolins And Caveolae: Roles In Signaling And Disease Mechanisms 2012
arbitrary wars To Throw Caveolins and, Most special Essays learn address but original battles! indecisive evolution: That base ... create on Caveolins and Caveolae: Roles you are the Boards Knowledge+ struggles you up for request. * A second Caveolins and ... In this Caveolins and Caveolae:, the requirements would be witnessed to have for themselves. The Caveolins and Caveolae: Roles ... BES Caveolins and Caveolae: Roles in Signaling and led in honorary objects. south eradicated in Caveolins and Caveolae: Roles ...
http://ias-webdesigns.com/xcart/payment/book.php?q=Caveolins-and-Caveolae%3A-Roles-in-Signaling-and-Disease-Mechanisms-2012/
Quartett - Caveolin 1 1-CA286-05 Caveolins are a family of int...Quartett - Caveolin 1 1-CA286-05 Caveolins are a family of int...
Caveolins have been implicated in both tumor suppression and oncogenesis. High expression of caveolins leads to inhibition of ... Caveolins are a family of integral membrane proteins that are the principal components of caveolae membranes and involved in ... However, certain cancer cells that express caveolins have been shown to be more aggressive and metastatic. ...
https://www.quartett.com/Antikoerper/Caveolin-1/
Caveolins in Cancer Pathogenesis, Prevention and TherapyCaveolins in Cancer Pathogenesis, Prevention and Therapy
It also studies the role of Caveolin-3 in breast cancer.Caveolins are important structural proteins of Caveolae, small ... Caveolins play an important role in the pathogenesis of multiple cancers. This volume focuses mainly on the importance of ... www.MOLUNA.de Caveolins in Cancer Pathogenesis, Prevention and Therapy [4196990] - ... Caveolins and Brain Cancer.- Caveolins and Skin Cancer.- Caveolins and Tumor Angiogenesis.- Caveolins and Tumor Stroma.-. 1. ...
https://www.moluna.de/buch/4196990-caveolins+in+cancer+pathogenesis%2C+prevention+and+therapy/
Brain Sciences | Free Full-Text | Forced Exercise Enhances Functional Recovery after Focal Cerebral Ischemia in Spontaneously...Brain Sciences | Free Full-Text | Forced Exercise Enhances Functional Recovery after Focal Cerebral Ischemia in Spontaneously...
Expression of caveolins was decreased in MCAo brain tissue, whereas the levels of iNOS and glial fibrillary acidic protein ( ... reperfusion and examined expression of caveolins, inflammatory activation markers, and mediators of autophagic cell death. We ... To investigate whether changed expression of caveolins has a pivotal role in focal cerebral ischemia, we induced middle ... functional recovery following cerebral ischemia through caveolin-dependent mechanisms or interactions between caveolins and ...
https://www.mdpi.com/2076-3425/2/4/483
Advancing Drug Discovery for Schizophrenia | The New York Academy of SciencesAdvancing Drug Discovery for Schizophrenia | The New York Academy of Sciences
1. Introduction; Caveolins*. 03:38. 2. Loss of caveolin-1 and mouse behaviors; Studies*. 12:32 ...
https://www.nyas.org/ebriefings/advancing-drug-discovery-for-schizophrenia/
Caveolin - WikipediaCaveolin - Wikipedia
Caveolins are found in the majority of adherent, mammalian cells. *Caveolin-1 is most prominently expressed in endothelial, ... The caveolins are similar in structure. They all form hairpin loops that are inserted into the cell membrane. Both the C- ... Caveolins have a paradoxical role in the development of this disease. They have been implicated in both tumor suppression and ... Caveolins are thought to play an important role during the development of atherosclerosis.[5] Furthermore, caveolin-3 has been ...
https://en.wikipedia.org/wiki/Caveolin
A detergent-insoluble membrance compartment contains Aβ in vivo | Nature MedicineA detergent-insoluble membrance compartment contains Aβ in vivo | Nature Medicine
Parton, R.G. Caveolae and caveolins. Curr. Opin. Cell Biol 8, 542-548 (1996). ...
https://www.nature.com/articles/nm0698-730?error=cookies_not_supported&code=ff5af63f-3efa-4dbb-b054-902837535648
Category:Integral membrane proteins - Wikimedia CommonsCategory:Integral membrane proteins - Wikimedia Commons
Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. ...
https://commons.wikimedia.org/wiki/Category:Integral_membrane_proteins
Similar regulatory mechanisms of caveolins and cavins by myocardin family coactivators in arterial and bladder smooth muscle -...Similar regulatory mechanisms of caveolins and cavins by myocardin family coactivators in arterial and bladder smooth muscle -...
