Caveolin 2
Caveolae
Membrane Proteins
Cell Membrane
Membrane Microdomains
Filipin
Detergents
Cell Compartmentation
Cholesterol
beta-Cyclodextrins
Clathrin
Endocytosis
Cells, Cultured
Octoxynol
Cyclodextrins
Signal Transduction
Dogs
Nitric Oxide Synthase Type III
Microscopy, Immunoelectron
Cell Fractionation
3T3 Cells
Golgi Apparatus
Amino Acid Sequence
Molecular Sequence Data
Protein Transport
Annexin A6
Neoplasms, Adipose Tissue
Protein Binding
Adipocytes
Glycosylphosphatidylinositols
Cytoplasmic Vesicles
Sequence Tagged Sites
Dynamins
Biological Transport
Microscopy, Confocal
Nitric Oxide Synthase
Blotting, Western
Recombinant Fusion Proteins
Adenomyosis
Solubility
Endosomes
Transfection
Microscopy, Electron
Centrifugation, Zonal
Muscle Proteins
Glucose Transporter Type 4
Microscopy, Fluorescence
Proto-Oncogene Proteins c-fyn
Fibroblasts
Precipitin Tests
Membrane Lipids
Androstenes
Carrier Proteins
Mice, Knockout
src-Family Kinases
Spodoptera
Fluorescent Antibody Technique
Cholesterol Oxidase
Immunohistochemistry
Cricetinae
Muscular Dystrophies
Phosphorylation
Fluorescent Antibody Technique, Indirect
Subcellular Fractions
Nitric Oxide
Coatomer Protein
Antigens, CD55
Receptor, Nerve Growth Factor
Monosaccharide Transport Proteins
RNA, Messenger
Immunoblotting
Endothelium, Vascular
Clathrin-Coated Vesicles
COS Cells
Intracellular Membranes
G(M1) Ganglioside
Glycosphingolipids
Tissue Distribution
Rats, Sprague-Dawley
Heterotrimeric GTP-Binding Proteins
Brefeldin A
GTP-Binding Protein alpha Subunits, Gi-Go
DNA, Complementary
CHO Cells
Tyrosine-phosphorylated caveolin-1: immunolocalization and molecular characterization. (1/121)
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)Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines. (2/121)
The CA microsatellite repeat marker, D7S522, is located at the center of a approximately 1000 kb smallest common deleted region that is lost in many forms of human cancer. It has been proposed that a putative tumor suppressor gene lies in close proximity to D7S522, within this smallest common deleted region. However, the genes located in proximity to D7S522 have remained elusive. Recently, we identified five independent BAC clones (approximately 100-200 kb) containing D7S522 and the human genes encoding caveolins 1 and 2. Here, we present the detailed organization of the caveolin locus and its relationship to D7S522, as deduced using a shot-gun sequencing approach. We derived two adjacent contigs for a total coverage of approximately 250 kb. Analysis of these contigs reveals that D7S522 is located approximately 67 kb upstream of the caveolin-2 gene and that the caveolin-2 gene is located approximately 19 kb upstream of the caveolin-1 gene, providing for the first time a detailed genetic map of this region. Further sequence analysis reveals many interesting features of the caveolin genes; these include the intron-exon boundaries and several previously unrecognized CA repeats that lie within or in close proximity to the caveolin genes. The first and second exons of both caveolin genes are embedded within CpG islands. These results suggest that regulation of caveolin gene expression may be controlled, in part, by methylation of these CpG regions. In support of this notion, we show here that the CGs in the 5' promoter region of the caveolin-1 gene are functionally methylated in two human breast cancer cell lines (MCF7 and T-47D) that fail to express the caveolin-1 protein. In contrast, the same CGs in cultured normal human mammary epithelial cells (NHMECs) are non-methylated and these cells express high levels of the caveolin-1 protein. Comparison of the human locus with the same locus in the pufferfish Fugu rubripes reveals that the overall organization of the caveolin-1/-2 locus is conserved from pufferfish to man. In conclusion, our current studies provide a systematic basis for diagnostically evaluating the potential deletion, mutation, or methylation of the caveolin genes in a variety of human tumors. (+info)The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo. (3/121)
