CD9
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| Location (UCSC) | Chr 12: 6.2 – 6.24 Mb | Chr 6: 125.44 – 125.47 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
CD9 is a gene encoding a protein that is a member of the transmembrane 4 superfamily also known as the
Function
Tetraspanin proteins are involved in a multitude of biological processes such as adhesion, motility, membrane fusion, signaling and protein trafficking.[5][10] Tetraspanins play a role in many biological processes because of their ability to interact with many different proteins including interactions between each other. Their distinct palmitoylation sites allow them to organize on the membrane into tetraspanin-enriched microdomains (TEM).[11][8][10] These TEMs are thought to play a role in many cellular processes including exosome biogenesis.[12] CD9 is commonly used as a marker for exosomes as it is contained on their surface.[11][10][13][14]
However, in some cases CD9 plays a larger role in the ability of exosomes to be more or less pathogenic. Shown in HIV-1 infection, exosomes are able to enhance HIV-1 entry through tetraspanin CD9 and CD81.[15] However, expression of CD9 on the cellular membrane seems to decrease the viral entry of HIV-1.[16][17]
CD9 has a diverse role in cellular processes as it has also been shown to trigger platelet activation and aggregation.
CD9 can also modulate cell adhesion[24] and migration.[25][26] This function makes CD9 of interest when studying cancer and cancer metastasis. However, it seems CD9 has a varying role in different types of cancers. Studies showed that CD9 expression levels have an inverse correlation to metastatic potential or patient survival. The over expression of CD9 was shown to decrease metastasis in certain types of melanoma, breast, lung, pancreas and colon carcinomas.[27][28][29][30][31] However in other studies, CD9 has been shown to increase migration or be highly expressed in metastatic cancers in various cell lines such as lung cancer,[25] scirrhous-type gastric cancer,[26] hepatocellular carcinoma,[32] acute lymphoblastic leukemia,[33] and breast cancer. Suggesting based on the cancer CD9 can be a tumor suppressor or promotor. [34] It has also been suggested that CD9 has an effect on the ability for cancer cells to develop chemoresistance.
Additionally, CD9 has been shown to block adhesion of Staphylococcus aureus to wounds. The adhesion is essential for infection of the wound.[35] This suggests that CD9 could be of possible use to as treatment for skin infection by Staphylococcus aureus.
Interactions
CD9 has been shown to
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000010278 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030342 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ PMID 25278937.
- ^ "CD9 CD9 molecule [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-12-04.
- ^ "CD9 Gene - GeneCards | CD9 Protein | CD9 Antibody". www.genecards.org. Retrieved 2019-12-04.
- ^ PMID 19709882.
- ^ PMID 16537545.
- ^ S2CID 5906694.
- ^ S2CID 28721583.
- PMID 23463506.
- PMID 20138817.
- PMID 27784871.
- PMID 29429034.
- PMID 17015697.
- PMID 20012525.
- PMID 8236164.
- PMID 27403440.
- PMID 10459022.
- PMID 23575678.
- PMID 10634790.
- PMID 17239847.
- PMID 30455686.
- ^ S2CID 46997236.
- ^ PMID 29438363.
- PMID 9472098.
- PMID 8521390.
- PMID 8478605.
- S2CID 19842716.
- S2CID 22410504.
- PMID 29749468.
- PMID 29286918.
- S2CID 32065330.
- PMID 27467693.
- PMID 12036870.
- ^ PMID 8630057.
- PMID 12175627.
- PMID 10741407.
- PMID 10694273.
- PMID 10065872.
- PMID 9804823.
- PMID 11278880.
- PMID 11087758.
- PMID 9360996.
- S2CID 23682577.
- PMID 23613949.
Further reading
- Horejsí V, Vlcek C (August 1991). "Novel structurally distinct family of leucocyte surface glycoproteins including CD9, CD37, CD53 and CD63". FEBS Letters. 288 (1–2): 1–4. S2CID 26316623.
- Berditchevski F (December 2001). "Complexes of tetraspanins with integrins: more than meets the eye". Journal of Cell Science. 114 (Pt 23): 4143–51. PMID 11739647.
- Ninomiya H, Sims PJ (July 1992). "The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the "b"domain of C9". The Journal of Biological Chemistry. 267 (19): 13675–80. PMID 1377690.
- Miyake M, Koyama M, Seno M, Ikeyama S (December 1991). "Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility". The Journal of Experimental Medicine. 174 (6): 1347–54. PMID 1720807.
- Boucheix C, Benoit P, Frachet P, Billard M, Worthington RE, Gagnon J, Uzan G (January 1991). "Molecular cloning of the CD9 antigen. A new family of cell surface proteins". The Journal of Biological Chemistry. 266 (1): 117–22. PMID 1840589.
- Iwamoto R, Senoh H, Okada Y, Uchida T, Mekada E (October 1991). "An antibody that inhibits the binding of diphtheria toxin to cells revealed the association of a 27-kDa membrane protein with the diphtheria toxin receptor". The Journal of Biological Chemistry. 266 (30): 20463–9. PMID 1939101.
- Benoit P, Gross MS, Frachet P, Frézal J, Uzan G, Boucheix C, Nguyen VC (January 1991). "Assignment of the human CD9 gene to chromosome 12 (region P13) by use of human specific DNA probes". Human Genetics. 86 (3): 268–72. S2CID 27178985.
- Lanza F, Wolf D, Fox CF, Kieffer N, Seyer JM, Fried VA, et al. (June 1991). "cDNA cloning and expression of platelet p24/CD9. Evidence for a new family of multiple membrane-spanning proteins". The Journal of Biological Chemistry. 266 (16): 10638–45. PMID 2037603.
- Higashihara M, Takahata K, Yatomi Y, Nakahara K, Kurokawa K (May 1990). "Purification and partial characterization of CD9 antigen of human platelets". FEBS Letters. 264 (2): 270–4. S2CID 42129059.
- Masellis-Smith A, Shaw AR (March 1994). "CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin". Journal of Immunology. 152 (6): 2768–77. S2CID 23491895.
- Chalupny NJ, Kanner SB, Schieven GL, Wee SF, Gilliland LK, Aruffo A, Ledbetter JA (July 1993). "Tyrosine phosphorylation of CD19 in pre-B and mature B cells". The EMBO Journal. 12 (7): 2691–6. PMID 7687539.
- Rubinstein E, Benoit P, Billard M, Plaisance S, Prenant M, Uzan G, Boucheix C (April 1993). "Organization of the human CD9 gene". Genomics. 16 (1): 132–8. PMID 8486348.
- Schmidt C, Künemund V, Wintergerst ES, Schmitz B, Schachner M (January 1996). "CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the alpha 6/beta 1 integrin and the neural adhesion molecule L1". Journal of Neuroscience Research. 43 (1): 12–31. S2CID 84774340.
- Sincock PM, Mayrhofer G, Ashman LK (April 1997). "Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin". The Journal of Histochemistry and Cytochemistry. 45 (4): 515–25. PMID 9111230.
- Rubinstein E, Poindessous-Jazat V, Le Naour F, Billard M, Boucheix C (August 1997). "CD9, but not other tetraspans, associates with the beta1 integrin precursor". European Journal of Immunology. 27 (8): 1919–27. S2CID 42866423.
- Cho, J.H., Kim, E., Son, Y. et al. (2020). CD9 induces cellular senescence and aggravates atherosclerotic plaque formation. Cell Death & Differentiation https://doi.org/10.1038/s41418-020-0537-9
External links
- Human CD9 genome location and CD9 gene details page in the UCSC Genome Browser.