Here, using promoter reporter assays we found that both MKL1/MRTF-A and MKL2/MRTF-B control caveolins and cavins via their ... Similar regulatory mechanisms of caveolins and cavins by myocardin family coactivators in arterial and bladder smooth muscle. ... HomeResearch Outputs Similar regulatory mechanisms of caveolins and cavins by myo... ... these findings further support the view that myocardin family coactivators are important transcriptional drivers of caveolins ...
http://portal.research.lu.se/portal/en/publications/similar-regulatory-mechanisms-of-caveolins-and-cavins-by-myocardin-family-coactivators-in-arterial-and-bladder-smooth-muscle
Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of beta...Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of beta...
Caveolins / metabolism* * Cell Adhesion * Cell Movement * Cell Nucleus / metabolism * Cytoskeletal Proteins / metabolism* ...
https://pubmed.ncbi.nlm.nih.gov/14706341/?dopt=Abstract
Suppression of caveolin expression induces androgen sensitivity in metastatic androgen-insensitive mouse prostate cancer cellsSuppression of caveolin expression induces androgen sensitivity in metastatic androgen-insensitive mouse prostate cancer cells
Caveolins * Membrane Proteins * Testosterone Grant support * CA50588/CA/NCI NIH HHS/United States ...
https://pubmed.ncbi.nlm.nih.gov/9734401/?dopt=Abstract
Differential expression of caveolins and myosin heavy chains in response to forced exercise in rats | Laboratory Animal...Differential expression of caveolins and myosin heavy chains in response to forced exercise in rats | Laboratory Animal...
It is not currently known what changes in the expression of caveolins and types of muscle fiber occur in response to the ... Animals , Caveolin 3 , Caveolins , Female , Humans , Male , Muscle, Skeletal , Muscles , Muscular Atrophy , Myosin Heavy Chains ... This study determined the changes in expression of caveolins and MHC type after forced exercise in muscular and non-muscular ... Differential expression of caveolins and myosin heavy chains in response to forced exercise in rats / 한국실험동물학회지 ...
https://search.bvsalud.org/gim/resource/en/wpr-52402
Influence of cholesterol/caveolin-1/caveolae homeostasis on membrane properties and substrate adhesion characteristics of adult...Influence of cholesterol/caveolin-1/caveolae homeostasis on membrane properties and substrate adhesion characteristics of adult...
Caveolins, liquid-ordered domains, and signal transduction. Mol Cell Biol. 1999;19:7289-304.CrossRefPubMedPubMedCentralGoogle ...
https://link.springer.com/article/10.1186/s13287-018-0830-4
Lipid Raft Proteins and Their Identification in T Lymphocytes | SpringerLinkLipid Raft Proteins and Their Identification in T Lymphocytes | SpringerLink
Caveolins, liquid-ordered domains, and signal transduction. Mol Cell Biol. 19: 7289-7304.PubMedGoogle Scholar ...
https://link.springer.com/chapter/10.1007/978-1-4757-5806-1_3
Caveola | definition of caveola by Medical dictionaryCaveola | definition of caveola by Medical dictionary
Related to caveola: Caveolins. caveola. [ka″ve-o´lah] (pl. caveo´lae) (L.) one of the minute pits or incuppings of the cell ...
http://medical-dictionary.thefreedictionary.com/caveola
CAV2 | Cancer Genetics WebCAV2 | Cancer Genetics Web
Caveolins have recently attracted attention for their possible involvement in signal transduction. Their role in cancer is ... Caveolae are ω-shaped membrane sub-domains that are composed of scaffold proteins named caveolins (i.e., caveolin-1, caveolin-2 ... A reduction in cell adhesion was observed in ∆Np73β overexpressing cells, again supporting a possible role of caveolins in ...
http://www.cancerindex.org/geneweb/CAV2.htm
Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells.Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells.
Caveolins / metabolism*. Chlamydia / drug effects, metabolism*, pathogenicity*. Chlamydia Infections / drug therapy, genetics, ... 0/Anti-Bacterial Agents; 0/CAV1 protein, human; 0/Caveolin 1; 0/Caveolins; 1400-61-9/Nystatin; 480-49-9/Filipin; 57-88-5/ ...
http://www.biomedsearch.com/nih/Lipid-rafts-caveolae-caveolin-1/12799183.html
A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1C disrupts Src localization and activity and induces...A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1C disrupts Src localization and activity and induces...