The mammalian caveolin gene family consists of caveolins-1, -2, and -3. The expression of caveolin-3 is muscle-specific. In contrast, caveolins-1 and -2 are co-expressed, and they form a hetero-oligomeric complex in many cell types, with particularly high levels in adipocytes, endothelial cells, and fibroblasts. These caveolin hetero-oligomers are thought to represent the functional assembly units that drive caveolae formation in vivo. Here, we investigate the mechanism by which caveolins-1 and -2 form hetero-oligomers. We reconstituted this reciprocal interaction in vivo and in vitro using a variety of complementary approaches, including the generation of glutathione S-transferase fusion proteins and synthetic peptides. Taken together, our results indicate that the membrane-spanning domains of both caveolins-1 and -2 play a critical role in mediating their ability to interact with each other. This is the first demonstration that these unusual membrane-spanning regions found in the caveolin family play a specific role in protein-protein interactions. (+info)Vimentin-dependent utilization of LDL-cholesterol in human adrenal tumor cells is not associated with the level of expression of apoE, sterol carrier protein-2, or caveolin. (4/121)
SW-13 adrenal tumor cells that lack detectable intermediate filaments (IF-free) exhibit an impaired capacity to esterify lipoprotein-derived cholesterol compared with cells that contain vimentin filaments. IF-free cells were found to synthesize and secrete significant amounts of apoE, while apoE secretion was nearly undetectable in cell lines that spontaneously express vimentin. However, stable transfectants that express a mouse vimentin cDNA exhibited elevated levels of cholesterol esterification and apoE secretion compared with untransfected IF-free cells, indicating that apoE secretion is not directly related to the capacity of these cells to esterify cholesterol. Some of the cell lines that differed in the level of apoE synthesis and secretion had similar levels of apoE mRNA, suggesting that the differences in expression involve a post-transcriptional mechanism. Treatment of these cells with forskolin and IBMX, 8br-cAMP, or TPA had no effect on apoE secretion. The level of sterol carrier protein-2 (SCP(2)) synthesis and the distribution of SCP(2) between membrane and soluble cellular fractions was not observably different in cells that contained or lacked vimentin. SW-13 cell lines contained little or no detectable caveolin-1 or caveolin-2. These studies demonstrate that the difference in the capacity of these adrenal tumor cells that contain or lack vimentin filaments to esterify low density lipoprotein-cholesterol is not obviously associated with the level of expression or distribution of apoE, SCP(2), or caveolins. (+info)Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1. (5/121)
We have characterized comparatively the subcellular distributions of caveolins-1 and -2, their interactions and their roles in caveolar formation in polarized epithelial cells. In Fischer rat thyroid (FRT) cells, which express low levels of caveolin-2 and no caveolin-1, caveolin-2 localizes exclusively to the Golgi complex but is partially redistributed to the plasma membrane upon co-expression of caveolin-1 by transfection or by adenovirus-mediated transduction. In Madin-Darby canine kidney (MDCK) cells, which constitutively express both caveolin-1 and -2, caveolin-2 localized to both the Golgi complex and to the plasma membrane, where it co-distributed with caveolin-1 in flat patches and in caveolae. In FRT cells, endogenous or overexpressed caveolin-2 did not associate with low density Triton insoluble membranes that floated in sucrose density gradients but was recruited to these membranes when co-expressed together with caveolin-1. In MDCK cells, both caveolin-1 and caveolin-2 associated with low density Triton-insoluble membranes. In FRT cells, transfection of caveolin-1 promoted the assembly of plasma membrane caveolae that localized preferentially (over 99%) to the basolateral surface, like constitutive caveolae of MDCK cells. In contrast, as expected from its intracellular distribution, endogenous or overexpressed caveolin-2 did not promote the assembly of caveolae; rather, it appeared to promote the assembly of intracellular vesicles in the peri-Golgi area. The data reported here demonstrate that caveolin-1 and -2 have different and complementary subcellular localizations and functional properties in polarized epithelial cells and suggest that the two proteins co-operate to carry out specific as yet unknown tasks between the Golgi complex and the cell surface. (+info)Expression of caveolin-1 is required for the transport of caveolin-2 to the plasma membrane. Retention of caveolin-2 at the level of the golgi complex. (6/121)
