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- Table of Contents
3 Citations 5 Q&As
2 Citations 18 Q&As
1 Citations 16 Q&As
1 Citations 15 Q&As
1 Citations 16 Q&As
Facts about Caveolin-1.
Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3- dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway.
Human | |
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Gene Name: | CAV1 |
Uniprot: | Q03135 |
Entrez: | 857 |
Belongs to: |
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caveolin family |
CAV; CAV1; caveolae protein, 22kD; caveolin 1, caveolae protein, 22kDa; Caveolin1; Caveolin-1; cell growth-inhibiting protein 32; MSTP085; VIP21
Mass (kDA):
20.472 kDA
Human | |
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Location: | 7q31.2 |
Sequence: | 7; NC_000007.14 (116525009..116561185) |
Skeletal muscle, liver, stomach, lung, kidney and heart (at protein level). Expressed in the brain.
Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Membrane raft. Golgi apparatus, trans-Golgi network. Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae.
This boster biomarker has many uses, from identifying epithelioid tumors to helping differentiate epithelioid mesothelioma from lung adenocarcinoma. In this article, we'll explain some of the uses for the CAV1 marker. Fibronectin is a 550kDa glycoprotein that is involved in cell adhesion and increases tumor-associated molecules like FSP-1 and EGF.
Fibronectin is a multifunctional extracellular matrix glycoprotein found in the basal membrane of all cells. It has diverse functions in many biological processes, including cell adhesion, growth, migration, and wound healing. Its cellular form is soluble, but a dimeric form is present at the cell surface, where it is involved in a wide range of processes such as adhesion and migration. Cellular fibronectin is expressed on the surface of platelets after activation.
When a cell experiences an injury, plasma fibronectin clots and replaces the blood clot matrix. In addition, cellular fibronectin interacts with integrins on the cell surface, forming a dense insoluble matrix. Fibronectin fibers branch out between adjacent cells, forming an extracellular matrix. As a result, fibronectin fibers are essential for wound healing and osteoblast mineralization.
Fibronectin is a mammalian glycoprotein with specific binding sites for a number of proteins. It is a major component of blood plasma, and is made by hepatocytes. It has three splicing regions. One of these regions is a Type I repeat that is essential for binding heparin. Type II repeats are found in cellular fibronectin, but only one subunit contains it.
Fibronectin binds pneumococci, a type of bacterium, by binding to its CnBr-activated SEPHAROSE 4B column. In addition, the adsorbed proteins were analyzed by SDS-PAGE using silver stain. The apparent molecular weight of these adsorbed proteins was similar to that of yeast enolase.
The RGD sequence is found in a wide variety of adhesive proteins, including those found in blood and extracellular matrices. Many of these molecules are recognized by integrin receptors, heterodimeric proteins with two membrane-spanning subunits. Some of these receptors recognize particular groups of adhesion proteins, while others recognize all adhesion proteins. The conformation of the RGD sequence may play a crucial role in cell recognition specificity.
The E-cadherin molecule can bind two cells by one of three mechanisms: homophilic or heterophilic binding. Homophilic binding is caused by molecules of the same kind on adjacent cells, while heterophilic binding is mediated by secreted multivalent linker molecules. In most cases, cadherins link cells by a homophilic mechanism. L cells do not express cadherin and are not capable of adhesion.
In vertebrates, there is a large family of extracellular matrix proteins called the Ig-SF. In Drosophila, there are approximately 150 genes encoding Ig-SF proteins, each encoding a protein with one to two Ig domains. Among these genes, one subfamily encodes a protein that may participate in intracellular communication and binding of pathogens. In addition, some of these proteins may also have predicted TM domains.
Previous work on mitotic adhesion has focused on cells dividing on fibronectin. The aVb5-positive reticular adhesion complex has important roles in mitosis. Cells that attach to vitronectin prefer aVb5-positive cells. It is an essential component for mitosis progression. It may also play a role in cell-cycle dynamics.
IL-6, a major cytokine that promotes acute inflammation, is thought to be a key regulator of tumor progression. Activation of the IL-6/STAT3 pathway increases the ability of malignant cells to proliferate. IL-6 also inhibits apoptosis and promotes liver regeneration. Moreover, tumor-associated fibroblasts (NAFs) can secrete a variety of proteins, including TGF-b, PDGF, and Interleukin-6.
This is important for determining the role of the tumor microenvironment and identifying novel strategies for treating cancer by targeting both cancer cells and stromal cells. Furthermore, cancer-associated molecules and cytokines may be better targeted by targeting tumor stromal cells in order to suppress metastasis and improve patient outcomes. The effects of these drugs may be seen at the metastatic site as well as in the primary tumor.