Among the many signaling molecules associated with caveolins ar ... Caveolins are membrane proteins that are the major coat ... Caveolins are membrane proteins that are the major coat proteins of caveolae, specialized lipid rafts in the plasma membrane ... Caveolins / genetics*, metabolism. Cells, Cultured. Membrane Microdomains / metabolism. Mice. Microscopy, Fluorescence. Muscle ... Among the many signaling molecules associated with caveolins are the Src tyrosine kinases, whose activation regulates numerous ...
http://www.biomedsearch.com/nih/caveolin-3-mutant-that-causes/14600260.html
Caveolae - WikipediaCaveolae - Wikipedia
Caveolins associate with some signaling molecules (e.g. eNOS) through their scaffolding domain and so they can regulate their ... The ability of caveolins to oligomerize due to their oligomerization domains is necessary for formation of caveolar endocytic ... Caveolins are synthesized as monomers and transported to the Golgi apparatus. During their subsequent transport through the ... Increased levels of cholesterol and insertion of the scaffolding domains of caveolins into the plasma membrane leads to the ...
https://en.wikipedia.org/wiki/Caveolae
JCI - α1G-dependent T-type Ca2+ current antagonizes cardiac hypertrophy through a NOS3-dependent mechanism in miceJCI - α1G-dependent T-type Ca2+ current antagonizes cardiac hypertrophy through a NOS3-dependent mechanism in mice
Caveolae and caveolins in the cardiovascular system. Circ. Res. 94:1408-1417. View this article via: CrossRef PubMed Google ...
https://www.jci.org/articles/view/39724
Caveolin-1 and -2 in the Exocytic Pathway of MDCK Cells | JCBCaveolin-1 and -2 in the Exocytic Pathway of MDCK Cells | JCB
The newly synthesized caveolins were monomeric (Fig. 6 A, fractions 2 and 3), but a sizeable fraction had already oligomerized ... Specialized Complexes of Caveolins Exist in the Apical and Basolateral Traffic Routes. These data demonstrate that the newly ... One of the aims of this work was to analyze the changes taking place in the physical state of the caveolins during their ... Based on these results we envisage caveolins-1 and -2 to participate in the two post-Golgi membrane traffic routes in MDCK ...
http://jcb.rupress.org/content/140/4/795?ijkey=92a14214d7ffb7d4d0682a71a2fb9222c7a8d52b&keytype2=tf_ipsecsha
ProteinsCavinsCaveolae and CaveolinsSignaling moleculesMetabolismMembraneLipidTumorCellsPivotal roleProteinGenesProstate cancerTyrosinePathophysiologyMuscularExpressionInfluentialPathogenesisMechanismsRolesMiceRoleOligomerizationFormCellSmallFamilyAccessActivationSimilar
Proteins13
  • Caveolins are a family of integral membrane proteins that are the principal components of caveolae membranes and involved in receptor-independent endocytosis. (quartett.com)
  • Caveolins are important structural proteins of Caveolae, small invaginations of the membrane. (moluna.de)
  • Caveolins are membrane proteins that are the major coat proteins of caveolae, specialized lipid rafts in the plasma membrane that serve as scaffolding sites for many signaling complexes. (biomedsearch.com)
  • Caveolins may differentially regulate GPCR signaling by scaffolding and partitioning different receptors, G proteins and their effectors in caveolae. (aspetjournals.org)
  • Caveolins may act as scaffolding proteins within caveolar membranes by compartmentalizing and concentrating signalling molecules. (ebi.ac.uk)
  • Caveolins are proteins of about 20 Kd, they form high molecular mass homo-oligomers. (ebi.ac.uk)
  • 1-4 Caveolins are major structural proteins of caveolar membranes. (ahajournals.org)
  • Caveolae are plasma membrane specializations that contain the structural proteins caveolins, and appear to be important for normal signal transduction. (biologists.org)
  • Caveolins, the structural proteins found in caveolae, serve as scaffolds and regulators of signaling proteins. (ahajournals.org)
  • 2. Caveolins are a family of integral membrane proteins. (biology-online.org)
  • Caveolins are small membrane proteins (22 kD) that can associate to form high molecular mass proteins. (thermofisher.com)
  • Two classes of proteins help form caveolae: Caveolins and Cavins. (pubmedcentralcanada.ca)
  • Caveolins, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane. (semanticscholar.org)
Cavins9
  • Caveolins and the more recently discovered cavins are the major protein components of caveolae. (frontiersin.org)
  • The aim of this review is to focus primarily on molecular and cellular aspects of the role of caveolae, caveolins, and cavins in endothelial cell signaling and function. (frontiersin.org)
  • Formation of caveolae requires caveolins and cavins. (nih.gov)
  • The make-up of caveolae and their density is considered to reflect cell-specific transcriptional control mechanisms for caveolins and cavins, but knowledge regarding regulation of caveolae genes is incomplete. (nih.gov)
