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- Table of Contents
Facts about CD151 antigen.
Human | |
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Gene Name: | CD151 |
Uniprot: | P48509 |
Entrez: | 977 |
Belongs to: |
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tetraspanin (TM4SF) family |
CD151 antigen (Raph blood group); CD151 antigenplatelet surface glycoprotein gp27; CD151 molecule (Raph blood group); CD151; GP27; Membrane glycoprotein SFA-1; MER2; PETA3; PETA-3; PETA-3SFA-1; platelet-endothelial cell tetraspan antigen 3; Platelet-endothelial tetraspan antigen 3; RAPH; SFA1; SFA-1; tetraspanin-24; TSPAN24; tspan-24; TSPAN24hemidesmosomal tetraspanin CD151
Mass (kDA):
28.295 kDA
Human | |
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Location: | 11p15.5 |
Sequence: | 11; NC_000011.10 (832952..838835) |
Expressed in a variety of tissues including vascular endothelium and epidermis. Expressed on erythroid cells, with a higher level of expression in erythroid precursors than on mature erythrocytes.
Membrane; Multi-pass membrane protein.
If you're interested in evaluating the potential of a new blood test to identify cancer cells, then you've come to the right place. CD151 is a highly specific marker that shows tumor cells to be infiltrated with cytotoxic T-cells. This marker can also help you better understand interactions between cells and their surroundings, as well as cytokine expression.
The CD151 marker is a key component in regulating the PI3K/Akt signal. It recruits a kinase called PI4-kinase, which generates phosphatidylinositol 3,4-bisphosphate, a signal that activates Akt. In HCCLM3 cells, CD151 expression was increased in contrast to the control HCCLM3 cells.
The CD151 marker is an important component of cancer metastasis. It has several important roles in cancer therapy. In addition to tumor growth, it is involved in self-renewal and differentiation. It also participates in DNA damage response and epigenetic mechanisms, as well as anchorage-dependent and -independent tumor cell survival. Therefore, it has a wide range of potential applications. However, it is still not yet fully understood how to use this marker in the clinical setting.
While it is not known how CD151 works in humans, studies have suggested that the protein is involved in the regulation of lung development. For example, anti-CD151 antibodies impair epithelial cell function, which disrupts integrin-mediated adhesion to the basement membrane. This interaction disrupts lung structure and function. But there is still a lot more to learn. To make the most of the CD151 marker, consider the following:
CD151 is a member of the tetraspanin family, which plays multiple roles in various tissues and functions. It supports de novo carcinogenesis in human skin squamous cell carcinoma. It interacts with integrin a3b1 and a6b4. Cysteine, an amino acid, plays a key role in this association. Interestingly, decreasing CD151 association decreases the growth of cancer cells.
Interestingly, exosomal CD151 promotes TNBC cell migration and invasion. Exosomes derived from breast cancer cell lines were also used to test the uptake of CD151 by recipient cells. A significant proportion of recipient cells exhibited a green signal 12 h after the exosomes were added. Moreover, CD151 has the potential to become a diagnostic biomarker in TNBC.
In addition to being a key component in glioma metastasis, CD151 is associated with integrins, which play an important role in tumor progression. Studies have shown that CD151 interacts directly with integrins via palmitoylated cysteine residues. Furthermore, CD151 is linked to integrin alpha3-bet1.
In addition to its potential as a therapeutic target, CD151 also has a significant impact on patient survival. Its ability to identify glioma stem cells has prognostic and therapeutic value. Studies suggest that the expression of CD151-a3b1 in patients with glioblastoma could also predict patient survival. This research further suggests that the CD151-integrin complex may be a valuable tool in glioblastoma treatment.
CD151 regulates the secretion of a large number of proteins through the exosomes. It also has an important role in human papillomavirus infection. It is an important part of basement membrane formation. Therefore, it has many useful uses in the field of cancer immunotherapy. And it is also associated with other inflammatory conditions, such as AIDS and inflammatory diseases. But the best use of this marker is for determining whether a cancer cell has a genetic tendency to develop tumors.
CD81 is a subunit of the B cell co-receptor complex. It is a member of the family of tetraspanins, which play important physiological roles in protein trafficking and other processes. The anti-CD81 antibody recognizes a conformational epitope on CD81 when bound to CD19. Mutations in CD81 inhibit the export activity of CD19.
The interactions of tetraspanins with other proteins are not quite so strong, because they do not contain extracellular ligands. Instead, these proteins associate with intracellular signaling enzymes and proteins through transmembrane domains. However, this theme may extend beyond CD151 to other tetraspanins. The CD151-a3b1 complex displays the strongest association with tetraspanins.
Palmitoylation of tetraspanin proteins occurred in all of them, but CD151 was particularly abundant. In the tetraspanin molecule, the cysteines at the C-terminus are aligned with the proximal cysteines of the intracellular membrane. The C-terminal cysteines of CD63 and CD81 align with those in CD151. Although CD81 also displays palmitoylation, it shows little association with other tetraspanin proteins.
The lack of functional genetic evidence for receptor functions may be the result of scarcity of key antibody reagents. However, tetraspanins have been implicated in the fusion of cell membranes and cell motility. Furthermore, they are important participants in signaling and cell fusion. This study highlights the importance of tetraspanin interactions in Boster Bio. If you are interested in exploring the role of tetraspanins in various diseases, this may be a great starting point.
Molecular interaction studies with human DCs indicate that the tetraspanin CD81 and CD9 interact with each other in the DC. This interaction is likely to be facilitated by the presence of CD9, which is expressed at high levels on DCs. The findings of this study suggest that CD81 and CD9 may interact to produce Th2 lymphocytes. For more details, please refer to the paper: Tetraspanin Interactions in Boster Bio
A detailed crystal structure of the tetraspanin CD81 has been obtained and is the first tetraspanin with a complete structure. The structure shows that the four transmembrane domains of the protein form a cone shaped internal cavity. The molecule in the internal cavity is stabilized by hydrogen bonds to another transmembrane domain. The second extracellular loop sits across the transmembrane cone in a closed conformation.
The biological activity of CD151 is dependent upon its ability to recognize the CD8 and CD9 molecule types. In the laboratory, SCF is commonly used to identify the cytokines CD8 and CD9, while EGFP is often used to detect the presence of other molecules. While SCF is not always accurate, it can provide an excellent cytokine expression level in cultured cells.
The CD40L molecule is a member of the TNF-R family. It was initially identified on B lymphocytes, but is now also expressed on dendritic cells, endothelial cells, and epithelial cells. It is thought to play a role in general immune regulation. Most research involving CD40 has focused on its role in signal transduction. Recent research has focused on CD40/CD40-L interactions.
Exosomes containing antigen-expressing exosomes were evaluated for immunological benefit. Using a DNA vaccine containing the antigen, mice displayed enhanced T cell responses. The tumor cells expressed ovalbumin. Exosomes were purified from cell supernatant after 48 days. Immunoblotting and ELISA were performed to determine protein concentrations in cells and exosomes. The white bars represent the supernatant.
PMID: 7632941 by Fitter S., et al. Molecular cloning of cDNA encoding a novel platelet-endothelial cell tetra-span antigen, PETA-3.
PMID: 8627808 by Hasegawa H., et al. SFA-1, a novel cellular gene induced by human T-cell leukemia virus type 1, is a member of the transmembrane 4 superfamily.