Caveolins-1 and -2 are normally co-expressed, and they form a hetero-oligomeric complex in many cell types. These caveolin hetero-oligomers are thought to represent the assembly units that drive caveolae formation in vivo. However, the functional significance of the interaction between caveolins-1 and -2 remains unknown. Here, we show that caveolin-1 co-expression is required for the transport of caveolin-2 from the Golgi complex to the plasma membrane. We identified a human erythroleukemic cell line, K562, that expresses caveolin-2 but fails to express detectable levels of caveolin-1. This allowed us to stringently assess the effects of recombinant caveolin-1 expression on the behavior of endogenous caveolin-2. We show that expression of caveolin-1 in K562 cells is sufficient to reconstitute the de novo formation of caveolae in these cells. In addition, recombinant expression of caveolin-1 allows caveolin-2 to form high molecular mass oligomers that are targeted to caveolae-enriched membrane fractions. In striking contrast, in the absence of caveolin-1 expression, caveolin-2 forms low molecular mass oligomers that are retained at the level of the Golgi complex. Interestingly, we also show that expression of caveolin-1 in K562 cells dramatically up-regulates the expression of endogenous caveolin-2. Northern blot analysis reveals that caveolin-2 mRNA levels remain constant under these conditions, suggesting that the expression of caveolin-1 stabilizes the caveolin-2 protein. Conversely, transient expression of caveolin-2 in CHO cells is sufficient to up-regulate endogenous caveolin-1 expression. Thus, the formation of a hetero-oligomeric complex between caveolins-1 and -2 stabilizes the caveolin-2 protein product and allows caveolin-2 to be transported from the Golgi complex to the plasma membrane. (+info)Caveolin-1 inhibits epidermal growth factor-stimulated lamellipod extension and cell migration in metastatic mammary adenocarcinoma cells (MTLn3). Transformation suppressor effects of adenovirus-mediated gene delivery of caveolin-1. (7/121)
Caveolin-1 is a principal component of caveolae membranes that may function as a transformation suppressor. For example, the human caveolin-1 gene is localized to a suspected tumor suppressor locus (D7S522; 7q31.1) that is deleted in human cancers, including mammary carcinomas. However, little is known about the role of caveolins in regulating cell movement, a critical parameter in determining metastatic potential. Here, we examine the role of caveolin-1 in cell movement. For this purpose, we employed an established cellular model, MTLn3, a metastatic rat mammary adenocarcinoma cell line. In this system, epidermal growth factor (EGF) stimulation induces rapid lamellipod extension and cell migration. Interestingly, we find that MTLn3 cells fail to express detectable levels of endogenous caveolin-1. To restore caveolin-1 expression in MTLn3 cells efficiently, we employed an inducible adenoviral gene delivery system to achieve tightly controlled expression of caveolin-1. We show here that caveolin-1 expression in MTLn3 cells inhibits EGF-stimulated lamellipod extension and cell migration and blocks their anchorage-independent growth. Under these conditions, EGF-induced activation of the p42/44 mitogen-activated protein kinase cascade is also blunted. Our results suggest that caveolin-1 expression in motile MTLn3 cells induces a non-motile phenotype. (+info)A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo. (8/121)
Caveolins form interlocking networks on the cytoplasmic face of caveolae. The cytoplasmically directed N and C termini of caveolins are separated by a central hydrophobic segment, which is believed to form a hairpin within the membrane. Here, we report that the caveolin scaffolding domain (CSD, residues 82-101), and the C terminus (residues 135-178) of caveolin-1 are each sufficient to anchor green fluorescent protein (GFP) to membranes in vivo. We also show that the first 16 residues of the C terminus (i.e. residues 135-150) are necessary and sufficient to attach GFP to membranes. When fused to the caveolin-1 C terminus, GFP co-localizes with two trans-Golgi markers and is excluded from caveolae. In contrast, the CSD targets GFP to caveolae, albeit less efficiently than full-length caveolin-1. Thus, caveolin-1 contains at least two membrane attachment signals: the CSD, dictating caveolar localization, and the C terminus, driving trans-Golgi localization. Additionally, we find that caveolin-1 oligomer/oligomer interactions require the distal third of the caveolin-1 C terminus. Thus, the caveolin-1 C-terminal domain has two separate functions: (i) membrane attachment (proximal third) and (ii) protein/protein interactions (distal third). (+info)Here are some possible causes of myoglobinuria:
1. Muscle injury or trauma: This can cause myoglobin to leak into the bloodstream and then into the urine.
2. Muscle disease: Certain muscle diseases, such as muscular dystrophy, can cause myoglobinuria.
3. Kidney damage: Myoglobin can accumulate in the kidneys and cause damage if the kidneys are not functioning properly.
4. Sepsis: Sepsis is a systemic infection that can cause muscle breakdown and myoglobinuria.
5. Burns: Severe burns can cause muscle damage and lead to myoglobinuria.
6. Heart attack: A heart attack can cause muscle damage and myoglobinuria.
7. Rhabdomyolysis: This is a condition where the muscles break down and release myoglobin into the bloodstream. It can be caused by various factors such as medication, infection, or injury.
Symptoms of myoglobinuria may include dark urine, proteinuria (excess protein in the urine), and kidney damage. Treatment depends on the underlying cause and may involve supportive care, medication, or dialysis to remove waste products from the blood.
There are several types of adipocytic neoplasms, including:
1. Lipomas: These are benign, slow-growing tumors that are composed of mature fat cells (adipocytes). They are usually soft to the touch and can be moved easily under the skin.
2. Liposarcomas: These are malignant tumors that also originate in adipose tissue. They can be slow-growing or aggressive and can infiltrate surrounding tissues.
3. Pigmented villonodular synovitis (PVN): This is a type of benign tumor that occurs in the synovial membrane, which lines the joints and tendons. It is composed of adipocytes and other cell types and can cause pain and stiffness in the affected joint.
4. Giant cell lipomatosis: This is a rare condition characterized by multiple small lipomas that are clustered together.
5. Spindle cell lipoma: This is a rare type of lipoma that contains spindle-shaped cells, which are elongated and irregular in shape.
These adipocytic neoplasms can be diagnosed through various imaging techniques such as ultrasonography, computed tomography (CT), magnetic resonance imaging (MRI), and fine needle aspiration biopsy. Treatment options vary depending on the type and location of the tumor, but may include surgical excision, radiation therapy, or chemotherapy.
Adenomyosis can cause symptoms such as heavy menstrual bleeding, painful periods, and pelvic pain. Treatment options for adenomyosis include hysterectomy (removal of the uterus), myomectomy (removal of fibroids), and hormonal therapy.
It is important to note that adenomyosis is different from endometriosis, which is a condition where tissue similar to the lining of the uterus grows outside of the uterus, such as on the ovaries or fallopian tubes.
Adenomyosis is a relatively rare condition and its exact cause is not fully understood. However, it is believed that hormonal factors and/or abnormalities in the development of the uterus during fetal development may play a role.
There are several types of muscular dystrophies, including:
1. Duchenne muscular dystrophy (DMD): This is the most common form of muscular dystrophy, affecting males primarily. It is caused by a mutation in the dystrophin gene and is characterized by progressive muscle weakness, wheelchair dependence, and shortened lifespan.
2. Becker muscular dystrophy (BMD): This is a less severe form of muscular dystrophy than DMD, affecting both males and females. It is caused by a mutation in the dystrophin gene and is characterized by progressive muscle weakness, but with a milder course than DMD.
3. Limb-girdle muscular dystrophy (LGMD): This is a group of disorders that affect the muscles around the shoulders and hips, leading to progressive weakness and degeneration. There are several subtypes of LGMD, each with different symptoms and courses.
4. Facioscapulohumeral muscular dystrophy (FSHD): This is a rare form of muscular dystrophy that affects the muscles of the face, shoulder, and upper arm. It is caused by a mutation in the D4Z4 repeat on chromosome 4.
5. Myotonic dystrophy: This is the most common adult-onset form of muscular dystrophy, affecting both males and females. It is characterized by progressive muscle stiffness, weakness, and wasting, as well as other symptoms such as cataracts, myotonia, and cognitive impairment.