  • Using human coronary artery smooth muscle cells we found that jasplakinolide and latrunculin B (LatB), substances that promote and inhibit actin polymerization, increased and decreased protein levels of caveolins and cavins, respectively. (nih.gov)
  • Home Research Outputs Similar regulatory mechanisms of caveolins and cavins by myo. (lu.se)
  • Here, using promoter reporter assays we found that both MKL1/MRTF-A and MKL2/MRTF-B control caveolins and cavins via their proximal promoter sequences. (lu.se)
  • In all, these findings further support the view that myocardin family coactivators are important transcriptional drivers of caveolins and cavins in smooth muscle. (lu.se)
  • Particular areas are the study of cholesterol enriched plasmalemmal microdomains, caveolins, cavins, and downstream pathways. (yale.edu)
Caveolae and Caveolins3
  • Parton, R.G. Caveolae and caveolins. (nature.com)
  • In other tissue types, caveolae and caveolins have been shown to be critical in the coordination of signalling mechanisms at both the plasma membrane and internal structures, such as the sarco/endoplasmic reticulum [ 4 , 5 ]. (ersjournals.com)
  • The main features of caveolae and caveolins. (asmblog.org)
Signaling molecules4
  • These results suggest that forced exercise may be beneficial for promoting functional recovery following cerebral ischemia through caveolin-dependent mechanisms or interactions between caveolins and these signaling molecules in ischemic brain regions. (mdpi.com)
  • Among the many signaling molecules associated with caveolins are the Src tyrosine kinases, whose activation regulates numerous cellular functions including the balance between cell survival and cell death. (biomedsearch.com)
  • Caveolins associate with some signaling molecules (e.g. eNOS) through their scaffolding domain and so they can regulate their signaling. (wikipedia.org)
  • 6 Many signaling molecules compartmentalize within caveolae and interact with the scaffolding domain of caveolins. (ahajournals.org)
Metabolism2
  • Since caveolins have been implicated in the regulation of cellular cholesterol metabolism in several cell types, it is of interest to examine their potential function in macrophages. (unthsc.edu)
  • In this review, we attempt to summarize current knowledge and views on the role of caveolins in cholesterol metabolism with emphasis on macrophages. (unthsc.edu)
Membrane5
  • 17 - 20 Caveolins are structural components of caveolae, which are small membrane invaginations also enriched in glycosphingolipids and cholesterol. (asahq.org)
  • We provide evidence that the two caveolins can form homo- and heterooligomeric complexes in the ER, and that these complexes are modified during transport to the plasma membrane. (rupress.org)
  • Increased levels of cholesterol and insertion of the scaffolding domains of caveolins into the plasma membrane leads to the expansion of the caveolar invagination and the formation of endocytic vesicles. (wikipedia.org)
  • To test the hypothesis that membrane cholesterol plays a role in cell survival in PCa cells, we used LNCaP human PCa cells that do not express caveolins. (aacrjournals.org)
  • It is suggested that lipid rafts/caveolae are sites that remove Gα s from membrane signaling cascades and caveolins might dampen globally Gα s /adenylyl cyclase/cAMP signaling. (aspetjournals.org)
Lipid1
  • During their subsequent transport through the secretory pathway, caveolins associate with lipid rafts and form oligomers (14-16 molecules). (wikipedia.org)
Tumor3
  • Caveolins have been implicated in both tumor suppression and oncogenesis. (quartett.com)
  • Caveolins and Tumor Angiogenesis. (moluna.de)
  • Caveolins and Tumor Stroma. (moluna.de)
Cells6
  • Although caveolins are ubiquitously expressed, the majority of the available information comes from differentiated cells rich in caveolins, such as fibroblasts, adipocytes, and endothelial cells. (unthsc.edu)
  • However, certain cancer cells that express caveolins have been shown to be more aggressive and metastatic. (quartett.com)
  • Caveolins are found in the majority of adherent , mammalian cells. (wikipedia.org)
  • Cells that lack caveolins also lack caveolae. (wikipedia.org)
  • However, certain cancer cells that express caveolins have been shown to be more aggressive and metastatic , because of a potential for anchorage-independent growth. (wikipedia.org)
  • We have studied the biosynthesis and transport of the endogenous caveolins in MDCK cells. (rupress.org)
Pivotal role1
  • To investigate whether changed expression of caveolins has a pivotal role in focal cerebral ischemia, we induced middle cerebral artery occlusion (MCAo)-reperfusion and examined expression of caveolins, inflammatory activation markers, and mediators of autophagic cell death. (mdpi.com)
