Basigin
Basigin (BSG) also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or cluster of differentiation 147 (CD147) is a protein that in humans is encoded by the BSG gene.[5][6][7] This protein is a determinant for the Ok blood group system. Basigin has been shown to be an essential receptor on red blood cells for the human malaria parasite, Plasmodium falciparum.[8]
Function
Basigin is a member of the immunoglobulin superfamily, with a structure related to the putative primordial form of the family. As members of the immunoglobulin superfamily play fundamental roles in intercellular recognition involved in various immunologic phenomena, differentiation, and development, basigin is thought also to play a role in intercellular recognition (Miyauchi et al., 1991; Kanekura et al., 1991).[9][10]
It has a variety of functions. In addition to its metalloproteinase-inducing ability, basigin also regulates several distinct functions, such as spermatogenesis, expression of the monocarboxylate transporter and the responsiveness of lymphocytes.[6] Basigin is a type I integral membrane receptor that has many ligands, including the cyclophilin (CyP) proteins Cyp-A and CyP-B and certain integrins.[11][12][13] It is expressed by many cell types, including epithelial cells, endothelial cells and leukocytes. The human basigin protein contains 269 amino acids that form two heavily glycosylated C2 type immunoglobulin-like domains at the N-terminal extracellular portion. A second form of basigin has also been characterized that contains one additional immunoglobulin-like domain in its extracellular portion.[6]
Interactions
Basigin has been shown to interact with Ubiquitin C.[14]
Basigin has been shown to form a complex with monocarboxylate transporters in the retina of mice. Basigin appears to be required for proper placement of MCTs in the membrane. In the Basigin null mouse, the failure of MCTs to integrate with the membrane may be directly linked to a failure of nutrient transfer in the retinal pigmented epithelium (the lactates transported by MCTs 1, 3, and 4 are essential nutrients for the developing RPE), resulting in loss of sight in the null animal.[15]
Role in malaria
It has recently (November 2011) been found that basigin is a receptor that is essential to erythrocyte invasion by most strains of Plasmodium falciparum, the most virulent species of the plasmodium parasites that cause human malaria. It is hoped that by developing antibodies to the parasite ligand for Basigin, Rh5, a better vaccine for malaria might be found.[8] Basigin is bound by the PfRh5 protein on the surface of the malaria parasite.
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000172270 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023175 – 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.
- ^ Kasinrerk W, Fiebiger E, Stefanová I, Baumruker T, Knapp W, Stockinger H (1992). "Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule". J Immunol. 149 (3): 847–54. PMID 1634773.
- ^ a b c Yurchenko V, Constant S, Bukrinsky M (2006). "Dealing with the family: CD147 interactions with cyclophilins". Immunology. 117 (3): 301–9. doi:10.1111/j.1365-2567.2005.02316.x. PMC 1782239. PMID 16476049.
- ^ Miyauchi T, Masuzawa Y, Muramatsu T (1992). "The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen". J. Biochem. 110 (5): 770–4. PMID 1783610.
- ^ a b Crosnier C, Bustamante LY, Bartholdson SJ, Bei AK, Theron M, Uchikawa M, Mboup S, Ndir O, Kwiatkowski DP, Duraisingh MT, Rayner JC, Wright GJ (November 2011). "Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum". Nature. 480 (7378): 534–7. doi:10.1038/nature10606. PMC 3245779. PMID 22080952.
- ^ "Entrez Gene: BSG basigin (Ok blood group)".
- ^ Kanekura T, Chen X, Kanzaki T (2002). "Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts". Int. J. Cancer. 99 (4): 520–8. doi:10.1002/ijc.10390. PMID 11992541.
- ^ Yurchenko V, Zybarth G, O'Connor M, Dai W, Franchin G, Hao T, Guo H, Hung H, Toole B, Gallay P, Sherry B, Bukrinsky M (2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". J Biol Chem. 277 (25): 22959–65. doi:10.1074/jbc.M201593200. PMID 11943775.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Yurchenko V, O'Connor M, Dai W, Guo H, Toole B, Sherry B, Bukrinsky M (2001). "CD147 is a signaling receptor for cyclophilin B". Biochem Biophys Res Commun. 288 (4): 786–8. doi:10.1006/bbrc.2001.5847. PMID 11688976.
- ^ Berditchevski F, Chang S, Bodorova J, Hemler M (1997). "Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6". J Biol Chem. 272 (46): 29174–80. doi:10.1074/jbc.272.46.29174. PMID 9360995.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Wang, Wen-Juan; Li Qing-Quan; Xu Jing-Da; Cao Xi-Xi; Li Hai-Xia; Tang Feng; Chen Qi; Yang Jin-Ming; Xu Zu-De; Liu Xiu-Ping (2008). "Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells". Chemotherapy. 54 (4). Switzerland: 291–301. doi:10.1159/000151225. PMID 18689982.
{{cite journal}}: Cite has empty unknown parameters:|laydate=,|laysource=, and|laysummary=(help) - ^ W.J. Philip; J.D. Ochrietor; C. Rudoy; T. Muramatsu; P.J. Linser (2003). "Loss of MCT1, MCT3, and MCT4 expression in the retinal pigment epithelium and neural retina of the 5A11/basigin-null mouse". Invest.Ophthalmol.Vis.Sci. 44 (3). United States: 1305–1311. doi:10.1167/iovs.02-0552. PMID 12601063.
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Further reading
External links
- Ok blood group system at BGMUT Blood Group Antigen Gene Mutation Database at NCBI, NIH