Extra-S100A4 in stromal and tumor cells activates NF-kB. Increasing the phosphorylation of IKK a/b enhances cell migration, and nuclear translocation of intra-S100A4 promotes secretion of the tumor-associated molecules. Further, knockdown of S100A4 inhibits tumor growth. This compound is particularly beneficial in the treatment of digestive system malignancies.
S100 proteins are members of the S100 family, and several have been studied through genomic and functional analyses. The S100A4 protein contains a EF-hand motif that undergoes conformational change in response to calcium. S100A4 has no enzymatic activity, but exerts its biological effects through interactions with target proteins. S100A4 interacts with targets both intracellularly and extracellularly. The intracellular form forms covalent interactions with actins, NMIIIA, and tropomyosin.
The overexpression of S100A4 in cancer cells promotes the growth of metastatic cancers. Increased S100A4 expression is associated with poor prognosis and cancer metastasis in patients. Targeting S100A4 expression might be a novel therapeutic strategy in the treatment of cancer. However, it is not clear whether it will help cancer patients, but it is a promising biomarker.
The diagnosis of mesothelioma can be difficult because the symptoms are vague at first. General practitioners often order tests to rule out other respiratory illnesses. However, only a tumor biopsy can identify epithelioid mesothelioma, which is often delayed by a variety of obstacles.
The p63 and p40 immunohistochemical markers are both positive in lung squamous cell carcinoma. The expression of p63 and p40 is positive in 56.5% of squamous cell carcinomas are p63+. In contrast, p40+ tumors have immunoreactivity.
The epithelioid subtype has distinct features. Epithelial mesothelioma cells have a clumping behavior. They tend to have round or cubed shapes, and they are not mobile. They are also less likely to metastasize. The corresponding diagnosis of lung adenocarcinoma is made by the same criteria.
The immunohistochemical panel for mesothelioma was developed by Brockstedt U in 1996. The panel includes antibodies to the inflammatory proteins BerEP4, IL-6, CD15, and thrombomodulin. These markers can distinguish mesothelioma from lung adenocarcinoma.
AE1/AE3 immunostaining is the gold standard for mesothelium-associated antigens. This marker is commonly associated with non-epithelial histology. For example, MPM is typically devoid of expression of desmoplastic and pan-cytokeratins. Positive stains for these non-mesothelial markers may not be as useful as primary antibodies to mesothelial markers.
Another useful immunohistochemical marker is MUC4 expression. MUC4 expression is present in 50/60 (83%) cases of lung adenocarcinoma and 56 percent of the corresponding cases of lung squamous cell carcinoma. In a study of 60 cases of lung adenocarcinoma, MUC4 expression was negative in 49.7% and 0.6%, respectively. MUC4 is useful in differentiating epithelioid mesothelioma from lung adenocarcinoma and squamous cell carcinoma.
To better understand how this marker works, we first reviewed the literature. Previous studies have shown that CAV1 is a useful marker in the identification of Ewing sarcoma and other PNETs. However, a more rigorous testing of CAV1 alone has not been performed. A combined analysis of the markers would reveal a more robust method for Ewing sarcoma/PNET identification.
Currently, no specialized laboratory can carry out a comprehensive transcriptome-wide screen. However, several genes have been found to be potential specific markers in Ewing sarcoma. Among these, ATP1A1 and GLG1 are associated with high levels of expression. The high expression of ATP1A1 is dependent on the binding of EWSR1-FLI1 to super-enhancers, which can be detected by using reporter assays. Specific immunohistochemical staining detected the presence of ATP1A1 with 96% specificity.
The CAV1 gene is overexpressed in a significant number of cases of Ewing sarcoma. It is also overexpressed in several other tumor types, including DLBCL, MALT lymphoma, and MPNST (malignant peripheral nerve sheath tumor). Moreover, it is not specific to Ewing sarcoma.
Genetic testing has also shown that the CAV1 marker is useful in detecting the presence of PNET. This gene is involved in the fusion of EWS-FLI1 in a variety of tumor types. This gene is also involved in the onset of metastatic Ewing sarcoma. This marker can help differentiate Ewing sarcoma/PNET from other cancer types.
In addition to identifying Ewing sarcoma from other PNETs, the CAV1 gene is used to confirm diagnosis. This gene is present in all types of Ewing sarcoma, including Ewing sarcoma and other PNETs. It is highly useful in confirming the diagnosis of this disease. The CAV1 gene is a common mutation that occurs in Ewing sarcoma and in some types of PNET.
PMID: 1360410 by Glenney J.R. Jr.; The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles.
PMID: 10086342 by Hurlstone A.F., et al. Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines.
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