There is currently no cure for muscular dystrophies, but various treatments are available to manage the symptoms and slow the progression of the disease. These include physical therapy, orthotics and assistive devices, medications to manage pain and other symptoms, and in some cases, surgery. Researchers are actively working to develop new treatments and a cure for muscular dystrophies, including gene therapy, stem cell therapy, and small molecule therapies.
It's important to note that muscular dystrophy can be inherited in an autosomal dominant, autosomal recessive, or X-linked manner, depending on the specific type of dystrophy. This means that the risk of inheriting the condition depends on the mode of inheritance and the presence of mutations in specific genes.
In summary, muscular dystrophy is a group of genetic disorders characterized by progressive muscle weakness and degeneration. There are several types of muscular dystrophy, each with different symptoms and courses. While there is currently no cure for muscular dystrophy, various treatments are available to manage the symptoms and slow the progression of the disease. Researchers are actively working to develop new treatments and a cure for muscular dystrophy.
Lipid droplets' functional protein caveolin-2 is associated with lipid metabolism-related molecule FABP5 and EMT marker E...
Expression of caveolin-1 in tooth germ, ameloblastoma and ameloblastic carcinoma. | Med Oral Patol Oral Cir Bucal;26(2): e238...
Cav2 Mouse Gene Details | caveolin 2 | International Mouse Phenotyping Consortium
Right here we show that tyrosine phosphorylation of caveolin-2 (Cav-2) adversely - CFTR cystic fibrosis transmembrane...
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Epithelial membrane protein 2 governs transepithelial migration of neutrophils into the airspace - PubMed
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Identification of molecular classification and gene signature for predicting prognosis and immunotherapy response in HNSCC...
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MedlinePlus: Genes: C
CAV1
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Pharos : Target Details - CAV2
DeCS
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Pharos : Target List
Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission | Journal of Neuroscience
GSE37605 TREG VS TCONV C57BL6 FOXP3 FUSION GFP DN
Find Research outputs - Augusta University Research Profiles
Human Genome Epidemiology Literature Finder|Home|PHGKB
David R. Fulton, M.D. | Harvard Catalyst Profiles | Harvard Catalyst
Jeffrey Haspel - Research output
- Research Profiles at Washington University School of Medicine
WHO EMRO | Serum endostatin and vascular endothelial growth factor levels in patients with pre-eclampsia | Volume 12, issue 1...
WHO EMRO | Serum endostatin and vascular endothelial growth factor levels in patients with pre-eclampsia | Volume 12, issue 1...
Cav22
- Caveolin-1 and Caveolin-2 (CAV1 and CAV2) are proteins associated with intercellular neurotrophic signalling. (umassmed.edu)
- There is converging evidence that CAV1 and CAV2 (CAV1/2) genes have a role in ALS. (umassmed.edu)
Protein7
- The caveolin-1 protein (structural component of membrane caveolae ) plays important roles in several biological functions, such as endocytosis , cell adhesion , and cell signaling . (bvsalud.org)
- Presence of caveolin-1 protein was confirmed by Western blot analysis . (bvsalud.org)
- Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits ,MHC), 2 alkali light chain subunits ,MLC) and 2 regulatory light chain subunits ,MLC2). (morainetownshipdems.org)
- Treatment with METH induced phosphorylation of ERK1/2 and caveolin-1 protein. (nih.gov)
- Caveolin (Cav)-3, the cardiomyocyte-specific caveolar structural protein isoform, is decreased in the diabetic heart. (elsevier.com)
- actin related protein 2/3 compl. (gsea-msigdb.org)
- Lung endothelial monocyte-activating protein 2 is a mediator of cigarette smoke-induced emphysema in mice. (nih.gov)
Caveolae2
CAV16
- Disease-associated variants have been identified within CAV1/2 enhancers, which reduce gene expression and lead to disruption of membrane lipid rafts. (umassmed.edu)