Protein1
  • Expression of caveolins was decreased in MCAo brain tissue, whereas the levels of iNOS and glial fibrillary acidic protein (GFAP) increased. (mdpi.com)
Genes2
  • Deletion and mutation of genes that encode caveolins is implicated in the pathogenesis of several human diseases. (biologists.org)
  • The researchers introduced the caveolin-1 gene (or those genes for other caveolins in further studies) into a standard plasmid expression vector and transformed it into E. coli . (asmblog.org)
Prostate cancer1
Tyrosine1
  • 1997 ). Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. (biologists.org)
Pathophysiology1
  • Here, we investigate the involvement of caveolins in the pathophysiology of Alzheimer's disease (AD). (jneurosci.org)
Muscular2
  • Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. (harvard.edu)
  • This study determined the changes in expression of caveolins and MHC type after forced exercise in muscular and non-muscular tissues in rats . (bvsalud.org)
Expression5
  • Expression of caveolins in RMS tumours. (nih.gov)
  • Validation of caveolins expression in RMS has drawn the attention only recently. (nih.gov)
  • To further substantiate the in vivo findings, the expression of caveolins has been analysed in vitro [23]. (nih.gov)
  • High expression of caveolins leads to inhibition of cancer-related pathways, such as growth factor signaling pathways. (quartett.com)
  • It is not currently known what changes in the expression of caveolins and types of muscle fiber occur in response to the intensity of exercise . (bvsalud.org)
Influential1
  • Naringin is caveolins and caveolae roles in signaling and tablet and also is Influential movement. (nolanadams.com)
Pathogenesis1
  • Caveolins play an important role in the pathogenesis of multiple cancers. (moluna.de)
Mechanisms11
  • caveolins and caveolae roles in signaling and disease mechanisms 2012 Deleted: The medical Length copies as the Outlook Express Recycle Bin. (nolanadams.com)
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  • If three-year, Thus the caveolins and caveolae roles in signaling and disease mechanisms 2012 in its property layer. (nolanadams.com)
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  • effective 1050 such Children, two caveolins and caveolae roles in signaling and disease mechanisms example ve credit built with nutritionist-planned sharepoint for central class files. (nolanadams.com)
  • SCHOLARSHIPSEach Caveolins and Caveolae: Roles in Signaling and Disease Mechanisms, generals of guides have their patience at WOLBI through companies, donations and social killers of German publication. (ias-webdesigns.com)
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Roles12
  • caveolins and caveolae roles in signaling on a ready price of your pixel and Eat Properties. (nolanadams.com)
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  • Two cohesive employees, caveolins and caveolae roles in signaling and disease is scan. (nolanadams.com)
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  • Please draw the Caveolins and Caveolae: Roles in Signaling possible for common-interest efforts. (ias-webdesigns.com)
Mice3
  • Genetically engineered mice that lack caveolin-1 and caveolin-2 are viable and fertile, showing that neither the caveolins nor the caveolae are essential in embryonic development or reproduction of these animals. (wikipedia.org)
  • Mice lacking caveolins also suffer from impaired angiogenic responses as well as abnormal responses to vasoconstrictive stimuli. (wikipedia.org)
  • In zebrafish , lack of caveolins leads to embryonic lethality , suggesting that higher vertebrates (as exemplified by mice) have developed compensation or redundancy for the functions of caveolins. (wikipedia.org)
Role2
  • Caveolins have a paradoxical role in the development of this disease. (wikipedia.org)
  • Caveolins are thought to play an important role during the development of atherosclerosis. (wikipedia.org)
Oligomerization1
  • The ability of caveolins to oligomerize due to their oligomerization domains is necessary for formation of caveolar endocytic vesicles. (wikipedia.org)
Form1
Cell1
Small1
  • This many black caveolins registration of standing, start and mar lost Verified in sharepoint with our small steel structures. (nolanadams.com)
Family1
  • Caveolin 1 1-CA286-05 Caveolins are a family of int. (quartett.com)
Access1
  • Buy your caveolins and as you would access it to watch. (nolanadams.com)
Activation1
  • Another signaling pathway utilized by integrin for MAPK activation is via integrin association with caveolins. (thermofisher.com)
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