CD151

Template:PBB CD151 molecule (Raph blood group), also known as CD151 (Cluster of Differentiation 151), is a human gene.^[1]

Function

The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins and other transmembrane 4 superfamily proteins. It is involved in cellular processes including cell adhesion and may regulate integrin trafficking and/or function. This protein enhances cell motility, invasion and metastasis of cancer cells. Multiple alternatively spliced transcript variants that encode the same protein have been described for this gene.^[1]

Interactions

CD151 has been shown to interact with CD46.^[2]

References

^ ^a ^b "Entrez Gene: CD151 CD151 molecule (Raph blood group)".
^ Lozahic S, Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E (March 2000). "CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans". Eur. J. Immunol. 30 (3): 900–7. doi:10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X. PMID 10741407.

Berditchevski F (2002). "Complexes of tetraspanins with integrins: more than meets the eye". J. Cell. Sci. 114 (Pt 23): 4143–51. PMID 11739647.
Ashman LK (2003). "CD151". J. Biol. Regul. Homeost. Agents. 16 (3): 223–6. PMID 12456024.
Ashman LK, Aylett GW, Mehrabani PA, Bendall LJ, Niutta S, Cambareri AC, Cole SR, Berndt MC (1992). "The murine monoclonal antibody, 14A2.H1, identifies a novel platelet surface antigen". Br. J. Haematol. 79 (2): 263–70. doi:10.1111/j.1365-2141.1991.tb04531.x. PMID 1958484.
Fitter S, Tetaz TJ, Berndt MC, Ashman LK (1995). "Molecular cloning of cDNA encoding a novel platelet-endothelial cell tetra-span antigen, PETA-3". Blood. 86 (4): 1348–55. PMID 7632941.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Hasegawa H, Utsunomiya Y, Kishimoto K, Yanagisawa K, Fujita S (1996). "SFA-1, a novel cellular gene induced by human T-cell leukemia virus type 1, is a member of the transmembrane 4 superfamily". J. Virol. 70 (5): 3258–63. PMC 190191. PMID 8627808.
Hasegawa H, Kishimoto K, Yanagisawa K, Terasaki H, Shimadzu M, Fujita S (1997). "Assignment of SFA-1 (PETA-3), a member of the transmembrane 4 superfamily, to human chromosome 11p15.5 by fluorescence in situ hybridization". Genomics. 40 (1): 193–6. doi:10.1006/geno.1996.4563. PMID 9070943.
Sincock PM, Mayrhofer G, Ashman LK (1997). "Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin". J. Histochem. Cytochem. 45 (4): 515–25. doi:10.1177/002215549704500404. PMID 9111230.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Fitter S, Seldin MF, Ashman LK (1998). "Characterisation of the mouse homologue of CD151 (PETA-3/SFA-1); genomic structure, chromosomal localisation and identification of 2 novel splice forms". Biochim. Biophys. Acta. 1398 (1): 75–85. doi:10.1016/S0167-4781(98)00034-7. PMID 9602068.
Sincock PM, Fitter S, Parton RG, Berndt MC, Gamble JR, Ashman LK (1999). "PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function". J. Cell. Sci. 112 ( Pt 6): 833–44. PMID 10036233.
Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E (1999). "Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions". Biochem. J. 340 (1): 103–11. doi:10.1042/0264-6021:3400103. PMC 1220227. PMID 10229664.
Testa JE, Brooks PC, Lin JM, Quigley JP (1999). "Eukaryotic expression cloning with an antimetastatic monoclonal antibody identifies a tetraspanin (PETA-3/CD151) as an effector of human tumor cell migration and metastasis". Cancer Res. 59 (15): 3812–20. PMID 10447000.
Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A (2000). "The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes". J. Cell Biol. 149 (4): 969–82. doi:10.1083/jcb.149.4.969. PMC 2174566. PMID 10811835.
Whittock NV, McLean WH (2001). "Genomic organization, amplification, fine mapping, and intragenic polymorphisms of the human hemidesmosomal tetraspanin CD151 gene". Biochem. Biophys. Res. Commun. 281 (2): 425–30. doi:10.1006/bbrc.2001.4384. PMID 11181065.
Charrin S, Le Naour F, Oualid M, Billard M, Faure G, Hanash SM, Boucheix C, Rubinstein E (2001). "The major CD9 and CD81 molecular partner. Identification and characterization of the complexes". J. Biol. Chem. 276 (17): 14329–37. doi:10.1074/jbc.M011297200. PMID 11278880.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Suzuki Y, Tsunoda T, Sese J, Taira H, Mizushima-Sugano J, Hata H, Ota T, Isogai T, Tanaka T, Nakamura Y, Suyama A, Sakaki Y, Morishita S, Okubo K, Sugano S (2001). "Identification and characterization of the potential promoter regions of 1031 kinds of human genes". Genome Res. 11 (5): 677–84. doi:10.1101/gr.164001. PMC 311086. PMID 11337467.
Kohno M, Hasegawa H, Miyake M, Yamamoto T, Fujita S (2002). "CD151 enhances cell motility and metastasis of cancer cells in the presence of focal adhesion kinase". Int. J. Cancer. 97 (3): 336–43. doi:10.1002/ijc.1605. PMID 11774285.
Zhang XA, Kazarov AR, Yang X, Bontrager AL, Stipp CS, Hemler ME (2002). "Function of the tetraspanin CD151-alpha6beta1 integrin complex during cellular morphogenesis". Mol. Biol. Cell. 13 (1): 1–11. doi:10.1091/mbc.01-10-0481. PMC 65068. PMID 11809818.

External links

Raph blood group system in the BGMUT blood group antigen gene mutation database

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This membrane protein–related article is a stub. You can help Wikipedia by expanding it.

[entrez-1] "Entrez Gene: CD151 CD151 molecule (Raph blood group)".

[pmid10741407-2] Lozahic S, Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E (March 2000). "CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans". Eur. J. Immunol. 30 (3): 900–7. doi:10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X. PMID 10741407.

[1]

[2]

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

v t e Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)
Arrestin	SAG ARRB1 ARRB2 ARR3
Membrane-spanning 4A	MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18
Myelin	Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin-associated glycoprotein Myelin protein zero
Pulmonary surfactant	Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein C
Tetraspanin	TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34
Other/ungrouped	Calnexin LDL-receptor-related protein-associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF
see also other cell membrane protein disorders

CD151

Function

Interactions

See also

References

Further reading

External links