- Using large ALS whole-genome sequencing and post-mortem RNA sequencing datasets (5987 and 365 tissue samples, respectively), and iPSC-derived motor neurons from 55 individuals, we investigated the role of CAV1/2 expression and enhancer variants in the ALS phenotype. (umassmed.edu)
- We also identify increased survival among carriers of CAV1/2 enhancer mutations compared to non-carriers within Project MinE and slower progression as measured by the ALSFRS. (umassmed.edu)
- We propose that carriers of CAV1/2 enhancer mutations may be conceptualised as an ALS subtype who present a less severe ALS phenotype with a longer survival duration and slower progression. (umassmed.edu)
- Upregulation of CAV1/2 genes in ALS cases may indicate a causal pathway or a compensatory mechanism. (umassmed.edu)
- Given prior research supporting the beneficial role of CAV1/2 expression in ALS patients, we consider a compensatory mechanism to better fit the available evidence, although further investigation into the biological pathways associated with CAV1/2 is needed to support this conclusion. (umassmed.edu)
Phosphorylation3
- Right here we show that tyrosine phosphorylation of caveolin-2 (Cav-2) adversely regulates the anti-proliferative function of transforming development factor beta (TGF-beta) in endothelial cells. (morainetownshipdems.org)
- Manifestation amounts and subcellular focusing on of retrovirally re-expressed serine and tyrosine phosphorylation-deficient mutants are much like WT Cav-2 Previously, we've identified that Cav-2 KO MLECs had been more delicate than WT MLECs to anti-proliferative aftereffect of TGF- which retroviral re-expression of WT Cav-2 in Cav-2 KO MLECs led to an identical response to TGF- as with WT MLECs [14]. (morainetownshipdems.org)
- Particularly, we've re-expressed WT-Cav-2, serine residues 23 and 36 phosphorylation-deficient mutant (S23/36A-Cav-2) aswell as tyrosine residues 19 and 27 phosphorylation-deficient mutant (Y19/27F-Cav-2) in Cav-2 KO MLECs. (morainetownshipdems.org)
Isoforms1
- Alternatively spliced transcripts encode alpha and beta isoforms of caveolin 1. (nih.gov)
Tyrosine1
- It interacts with 2 tyrosine kinases: fms-like tyrosine kinase-1, Flt-1 (VEGFR-1), and kinase domain-containing region, Flk-1/KDR (VEGFR-2) [2]. (who.int)
Membrane2
Gene1
- Comprehensive investigation of the caveolin 2 gene: resequencing and association for kidney transplant outcomes. (cdc.gov)
Erk12
- Using HaCaT keratinocytes, knockdown of Dsg2 decreases EGFR expression and abrogates the activation of EGFR, c-Src and Stat3, but not Erk1/2 or Akt, in response to EGF ligand stimulation. (nih.gov)
- Inhibition of ERK1/2 activity or caveolin-1 silencing protected against METH-induced alterations of occludin levels. (nih.gov)
Interacts1
- 9. Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells. (nih.gov)
Integrin1
- integrin subunit beta 2 [Source. (gsea-msigdb.org)
Roles1
- The expression patterns and roles of caveolin-1 in the oral epithelium and in embryonic and odontogenic tumor tissues are still unclear. (bvsalud.org)
Insulin3
- 6. Regulation of insulin response in skeletal muscle cell by caveolin status. (nih.gov)
- 17. Caveolin-1 loss of function accelerates glucose transporter 4 and insulin receptor degradation in 3T3-L1 adipocytes. (nih.gov)
- insulin like growth factor 2 re. (gsea-msigdb.org)
Proteins1
- Caveolin 1 and caveolin 2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. (nih.gov)
Migration1
- Endothelial dysfunction is now regarded as an regulation, vascular smooth cell proliferation, early pivotal event in atherogenesis 2 and has trans endothelial leukocyte migration, been shown to precede development of clinically thrombosis and thrombolytic balance. (who.int)
Chromosome1
- chromosome 2 open reading frame. (gsea-msigdb.org)
Alexa Fluor2
- Cells had been after that incubated sequentially with 0.1% Triton X-100 (v/v) in DPBS for 10 min, DPBS plus 5% goat serum for 30 min, and thereafter with anti-Cav-2 antibody (1:100) in 0.2% BSA for 2 h, washed 3 x, and incubated with Alexa Fluor 488 nm-labeled extra antibody (Invitrogen Corp.) diluted 1:500, accompanied by staining with DAPI (Sigma). (morainetownshipdems.org)
- BT474 breast cancer cell line was stained with 2 µg/mL anti-human CD340/Her-2 Alexa Fluor® 647 and nuclear counterstained with DAPI. (biolegend.com)
Investigation1
- Background: This study involves the investigation of spontaneous and induced secretion of the pro-inflammatory cytokine tumor necrosis factor-α (TNF-α) and the anti-inflammatory chemokine C-C motif chemokine ligand 18 (CCL18) by monocytes isolated from blood of patients with long-term type 2 diabetes mellitus (T2DM), both with or without foot ulcers. (podiatryarena.com)
Mutant1
- 10. A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1C disrupts Src localization and activity and induces apoptosis in skeletal myotubes. (nih.gov)
Occurs in 2 phases1
- Pre-eclampsia occurs in 2 phases: abnormal implantation of the placenta leads to impaired placental blood flow, which then induces the release of a critical placental substance into the maternal circulation. (who.int)
20212
- Med Oral Patol Oral Cir Bucal;26(2): e238-e245, 2021 Mar 01. (bvsalud.org)
- 26(2): e238-e245, 2021 Mar 01. (bvsalud.org)
Endothelial1
- Type I Interferon Activation and Endothelial Dysfunction in Caveolin-1 Insufficiency-associated Pulmonary Arterial Hypertension. (nih.gov)
Pathogenesis1
- GLI pathogenesis related 2 [Sou. (gsea-msigdb.org)
Antibody1
- The antibody solution should be stored undiluted between 2°C and 8°C, and protected from prolonged exposure to light. (biolegend.com)
Role1
- The overexpression of caveolin-1 in AM and AC compared to its expression in normal gingival epithelium ( adult tissue ) suggests a possible role of caveolin-1 in protumoral events, but due to the similar immunoexpression observed in AM and AC, caveolin-1 may not necessarily participate in the malignant transformation process. (bvsalud.org)
Diabetes1
- Of the approximate 30 million Americans that suffer from Type 2 diabetes, 25% will develop a foot ulcer during their lifetime that often exhibit impaired healing with a cost of diagnosis and treatment exceeding $250 billion per year. (podiatryarena.com)
Expression3
- Expression of caveolin-1 in tooth germ, ameloblastoma and ameloblastic carcinoma. (bvsalud.org)
- The expression of caveolin-1 was evaluated in samples of the normal gingival epithelium (n=7), human tooth germ (TG) (n=12), ameloblastoma (AM) (n=83), and ameloblastic carcinoma (AC) (n=9) by immunohistochemistry . (bvsalud.org)
- LY333531 suppressed the decreased expression of myocardial NO, Cav-3, phosphorylated (p)-Akt, and p-eNOS and also mitigated the augmentation of O2 2, nitrotyrosine, Cav-1, and iNOS expression. (elsevier.com)
Human1
- The desmosomal cadherin, desmoglein 2 (Dsg2), is deregulated in a variety of human cancers including those of the skin. (nih.gov)
Association1
- 12. Induction of caveolin during adipogenesis and association of GLUT4 with caveolin-rich vesicles. (nih.gov)
Show1
- The caveolin-1 immunoexpression patterns throughout the stages of TG show its importance during odontogenesis . (bvsalud.org)
Comprehensive1
- Nevertheless, the comprehensive molecular mechanisms of the inhibitory part of Cav-2 in anti-proliferative aftereffect of TGF- in ECs never have been analyzed. (morainetownshipdems.org)
Alpha1
- The proteomics and genomics discovery phases yielded an increase in RANTES (CCL5), CXCL2 (GRO2), and Leucine Rich Alpha-2- glycoprotein in non-healing patients whereas there was an increase in interleukin IL-8, granulocyte colony stimulating factor (G-CSF), colony stimulating factor-2, matrix metalloprotease 7, Alpha-2-HS-glycoprotein, and Kininogen 1 in healing patients. (podiatryarena.com)
Mouse1
- 2011. N-(2-mercaptopropionyl)-glycine but not allopurinol prevented cigarette smoke-induced alveolar enlargement in mouse. (nih.gov)
Critical1
- More than fifty percent of cancer patients, including patients with the most devastating central nervous system malignancy, glioblastoma [ 1 , 2 , 3 ], receive radiation as a critical component of their standard treatment regimen [ 4 ]. (oncotarget.com)
Source1
- carboxylesterase 2 [Source:HGNC. (gsea-msigdb.org)